PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 29202233-1 2017 Novel hybrid molecule containing 2-mercaptoethylamine was synthesized starting from O-propyloxime-N-propoxy bacteriopurpurinimide (dipropoxy-BPI), which was readily oxidized in oxygen atmosphere yielding the corresponding disulfide analogue (disulfide-BPI). Cysteamine 33-53 bactericidal permeablility increasing protein Mus musculus 141-144 29202233-1 2017 Novel hybrid molecule containing 2-mercaptoethylamine was synthesized starting from O-propyloxime-N-propoxy bacteriopurpurinimide (dipropoxy-BPI), which was readily oxidized in oxygen atmosphere yielding the corresponding disulfide analogue (disulfide-BPI). Cysteamine 33-53 bactericidal permeablility increasing protein Mus musculus 252-255 28150141-11 2017 Validating the in vivo studies, we demonstrate that treatment of human bronchial epithelial cells (Beas2b cells) with the proteasome inhibitor (MG-132) induces HIF-1alpha expression that is controlled by co-treatment with autophagy-inducing drug, cysteamine. Cysteamine 247-257 hypoxia inducible factor 1 subunit alpha Homo sapiens 160-170 28649022-0 2017 A portable RGB sensing gadget for sensitive detection of Hg2+ using cysteamine-capped QDs as fluorescence probe. Cysteamine 68-78 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 57-60 28649022-6 2017 The detection mechanism was mainly ascribed to the electron transfer from cysteamine capped QDs to Hg2+, resulting in a fluorescence quenching phenomenon. Cysteamine 74-84 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 99-102 28911222-1 2017 Pantetheinase, which catalyzes the cleavage of pantetheine to pantothenic acid (vitamin B5) and cysteamine, is involved in the regulation of oxidative stress, pantothenate recycling and cell migration. Cysteamine 96-106 vanin 1 Homo sapiens 0-13 28751454-3 2017 Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Cysteamine 0-10 vascular endothelial growth factor A Mus musculus 86-120 28982193-4 2017 Cysteamine is a TG2 inhibitor and proteostasis regulator with the potential to restore autophagy. Cysteamine 0-10 transglutaminase 2 Homo sapiens 16-19 28982193-10 2017 Finally, cysteamine decreased TG2, p62, and beclin-1 accumulation in CF, leading to increased Burkholderia uptake into autophagosomes, increased macrophage CFTR expression, and decreased ROS and IL-1beta production. Cysteamine 9-19 transglutaminase 2 Homo sapiens 30-33 28751454-3 2017 Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Cysteamine 0-10 vascular endothelial growth factor A Mus musculus 122-126 28751454-3 2017 Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Cysteamine 0-10 cadherin 5 Mus musculus 163-197 28751454-3 2017 Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Cysteamine 55-65 vascular endothelial growth factor A Mus musculus 86-120 28751454-3 2017 Cysteamine and ethanolamine, the sulfhydryl group-free cysteamine analogue, inhibited vascular endothelial growth factor (VEGF)-induced stress fiber formation and vascular endothelial (VE)-cadherin disruption in endothelial cells, which play a critical role in modulating endothelial permeability. Cysteamine 55-65 vascular endothelial growth factor A Mus musculus 122-126 28751454-5 2017 We then investigated the potential roles of reactive oxygen species (ROS) and transglutaminase (TGase) in the cysteamine prevention of VEGF-induced vascular leakage. Cysteamine 110-120 vascular endothelial growth factor A Mus musculus 135-139 28751454-6 2017 Cysteamine, but not ethanolamine, inhibited VEGF-induced ROS generation in endothelial cells and diabetic retinas. Cysteamine 0-10 vascular endothelial growth factor A Mus musculus 44-48 28751454-7 2017 In contrast, VEGF-induced TGase activation was prevented by both cysteamine and ethanolamine. Cysteamine 65-75 vascular endothelial growth factor A Mus musculus 13-17 28751454-8 2017 Our findings suggest that cysteamine protects against vascular leakage through inhibiting VEGF-induced TGase activation rather than ROS generation in diabetic retinas. Cysteamine 26-36 vascular endothelial growth factor A Mus musculus 90-94 28767736-7 2017 Moreover, CSE-induced aggresome-formation (LC3B-GFP and Ub-RFP co-localization) and autophagy-flux impairment was significantly (p<0.01) mitigated by cysteamine (p<0.05) or fisetin (p<0.05) treatment, indicating the restoration of CSE-mediated autophagy-impairment. Cysteamine 153-163 microtubule associated protein 1 light chain 3 beta Homo sapiens 43-47 28445813-2 2017 The sensor relies on cysteamine capped gold nanoparticles (N-AuNPs) covalently linked with anti-PSMA antibody (Ab) for target specificity. Cysteamine 21-31 folate hydrolase 1 Homo sapiens 96-100 28711572-2 2017 DHL encompasses various histologies of lymphomas where the MYC oncogene and either BCL2 or BCL6 oncogenes are present concomitantly. Cysteamine 0-3 MYC proto-oncogene, bHLH transcription factor Homo sapiens 59-62 28711572-2 2017 DHL encompasses various histologies of lymphomas where the MYC oncogene and either BCL2 or BCL6 oncogenes are present concomitantly. Cysteamine 0-3 BCL2 apoptosis regulator Homo sapiens 83-87 28711572-2 2017 DHL encompasses various histologies of lymphomas where the MYC oncogene and either BCL2 or BCL6 oncogenes are present concomitantly. Cysteamine 0-3 BCL6 transcription repressor Homo sapiens 91-95 28711572-3 2017 Several observational studies and retrospective series have demonstrated that patients with DHL carry a poor prognosis and respond less and for a shorter duration to standard R-CHOP (rituximab, cyclophosphamide, vincristine, adriamycin, and prednisone). Cysteamine 92-95 DNA damage inducible transcript 3 Homo sapiens 177-181 28902888-5 2017 RESULTS: We first evaluated the effect of dendrimer-based cysteamine analogue (PAMAM-DENCYS) on the intrinsic autophagy response in IB3-1 cells and observed a significant reduction in Ub-RFP and LC3-GFP co-localization (aggresome-bodies) by PAMAM-DENCYS treatment as compared to plain dendrimer (PAMAM-DEN) control. Cysteamine 58-68 tripartite motif containing 27 Homo sapiens 187-190 28902888-5 2017 RESULTS: We first evaluated the effect of dendrimer-based cysteamine analogue (PAMAM-DENCYS) on the intrinsic autophagy response in IB3-1 cells and observed a significant reduction in Ub-RFP and LC3-GFP co-localization (aggresome-bodies) by PAMAM-DENCYS treatment as compared to plain dendrimer (PAMAM-DEN) control. Cysteamine 58-68 microtubule associated protein 1 light chain 3 alpha Homo sapiens 195-198 28767736-7 2017 Moreover, CSE-induced aggresome-formation (LC3B-GFP and Ub-RFP co-localization) and autophagy-flux impairment was significantly (p<0.01) mitigated by cysteamine (p<0.05) or fisetin (p<0.05) treatment, indicating the restoration of CSE-mediated autophagy-impairment. Cysteamine 153-163 tripartite motif containing 27 Homo sapiens 59-62 27447111-0 2017 A novel treatment of cystic fibrosis acting on-target: cysteamine plus epigallocatechin gallate for the autophagy-dependent rescue of class II-mutated CFTR. Cysteamine 55-65 CF transmembrane conductance regulator Homo sapiens 151-155 28475457-12 2017 When considered in conjunction with reports of patients with newly diagnosed DHL, which demonstrate lower rates of disease response to R-CHOP compared with intensive front-line therapy, our findings further support the use of intensive front-line therapy for this patient population. Cysteamine 77-80 DNA damage inducible transcript 3 Homo sapiens 137-141 28043364-8 2017 Results showed that protein levels of HGF, GHR, and IGF1R were decreased after 5 months of cysteamine treatment. Cysteamine 91-101 hepatocyte growth factor Ovis aries 38-41 28439920-7 2017 As compared to CDO, ADO is less studied, even though it has a key role in cysteamine metabolism. Cysteamine 74-84 2-aminoethanethiol dioxygenase Homo sapiens 20-23 27876599-2 2017 METHODS: In order to obtain such a hydrophobic mucoadhesive polymer, Eudragit S100 was thiolated by covalent attachment of cysteamine. Cysteamine 124-134 S100 calcium binding protein A1 Homo sapiens 79-83 27245869-5 2017 Cysteamine supplementation also increased the messenger RNA abundance of SLC7A7, SLC7A9 and SLC15A1, occludin, claudin-1 and zonula occludens protein-1 (P < 0.001) in the jejunum mucosa. Cysteamine 0-10 solute carrier family 7 member 7 Sus scrofa 73-79 27245869-5 2017 Cysteamine supplementation also increased the messenger RNA abundance of SLC7A7, SLC7A9 and SLC15A1, occludin, claudin-1 and zonula occludens protein-1 (P < 0.001) in the jejunum mucosa. Cysteamine 0-10 solute carrier family 7 member 9 Sus scrofa 81-87 27245869-5 2017 Cysteamine supplementation also increased the messenger RNA abundance of SLC7A7, SLC7A9 and SLC15A1, occludin, claudin-1 and zonula occludens protein-1 (P < 0.001) in the jejunum mucosa. Cysteamine 0-10 solute carrier family 15 member 1 Sus scrofa 92-99 27245869-5 2017 Cysteamine supplementation also increased the messenger RNA abundance of SLC7A7, SLC7A9 and SLC15A1, occludin, claudin-1 and zonula occludens protein-1 (P < 0.001) in the jejunum mucosa. Cysteamine 0-10 occludin Sus scrofa 101-109 27245869-5 2017 Cysteamine supplementation also increased the messenger RNA abundance of SLC7A7, SLC7A9 and SLC15A1, occludin, claudin-1 and zonula occludens protein-1 (P < 0.001) in the jejunum mucosa. Cysteamine 0-10 claudin 1 Sus scrofa 111-151 27245869-7 2017 Additionally, cysteamine supplementation increased the concentrations of secretory immunoglobulin A (IgA) (P < 0.05), IgM (P < 0.001) and IgG (P < 0.001) in the jejunal mucosa. Cysteamine 14-24 IGHA Sus scrofa 83-105 28316092-6 2017 Mechanistically, GPRC5A regulates NF-kappaB mediated Vanin-1 expression which is the predominant enzyme for cysteamine generation. Cysteamine 108-118 G protein-coupled receptor, family C, group 5, member A Mus musculus 17-23 28316092-6 2017 Mechanistically, GPRC5A regulates NF-kappaB mediated Vanin-1 expression which is the predominant enzyme for cysteamine generation. Cysteamine 108-118 vanin 1 Mus musculus 53-60 28316092-7 2017 Administration of cystamine (the disulfide form of cysteamine) in GPRC5A deficient cell lines inhibited gamma-GCS activity, leading to reduction of GSH level and increase of cell growth. Cysteamine 51-61 G protein-coupled receptor, family C, group 5, member A Mus musculus 66-72 27561233-7 2017 The CS induced acquired-CFTR dysfunction involves CFTR-accumulation in aggresome-bodies that can be rescued by an autophagy-inducing antioxidant drug, cysteamine. Cysteamine 151-161 CF transmembrane conductance regulator Homo sapiens 24-28 27561233-7 2017 The CS induced acquired-CFTR dysfunction involves CFTR-accumulation in aggresome-bodies that can be rescued by an autophagy-inducing antioxidant drug, cysteamine. Cysteamine 151-161 CF transmembrane conductance regulator Homo sapiens 50-54 28043364-8 2017 Results showed that protein levels of HGF, GHR, and IGF1R were decreased after 5 months of cysteamine treatment. Cysteamine 91-101 growth hormone receptor Ovis aries 43-46 28043364-8 2017 Results showed that protein levels of HGF, GHR, and IGF1R were decreased after 5 months of cysteamine treatment. Cysteamine 91-101 insulin-like growth factor 1 receptor Ovis aries 52-57 28061782-5 2017 RESULTS: Three cases of DHL were detected: two with translocations of MYC and BCL2 and one with translocations of MYC and BCL6, all leading to death in less than six months. Cysteamine 24-27 MYC proto-oncogene, bHLH transcription factor Homo sapiens 70-73 28079883-0 2017 Cysteamine re-establishes the clearance of Pseudomonas aeruginosa by macrophages bearing the cystic fibrosis-relevant F508del-CFTR mutation. Cysteamine 0-10 CF transmembrane conductance regulator Homo sapiens 126-130 28061782-5 2017 RESULTS: Three cases of DHL were detected: two with translocations of MYC and BCL2 and one with translocations of MYC and BCL6, all leading to death in less than six months. Cysteamine 24-27 BCL2 apoptosis regulator Homo sapiens 78-82 28061782-5 2017 RESULTS: Three cases of DHL were detected: two with translocations of MYC and BCL2 and one with translocations of MYC and BCL6, all leading to death in less than six months. Cysteamine 24-27 MYC proto-oncogene, bHLH transcription factor Homo sapiens 114-117 28061782-5 2017 RESULTS: Three cases of DHL were detected: two with translocations of MYC and BCL2 and one with translocations of MYC and BCL6, all leading to death in less than six months. Cysteamine 24-27 BCL6 transcription repressor Homo sapiens 122-126 28766546-3 2017 The majority of DHL is represented by s-MYC/BCL2 cases. Cysteamine 16-19 MYC proto-oncogene, bHLH transcription factor Homo sapiens 40-43 28079883-6 2017 We demonstrate that the proteostasis regulator cysteamine, which rescues the function of the most common F508del-CFTR mutant and hence reduces lung inflammation in CF patients, can also repair the defects of CF macrophages, thus restoring both bacterial internalization and clearance through a process that involves upregulation of the pro-autophagic protein Beclin 1 and re-establishment of the autophagic pathway. Cysteamine 47-57 CF transmembrane conductance regulator Homo sapiens 113-117 28079883-6 2017 We demonstrate that the proteostasis regulator cysteamine, which rescues the function of the most common F508del-CFTR mutant and hence reduces lung inflammation in CF patients, can also repair the defects of CF macrophages, thus restoring both bacterial internalization and clearance through a process that involves upregulation of the pro-autophagic protein Beclin 1 and re-establishment of the autophagic pathway. Cysteamine 47-57 beclin 1 Homo sapiens 359-367 28302986-0 2017 SERS Measurement of Cysteamine Molecules Stretched by the Electromagnetophoretic Force. Cysteamine 20-30 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 0-4 28302986-2 2017 The effect of an electromagnetophoretic force for the stretching of cysteamine molecules was examined by using SERS spectrometry. Cysteamine 68-78 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 111-115 28302986-4 2017 Under a constant magnetic field, when an electric current was applied to the conductive medium in the capillary, the shift of SERS bands and the increase of the trans/gauche ratio of cysteamine were observed, suggesting a molecular conformation change of cysteamine due to the stretching force. Cysteamine 255-265 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 126-130 27641479-5 2016 The monoclonal antibody of PSA (anti-PSA) was covalently immobilized on dendrimers which were attached onto the modified Au surface (Au/Cys/Fc-PAMAMs/anti-PSA). Cysteamine 136-139 kallikrein related peptidase 3 Homo sapiens 27-30 27641479-5 2016 The monoclonal antibody of PSA (anti-PSA) was covalently immobilized on dendrimers which were attached onto the modified Au surface (Au/Cys/Fc-PAMAMs/anti-PSA). Cysteamine 136-139 kallikrein related peptidase 3 Homo sapiens 37-40 27641479-5 2016 The monoclonal antibody of PSA (anti-PSA) was covalently immobilized on dendrimers which were attached onto the modified Au surface (Au/Cys/Fc-PAMAMs/anti-PSA). Cysteamine 136-139 kallikrein related peptidase 3 Homo sapiens 37-40 27641479-7 2016 The Au/Cys/FcPAMAM/anti-PSA immunosensor showed excellent performance for PSA at the pulse amplitude; 50mV and the scan rate; 10mV/s in a wide linear concentration range of 0.01ng-100ngmL(-1). Cysteamine 7-10 kallikrein related peptidase 3 Homo sapiens 24-27 27641479-7 2016 The Au/Cys/FcPAMAM/anti-PSA immunosensor showed excellent performance for PSA at the pulse amplitude; 50mV and the scan rate; 10mV/s in a wide linear concentration range of 0.01ng-100ngmL(-1). Cysteamine 7-10 kallikrein related peptidase 3 Homo sapiens 74-77 27372512-0 2016 Cysteamine capped CdS quantum dots as a fluorescence sensor for the determination of copper ion exploiting fluorescence enhancement and long-wave spectral shifts. Cysteamine 0-10 CDP-diacylglycerol synthase 1 Homo sapiens 18-21 27372512-1 2016 We described a turn-on fluorescence sensor for the determination of Cu(2+) ions, utilizing the quantum confinement effect of cadmium sulfide quantum dots capped with cysteamine (Cys-CdS QDs). Cysteamine 166-176 CDP-diacylglycerol synthase 1 Homo sapiens 182-185 26976279-7 2016 Proteostasis regulators such as cysteamine can rescue and stabilize a functional F508del-CFTR protein through suppressing TG2 activation and restoring autophagy in vivo in F508del-CFTR homozygous mice, in vitro in CF patient-derived cell lines, ex vivo in freshly collected primary patient"s nasal cells, as well as in a pilot clinical trial involving homozygous F508del-CFTR patients. Cysteamine 32-42 cystic fibrosis transmembrane conductance regulator Mus musculus 89-93 26976279-7 2016 Proteostasis regulators such as cysteamine can rescue and stabilize a functional F508del-CFTR protein through suppressing TG2 activation and restoring autophagy in vivo in F508del-CFTR homozygous mice, in vitro in CF patient-derived cell lines, ex vivo in freshly collected primary patient"s nasal cells, as well as in a pilot clinical trial involving homozygous F508del-CFTR patients. Cysteamine 32-42 transglutaminase 2, C polypeptide Mus musculus 122-125 26976279-7 2016 Proteostasis regulators such as cysteamine can rescue and stabilize a functional F508del-CFTR protein through suppressing TG2 activation and restoring autophagy in vivo in F508del-CFTR homozygous mice, in vitro in CF patient-derived cell lines, ex vivo in freshly collected primary patient"s nasal cells, as well as in a pilot clinical trial involving homozygous F508del-CFTR patients. Cysteamine 32-42 cystic fibrosis transmembrane conductance regulator Mus musculus 180-184 26976279-7 2016 Proteostasis regulators such as cysteamine can rescue and stabilize a functional F508del-CFTR protein through suppressing TG2 activation and restoring autophagy in vivo in F508del-CFTR homozygous mice, in vitro in CF patient-derived cell lines, ex vivo in freshly collected primary patient"s nasal cells, as well as in a pilot clinical trial involving homozygous F508del-CFTR patients. Cysteamine 32-42 CF transmembrane conductance regulator Homo sapiens 180-184 28766546-3 2017 The majority of DHL is represented by s-MYC/BCL2 cases. Cysteamine 16-19 BCL2 apoptosis regulator Homo sapiens 44-48 28766546-5 2017 The paper describes a case of DHL with concomitant c-MYC and BCL6 gene rearrangements, which mimics diffuse large B-cell lymphoma, leg-type. Cysteamine 30-33 MYC proto-oncogene, bHLH transcription factor Homo sapiens 51-56 28766546-5 2017 The paper describes a case of DHL with concomitant c-MYC and BCL6 gene rearrangements, which mimics diffuse large B-cell lymphoma, leg-type. Cysteamine 30-33 BCL6 transcription repressor Homo sapiens 61-65 27529405-9 2016 To show the utility of this caging group in biomaterial applications, we covalently modified hydrogels with mBhc-protected cysteamine. Cysteamine 123-133 PHD finger protein 21A Mus musculus 108-112 27035618-0 2016 A novel treatment of cystic fibrosis acting on-target: cysteamine plus epigallocatechin gallate for the autophagy-dependent rescue of class II-mutated CFTR. Cysteamine 55-65 CF transmembrane conductance regulator Homo sapiens 151-155 27234323-2 2016 Recent work indicates tissue transglutaminase (TG2) plays a pivotal intracellular role in proteostasis in CF epithelia and that the pan TG inhibitor cysteamine improves CFTR stability. Cysteamine 149-159 transglutaminase 2 Homo sapiens 22-45 27234323-2 2016 Recent work indicates tissue transglutaminase (TG2) plays a pivotal intracellular role in proteostasis in CF epithelia and that the pan TG inhibitor cysteamine improves CFTR stability. Cysteamine 149-159 CF transmembrane conductance regulator Homo sapiens 169-173 27035618-1 2016 We previously reported that the combination of two safe proteostasis regulators, cysteamine and epigallocatechin gallate (EGCG), can be used to improve deficient expression of the cystic fibrosis transmembrane conductance regulator (CFTR) in patients homozygous for the CFTR Phe508del mutation. Cysteamine 81-91 CF transmembrane conductance regulator Homo sapiens 180-231 27035618-1 2016 We previously reported that the combination of two safe proteostasis regulators, cysteamine and epigallocatechin gallate (EGCG), can be used to improve deficient expression of the cystic fibrosis transmembrane conductance regulator (CFTR) in patients homozygous for the CFTR Phe508del mutation. Cysteamine 81-91 CF transmembrane conductance regulator Homo sapiens 233-237 27035618-1 2016 We previously reported that the combination of two safe proteostasis regulators, cysteamine and epigallocatechin gallate (EGCG), can be used to improve deficient expression of the cystic fibrosis transmembrane conductance regulator (CFTR) in patients homozygous for the CFTR Phe508del mutation. Cysteamine 81-91 CF transmembrane conductance regulator Homo sapiens 270-274 27035618-9 2016 Altogether, these results suggest that the combination treatment of cysteamine plus EGCG acts "on-target" because it can only rescue CFTR function when autophagy is functional (in mice) and improves CFTR function when a rescuable protein is expressed (in mice and men). Cysteamine 68-78 cystic fibrosis transmembrane conductance regulator Mus musculus 133-137 27035618-9 2016 Altogether, these results suggest that the combination treatment of cysteamine plus EGCG acts "on-target" because it can only rescue CFTR function when autophagy is functional (in mice) and improves CFTR function when a rescuable protein is expressed (in mice and men). Cysteamine 68-78 cystic fibrosis transmembrane conductance regulator Mus musculus 199-203 27166675-14 2016 These finding suggest that IL-22 and its receptor have a crucial role in the development and pathogenesis of uveitis by facilitating inflammatory cell infiltration, and that cysteamine may be a useful therapeutic drug in treating uveitis by down-regulating IL-22Ralpha expression in RPE. Cysteamine 174-184 interleukin 22 Homo sapiens 27-32 26820360-2 2016 The immunosensor was constructed by immobilizing a monoclonal anti-CA 15-3 antibody on the GO modified cysteamine (Cys) self-assembled monolayer (SAM) on an Au electrode (Au/Cys) through the amide bond formation between the carboxylic acid groups of GO/Py-COOH and amine groups of anti-CA 15-3. Cysteamine 103-113 mucin 1, cell surface associated Homo sapiens 67-74 26820360-2 2016 The immunosensor was constructed by immobilizing a monoclonal anti-CA 15-3 antibody on the GO modified cysteamine (Cys) self-assembled monolayer (SAM) on an Au electrode (Au/Cys) through the amide bond formation between the carboxylic acid groups of GO/Py-COOH and amine groups of anti-CA 15-3. Cysteamine 115-118 mucin 1, cell surface associated Homo sapiens 67-74 26820360-2 2016 The immunosensor was constructed by immobilizing a monoclonal anti-CA 15-3 antibody on the GO modified cysteamine (Cys) self-assembled monolayer (SAM) on an Au electrode (Au/Cys) through the amide bond formation between the carboxylic acid groups of GO/Py-COOH and amine groups of anti-CA 15-3. Cysteamine 115-118 mucin 1, cell surface associated Homo sapiens 286-293 26915455-5 2016 Cystine depletion by cysteamine afforded cytoprotection in CTNS knockdown cells by reducing oxidative stress, normalizing intracellular GSH and ATP content, and preserving cell viability. Cysteamine 21-31 cystinosin, lysosomal cystine transporter Homo sapiens 59-63 26915455-13 2016 Treatment of CTNS knockdown PTECs with the cystine-depleting agent cysteamine resulted in the normalization of OS index, increased GSH and ATP content, and preservation of cell viability. Cysteamine 67-77 cystinosin, lysosomal cystine transporter Homo sapiens 13-17 26449607-5 2016 However, because cysteamine does not correct all complications of cystinosis, including Fanconi syndrome, we hypothesized that cystinosin could have novel roles in addition to transporting cystine out of the lysosome. Cysteamine 17-27 cystinosin, lysosomal cystine transporter Homo sapiens 127-137 26993135-5 2016 This analysis implicated allelic variation within pantetheinase genes (Vnn1 and Vnn3), which we propose impaired the biosynthesis of cysteamine, could affect susceptibility to HIT. Cysteamine 133-143 vanin 1 Mus musculus 71-75 27150250-3 2016 Mice defective in the enzyme pantetheinase (Vnn3) show increased susceptibility to blood-stage malaria (increased parasitaemia, reduced survival), and supplementation of Vnn3 mutants with the reaction product of pantetheinase, cysteamine, corrects in part the malaria-susceptibility phenotype of the mutants. Cysteamine 227-237 vanin 1 Mus musculus 29-42 26743654-4 2016 (1)H NMR spectra suggested that 3-mercaptopropionic acid and 2-aminoethanethiol were successfully introduced into the vinyl-bearing PHA. Cysteamine 61-79 lamin B receptor Homo sapiens 132-135 26993135-5 2016 This analysis implicated allelic variation within pantetheinase genes (Vnn1 and Vnn3), which we propose impaired the biosynthesis of cysteamine, could affect susceptibility to HIT. Cysteamine 133-143 vanin 3 Mus musculus 80-84 26745957-0 2016 Effect of Cysteamine on Mutant ASL Proteins with Cysteine for Arginine Substitutions. Cysteamine 10-20 argininosuccinate lyase Homo sapiens 31-34 26845448-6 2016 Pancreatic ductal adenocarcinoma (PDA) overexpressed VNN1 further aggravates paraneoplastic islet dysfunction; decreases in GSH/PPAR-gamma concentrations and increases in ROS/cysteamine might be primary cause of this effect. Cysteamine 175-185 vanin 1 Homo sapiens 53-57 26745957-2 2016 OBJECTIVES: We investigated the effect of cysteamine on mutant argininosuccinate lyase (ASL), the second most common defect in the urea cycle. Cysteamine 42-52 argininosuccinate lyase Homo sapiens 63-86 26745957-2 2016 OBJECTIVES: We investigated the effect of cysteamine on mutant argininosuccinate lyase (ASL), the second most common defect in the urea cycle. Cysteamine 42-52 argininosuccinate lyase Homo sapiens 88-91 26745957-5 2016 However, incubation of transfected cells with 0.05 mM cysteamine immediately before the enzyme assay resulted in increased ASL activity of p.Arg94Cys, p.Arg379Cys, and p.Arg385Cys by 64, 20, and 197 %, respectively, and this result was significant (p < 0.01). Cysteamine 54-64 argininosuccinate lyase Homo sapiens 123-126 26448193-6 2016 In addition, MYC was more frequently partnered with IGH in SHL than in DHL (P=0.04). Cysteamine 71-74 MYC proto-oncogene, bHLH transcription factor Homo sapiens 13-16 27301206-2 2016 In this study, we used cysteamine-functionalized AuNPs to effectively deliver TGF-beta1 siRNA into hepatoma HepG2 cells in vitro and in vivo. Cysteamine 23-33 transforming growth factor beta 1 Homo sapiens 78-87 26838859-2 2016 In this immunosensor, cysteamine (Cys) and gold nanoparticles (AuNPs) were used to immobilize an anti-hCG monoclonal antibody onto a gold electrode (GE). Cysteamine 22-32 chorionic gonadotropin subunit beta 5 Homo sapiens 102-105 26838859-2 2016 In this immunosensor, cysteamine (Cys) and gold nanoparticles (AuNPs) were used to immobilize an anti-hCG monoclonal antibody onto a gold electrode (GE). Cysteamine 34-37 chorionic gonadotropin subunit beta 5 Homo sapiens 102-105 26700095-4 2016 Anti-CD20 IgG was digested and reduced specifically with beta-mercaptoethylamine to generate the Fab" fragment with two free mercapto groups in its hinge region. Cysteamine 57-80 keratin 20 Homo sapiens 5-9 26834954-2 2016 The most commonly seen DHL is diffuse large B-cell lymphoma (DLBCL) with t(14;18) and t(8;14) or t(8;22) resulting in overexpression of BCL2 and MYC, respectively. Cysteamine 23-26 BCL2 apoptosis regulator Homo sapiens 136-140 26834954-2 2016 The most commonly seen DHL is diffuse large B-cell lymphoma (DLBCL) with t(14;18) and t(8;14) or t(8;22) resulting in overexpression of BCL2 and MYC, respectively. Cysteamine 23-26 MYC proto-oncogene, bHLH transcription factor Homo sapiens 145-148 26700095-4 2016 Anti-CD20 IgG was digested and reduced specifically with beta-mercaptoethylamine to generate the Fab" fragment with two free mercapto groups in its hinge region. Cysteamine 57-80 FA complementation group B Homo sapiens 97-100 26422009-16 2015 Moreover, CS supplementation improved growth performance by increasing plasma IGF-1 concentrations possibly through alterations of mTOR and Akt/FOXO signaling pathways in skeletal muscle of finishing pigs. Cysteamine 10-12 insulin like growth factor 1 Sus scrofa 78-83 26464485-6 2015 Based on these findings, we aimed to study whether cysteamine was able to improve the function of p.R336C CBS variant. Cysteamine 51-61 cystathionine beta-synthase Homo sapiens 106-109 26464485-11 2015 Our results show that cysteamine and MEG are able to specifically improve the function of the CBS p.R336C variant, suggesting that any Arg-to-Cys substitution accessible to these small molecules may be converted back to a moiety resembling Arg. Cysteamine 22-32 cystathionine beta-synthase Homo sapiens 94-97 26422009-10 2015 CS supplementation also increased the concentrations of plasma insulin-like growth factor 1 (IGF-1) (P<0.001), and reduced the concentrations of leptin, SS, and PUN (P<0.001). Cysteamine 0-2 insulin like growth factor 1 Sus scrofa 63-91 26717387-8 2015 Cooccurrence of TP53 and BCL2 aberrations ameliorated the poor prognostic impact of single TP53+ or BCL2+ in MYC positive patients.This pilot study generates evidence for the complex interplay between the alterations of genetic pathways in DLBCL, which goes beyond the concept of DHL. Cysteamine 280-283 tumor protein p53 Homo sapiens 16-20 26717387-8 2015 Cooccurrence of TP53 and BCL2 aberrations ameliorated the poor prognostic impact of single TP53+ or BCL2+ in MYC positive patients.This pilot study generates evidence for the complex interplay between the alterations of genetic pathways in DLBCL, which goes beyond the concept of DHL. Cysteamine 280-283 BCL2 apoptosis regulator Homo sapiens 25-29 26717387-8 2015 Cooccurrence of TP53 and BCL2 aberrations ameliorated the poor prognostic impact of single TP53+ or BCL2+ in MYC positive patients.This pilot study generates evidence for the complex interplay between the alterations of genetic pathways in DLBCL, which goes beyond the concept of DHL. Cysteamine 280-283 tumor protein p53 Homo sapiens 91-95 26717387-8 2015 Cooccurrence of TP53 and BCL2 aberrations ameliorated the poor prognostic impact of single TP53+ or BCL2+ in MYC positive patients.This pilot study generates evidence for the complex interplay between the alterations of genetic pathways in DLBCL, which goes beyond the concept of DHL. Cysteamine 280-283 BCL2 apoptosis regulator Homo sapiens 100-104 26717387-8 2015 Cooccurrence of TP53 and BCL2 aberrations ameliorated the poor prognostic impact of single TP53+ or BCL2+ in MYC positive patients.This pilot study generates evidence for the complex interplay between the alterations of genetic pathways in DLBCL, which goes beyond the concept of DHL. Cysteamine 280-283 MYC proto-oncogene, bHLH transcription factor Homo sapiens 109-112 26422009-10 2015 CS supplementation also increased the concentrations of plasma insulin-like growth factor 1 (IGF-1) (P<0.001), and reduced the concentrations of leptin, SS, and PUN (P<0.001). Cysteamine 0-2 insulin like growth factor 1 Sus scrofa 93-98 26422009-12 2015 Additionally, CS supplementation increased the protein levels for the phosphorylated mammalian target of rapamycin (mTOR), eIF-4E binding protein 1, and ribosomal protein S6 kinase 1 (P<0.001). Cysteamine 14-16 mechanistic target of rapamycin kinase Homo sapiens 85-114 26422009-12 2015 Additionally, CS supplementation increased the protein levels for the phosphorylated mammalian target of rapamycin (mTOR), eIF-4E binding protein 1, and ribosomal protein S6 kinase 1 (P<0.001). Cysteamine 14-16 mechanistic target of rapamycin kinase Homo sapiens 116-120 26422009-12 2015 Additionally, CS supplementation increased the protein levels for the phosphorylated mammalian target of rapamycin (mTOR), eIF-4E binding protein 1, and ribosomal protein S6 kinase 1 (P<0.001). Cysteamine 14-16 eukaryotic translation initiation factor 4E binding protein 1 Homo sapiens 123-147 26422009-16 2015 Moreover, CS supplementation improved growth performance by increasing plasma IGF-1 concentrations possibly through alterations of mTOR and Akt/FOXO signaling pathways in skeletal muscle of finishing pigs. Cysteamine 10-12 mechanistic target of rapamycin kinase Sus scrofa 131-135 26422009-16 2015 Moreover, CS supplementation improved growth performance by increasing plasma IGF-1 concentrations possibly through alterations of mTOR and Akt/FOXO signaling pathways in skeletal muscle of finishing pigs. Cysteamine 10-12 AKT serine/threonine kinase 1 Sus scrofa 140-143 25980731-0 2015 The hen"s egg chorioallantoic membrane (HET-CAM) test to predict the ophthalmic irritation potential of a cysteamine-containing gel: Quantification using Photoshop and ImageJ. Cysteamine 106-116 calmodulin 3 Homo sapiens 44-47 25527033-4 2015 Meanwhile, cysteamine treatment reduced post-SAH elevated the reactive oxygen species level, the concentration of malondialdehyde, 3-nitrotyrosine, and 8-hydroxydeoxyguanosine and increased the glutathione peroxidase enzymatic activity, the concentration of glutathione and brain-derived neurotrophic factor in brain cortex at 48 h after SAH. Cysteamine 11-21 brain-derived neurotrophic factor Rattus norvegicus 274-307 25849043-2 2015 For this purpose, we have synthesized and biologically evaluated a series of Re(I)/(99m)Tc(I) tricarbonyl complexes (Re1-Re4 and Tc1-Tc4, respectively) stabilized by a cysteamine-based (N,S,O) chelator and containing 2-(4"-aminophenyl)benzothiazole pharmacophores. Cysteamine 168-178 transcobalamin 1 Homo sapiens 129-132 25989820-6 2015 The rougher, less passivating coating with cysteamine determined from cyclic voltammetry and scanning electron microscopy led to biosensors that are more sensitive to detect the breast cancer ERBB2 (HER2) biomarker in impedance spectroscopy measurements. Cysteamine 43-53 erb-b2 receptor tyrosine kinase 2 Homo sapiens 192-197 25989820-6 2015 The rougher, less passivating coating with cysteamine determined from cyclic voltammetry and scanning electron microscopy led to biosensors that are more sensitive to detect the breast cancer ERBB2 (HER2) biomarker in impedance spectroscopy measurements. Cysteamine 43-53 erb-b2 receptor tyrosine kinase 2 Homo sapiens 199-203 26549544-8 2015 The availability of free cysteamine is also regulated by hydrolysis of pantetheine by pantetheinase. Cysteamine 25-35 vanin 1 Mus musculus 86-99 25549939-9 2015 In rats, cysteamine administration induces glutathione depletion and AIF translocation leading to apoptosis of duodenal epithelium. Cysteamine 9-19 apoptosis inducing factor, mitochondria associated 1 Rattus norvegicus 69-72 24499020-2 2015 The best percentages of CASA motilities were achieved with 10 mg ml(-1) of fetuin and 2.5 mm of cysteamine. Cysteamine 96-106 casein alpha s1 Homo sapiens 24-28 26549544-11 2015 The use of Vnn1 knockout mice has provided clear evidence that Vnn1 modulates redox and immune pathways In vivo, both of which appear at least partially due to a loss of cysteamine/cystamine. Cysteamine 170-180 vanin 1 Mus musculus 63-67 26549544-13 2015 Cysteamine treatment has been used clinically as an antidote to APAP poisoning and in animal models against hepatotoxicants including APAP, galactosamine and CCl4. Cysteamine 0-10 chemokine (C-C motif) ligand 4 Mus musculus 158-162 25561924-0 2015 Effect of Cysteamine on Cell Growth and IgG4 Production in Recombinant Sp2.0 Cells. Cysteamine 10-20 Sp2 transcription factor Mus musculus 71-74 25110008-1 2014 Pantetheinase is an ubiquitous enzyme which hydrolyses D-pantetheine into cysteamine and pantothenate (vitamin B5) on the dissimilative pathway of CoA. Cysteamine 74-84 vanin 1 Mus musculus 0-13 24679006-6 2015 Our findings indicate a significant difference between these two types of DHL at a molecular level with pathogenetic implications, as arguably, TP53 mutations inhibiting p53 mediated promotion of apoptosis pose a synergistic advantage in clonal evolution of cells with malignantly enforced overexpression of BCL2. Cysteamine 74-77 tumor protein p53 Homo sapiens 144-148 24679006-6 2015 Our findings indicate a significant difference between these two types of DHL at a molecular level with pathogenetic implications, as arguably, TP53 mutations inhibiting p53 mediated promotion of apoptosis pose a synergistic advantage in clonal evolution of cells with malignantly enforced overexpression of BCL2. Cysteamine 74-77 tumor protein p53 Homo sapiens 170-173 24679006-6 2015 Our findings indicate a significant difference between these two types of DHL at a molecular level with pathogenetic implications, as arguably, TP53 mutations inhibiting p53 mediated promotion of apoptosis pose a synergistic advantage in clonal evolution of cells with malignantly enforced overexpression of BCL2. Cysteamine 74-77 BCL2 apoptosis regulator Homo sapiens 308-312 26824820-5 2015 MYC rearrangement was observed in 11 (48%) out of 23 patients: single-hit lymphoma in 3 patients and DHL in 8 (BCL2+/MYC+ in 6 cases and BCL6+/MYC+ in 2). Cysteamine 101-104 MYC proto-oncogene, bHLH transcription factor Homo sapiens 0-3 26824820-7 2015 The DHL group showed a correlation between the rearrangement of the BCL2+/MYC+ genes and the expression of MYC and BCL2 proteins in 5 out of 6 patients. Cysteamine 4-7 BCL2 apoptosis regulator Homo sapiens 68-72 26824820-7 2015 The DHL group showed a correlation between the rearrangement of the BCL2+/MYC+ genes and the expression of MYC and BCL2 proteins in 5 out of 6 patients. Cysteamine 4-7 MYC proto-oncogene, bHLH transcription factor Homo sapiens 74-77 26824820-7 2015 The DHL group showed a correlation between the rearrangement of the BCL2+/MYC+ genes and the expression of MYC and BCL2 proteins in 5 out of 6 patients. Cysteamine 4-7 MYC proto-oncogene, bHLH transcription factor Homo sapiens 107-110 26824820-7 2015 The DHL group showed a correlation between the rearrangement of the BCL2+/MYC+ genes and the expression of MYC and BCL2 proteins in 5 out of 6 patients. Cysteamine 4-7 BCL2 apoptosis regulator Homo sapiens 115-119 25052781-0 2014 Cysteamine, a pro-BDNF drug, as an adjunctive treatment for schizophrenia. Cysteamine 0-10 brain derived neurotrophic factor Homo sapiens 18-22 25478849-1 2014 Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B5) and cysteamine, a strong reducing agent. Cysteamine 218-228 vanin 1 Homo sapiens 41-48 25478849-1 2014 Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B5) and cysteamine, a strong reducing agent. Cysteamine 218-228 vanin 1 Homo sapiens 64-77 25110008-4 2014 We document the involvement of the Vnn1 pantetheinase in situations of increased tissue needs and propose that Vnn1 through recycling of pantothenate and release of cysteamine in tissues participates in the adaptive response of the tissue to stress. Cysteamine 165-175 vanin 1 Mus musculus 111-115 24873476-1 2014 We introduce a versatile ABC triblock terpoly- mer platform based on poly(ethylene oxide)-block-poly(allyl glycidyl ether)-block-poly(tert-butyl glycidyl ether) (PEO-b-PAGE-b-PtBGE) and subsequent functionalization of the PAGE segment with thiogalactose (hydroxyl), cysteamine (amino), and 2-mercaptopropionic acid (carboxy) by thiol-ene chemistry. Cysteamine 266-276 ATP binding cassette subfamily B member 6 (Langereis blood group) Homo sapiens 25-28 24712878-3 2014 Vanin-1 is endowed with pantetheinase activity, releasing cysteamine in tissues and regulating cell response to oxidative stress by modulating the production of glutathione. Cysteamine 58-68 vanin 1 Mus musculus 0-7 24712878-6 2014 This effect could be reversed by treatment of Sf-1 transgenic/Vnn1 null mice with cysteamine. Cysteamine 82-92 vanin 1 Mus musculus 62-66 24728046-3 2014 By regulating the composition of the precursors (AgNO3 and sulfur-N2H4 H2O complex) and multidentate polymers (poly(acrylic acid)-graft-cysteamine-graft-ethylenediamine), as well as the reaction time, Ag2S QDs (2.6-3.7 nm) are prepared, displaying tunable photoluminescence (PL) emission from red to the second near-infrared region (687-1096 nm). Cysteamine 136-146 angiotensin II receptor type 1 Homo sapiens 201-205 24234731-4 2014 DHL is group accompanied by IGH-BCL2 and MYC rearrangement, behaving highly aggressively, with a complex and distinct karyotype which can not be extrapolated solely by morphological pathological assessment, since it has not been entirely characteristic. Cysteamine 0-3 immunoglobulin heavy locus Homo sapiens 28-31 24234731-4 2014 DHL is group accompanied by IGH-BCL2 and MYC rearrangement, behaving highly aggressively, with a complex and distinct karyotype which can not be extrapolated solely by morphological pathological assessment, since it has not been entirely characteristic. Cysteamine 0-3 BCL2 apoptosis regulator Homo sapiens 32-36 24234731-4 2014 DHL is group accompanied by IGH-BCL2 and MYC rearrangement, behaving highly aggressively, with a complex and distinct karyotype which can not be extrapolated solely by morphological pathological assessment, since it has not been entirely characteristic. Cysteamine 0-3 MYC proto-oncogene, bHLH transcription factor Homo sapiens 41-44 24440420-3 2014 PEG-PAA-PDEA (1.9-0.8-8.2kgmol(-1)) was synthesized by controlled reversible addition-fragmentation chain transfer polymerization and further modified with cysteamine to yield the thiol-containing PEG-PAA(SH)-PDEA copolymer. Cysteamine 156-166 phosphodiesterase 6A Homo sapiens 8-12 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 Bcl2-like 1 Rattus norvegicus 216-222 24440466-0 2014 A new gel formulation of topical cysteamine for the treatment of corneal cystine crystals in cystinosis: the Cystadrops OCT-1 study. Cysteamine 33-43 solute carrier family 22 member 1 Homo sapiens 120-125 24385009-2 2014 In this study, we hypothesized that STAT3 signaling is activated and provides a critical protective role that is required for enterocyte survival during the early phases of cysteamine-induced duodenal ulcers. Cysteamine 173-183 signal transducer and activator of transcription 3 Rattus norvegicus 36-41 24385009-3 2014 METHODS: We studied the effect of inhibition of STAT3 activity on cysteamine-induced duodenal ulcers in rats and egr-1 knockout mice using STAT3/DNA binding assay, immunohistochemistry, immunoblot, and quantitative reverse transcriptase PCR analyses. Cysteamine 66-76 signal transducer and activator of transcription 3 Rattus norvegicus 48-53 24528841-3 2014 Anti-HER-3 antibody was covalently attached to cysteamine by glutaraldehyde and used as a bioreceptor in a biosensor system for the first time by this study. Cysteamine 47-57 erb-b2 receptor tyrosine kinase 3 Homo sapiens 5-10 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 apurinic/apyrimidinic endodeoxyribonuclease 1 Rattus norvegicus 224-229 24385009-4 2014 RESULTS: We found that G-quartet oligodeoxynucleotides T40214, a specific inhibitor of STAT3/DNA binding, aggravated cysteamine-induced duodenal ulcers in rats 2.8-fold (p < 0.05). Cysteamine 117-127 signal transducer and activator of transcription 3 Rattus norvegicus 87-92 24385009-5 2014 In the pre-ulcerogenic stage, cysteamine induced STAT3 tyrosine phosphorylation, its translocation to nuclei, an increased expression and nuclear translocation of importin alpha and beta in the rat duodenal mucosa. Cysteamine 30-40 signal transducer and activator of transcription 3 Rattus norvegicus 49-54 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 signal transducer and activator of transcription 3 Rattus norvegicus 35-40 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 signal transducer and activator of transcription 3 Rattus norvegicus 183-188 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 signal transducer and activator of transcription 3 Rattus norvegicus 183-188 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 vascular endothelial growth factor A Rattus norvegicus 210-214 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 0-10 suppressor of cytokine signaling 3 Rattus norvegicus 271-305 24385009-6 2014 Cysteamine enhanced the binding of STAT3 to its DNA consensus sequences at 6, 12, and 24 h after cysteamine by 1.5-, 1.8-, and 3.5-fold, respectively, and activated the expression of STAT3 target genes such as VEGF, Bcl-xL, Ref-1, and STAT3-induced feedback inhibitor, a suppressor of cytokine signaling 3. Cysteamine 97-107 signal transducer and activator of transcription 3 Rattus norvegicus 35-40 24385009-7 2014 We also demonstrated that egr-1 knockout mice, which are more susceptible to cysteamine-induced duodenal ulcers, had lower levels of STAT3 expression, its phosphorylation, expression of importin alpha or beta, and STAT3/DNA binding than wild-type mice in response to cysteamine. Cysteamine 77-87 early growth response 1 Mus musculus 26-31 24385009-7 2014 We also demonstrated that egr-1 knockout mice, which are more susceptible to cysteamine-induced duodenal ulcers, had lower levels of STAT3 expression, its phosphorylation, expression of importin alpha or beta, and STAT3/DNA binding than wild-type mice in response to cysteamine. Cysteamine 267-277 early growth response 1 Mus musculus 26-31 25350163-5 2014 Cysteamine was also able to increase the plasma membrane expression of the F508del-CFTR protein in nasal epithelial cells from F508del homozygous CF patients, and these effects persisted for 24 h after cysteamine withdrawal. Cysteamine 0-10 CF transmembrane conductance regulator Homo sapiens 83-87 24090870-0 2014 Design of a multiwalled carbon nanotube-Nafion-cysteamine modified tyrosinase biosensor and its adaptation of dopamine determination. Cysteamine 47-57 tyrosinase Homo sapiens 67-77 25350163-5 2014 Cysteamine was also able to increase the plasma membrane expression of the F508del-CFTR protein in nasal epithelial cells from F508del homozygous CF patients, and these effects persisted for 24 h after cysteamine withdrawal. Cysteamine 202-212 CF transmembrane conductance regulator Homo sapiens 83-87 25350163-4 2014 Here, we report that oral treatment with cysteamine greatly reduces the mortality rate and improves the phenotype of newborn mice bearing the F508del-CFTR mutation. Cysteamine 41-51 cystic fibrosis transmembrane conductance regulator Mus musculus 150-154 25350163-8 2014 Altogether, these results suggest that optimal schedules of cysteamine plus EGCG might be used for the treatment of CF caused by the F508del-CFTR mutation. Cysteamine 60-70 CF transmembrane conductance regulator Homo sapiens 141-145 24054673-0 2013 Selective turn-on fluorescence sensor for Ag+ using cysteamine capped CdS quantum dots: determination of free Ag+ in silver nanoparticles solution. Cysteamine 52-62 CDP-diacylglycerol synthase 1 Homo sapiens 70-73 24009239-7 2014 Furthermore, treatment with cysteamine reduced alpha-smooth muscle actin-positive interstitial myofibroblast proliferation and mRNA levels of extracellular matrix proteins in mice and attenuated myofibroblast differentiation and proliferation in vitro, but did not augment TGF-beta signaling. Cysteamine 28-38 transforming growth factor, beta 1 Mus musculus 273-281 24009239-9 2014 Taken together, these data suggest previously unrecognized antifibrotic actions of cysteamine via TGF-beta-independent mechanisms that include oxidative stress reduction and attenuation of the myofibroblast response to kidney injury and support further investigation into the potential benefit of cysteamine therapy in the treatment of CKD. Cysteamine 83-93 transforming growth factor beta 1 Homo sapiens 98-106 24222112-4 2013 MATERIALS AND METHODS: In the present study, we evaluated the mutational status of ID3 in 37 cases of DHL and 16 cases of sporadic Burkitt lymphoma in order to identify a possible association of this new found hallmark with the rare and insufficiently-defined entity of DHL, seeking to broaden the understanding of these lymphomas at a molecular level. Cysteamine 102-105 inhibitor of DNA binding 3, HLH protein Homo sapiens 83-86 24222112-4 2013 MATERIALS AND METHODS: In the present study, we evaluated the mutational status of ID3 in 37 cases of DHL and 16 cases of sporadic Burkitt lymphoma in order to identify a possible association of this new found hallmark with the rare and insufficiently-defined entity of DHL, seeking to broaden the understanding of these lymphomas at a molecular level. Cysteamine 270-273 inhibitor of DNA binding 3, HLH protein Homo sapiens 83-86 24222112-5 2013 RESULTS: We identified ID3 mutations in lymphomas with chromosomal aberrations at cMYC and either BCL2 or BCL6 at a frequency intermediate between that of DLBCL and Burkitt lymphoma, hinting at a common pathway in lymphomagenesis for a subset of patients with DHL. Cysteamine 260-263 inhibitor of DNA binding 3, HLH protein Homo sapiens 23-26 24054673-1 2013 Cadmium sulfide quantum dots capped with cysteamine (Cys-CdS QDs) were demonstrated as a selective fluorescence probe for sensing of free trace silver ions. Cysteamine 41-51 CDP-diacylglycerol synthase 1 Homo sapiens 57-60 25427467-2 2013 Glucose oxidase (GOx) was used as a model enzyme and was immobilized onto the gold surface forming a self assembled monolayer via FcSH and cysteamine. Cysteamine 139-149 hydroxyacid oxidase 1 Homo sapiens 0-15 23800975-3 2013 Restoring defective autophagy in CF airways by proteostasis regulators (such as cystamine and its reduced form, cysteamine) can rescue and stabilize DeltaF508-CFTR at the PM, thus enabling the action of CFTR potentiators, which are pharmacological agents that stimulate the function of CFTR as an ion channel. Cysteamine 112-122 CF transmembrane conductance regulator Homo sapiens 159-163 23800975-3 2013 Restoring defective autophagy in CF airways by proteostasis regulators (such as cystamine and its reduced form, cysteamine) can rescue and stabilize DeltaF508-CFTR at the PM, thus enabling the action of CFTR potentiators, which are pharmacological agents that stimulate the function of CFTR as an ion channel. Cysteamine 112-122 CF transmembrane conductance regulator Homo sapiens 203-207 23800975-3 2013 Restoring defective autophagy in CF airways by proteostasis regulators (such as cystamine and its reduced form, cysteamine) can rescue and stabilize DeltaF508-CFTR at the PM, thus enabling the action of CFTR potentiators, which are pharmacological agents that stimulate the function of CFTR as an ion channel. Cysteamine 112-122 CF transmembrane conductance regulator Homo sapiens 203-207 23800975-8 2013 These results provide the rationale for a combination therapy of CF in which pretreatment with cystamine or cysteamine enables the later action of CFTR potentiators. Cysteamine 108-118 CF transmembrane conductance regulator Homo sapiens 147-151 23511333-6 2013 Among sulfhydryl reagents, cysteamine and reduced glutathione (GSH), but not oxidized glutathione (GSSG) up to 1mM, inhibited PCMB-unmasked 125I-SI Ang II binding in brain and testis. Cysteamine 27-37 angiotensinogen Rattus norvegicus 148-154 23341189-2 2013 Previous reports suggest that decreased CD20 and/or CD19 expression by flow cytometry is relatively common in DHL and may help to identify cases requiring additional cytogenetic analysis. Cysteamine 110-113 keratin 20 Homo sapiens 40-44 23341189-2 2013 Previous reports suggest that decreased CD20 and/or CD19 expression by flow cytometry is relatively common in DHL and may help to identify cases requiring additional cytogenetic analysis. Cysteamine 110-113 CD19 molecule Homo sapiens 52-56 23978960-4 2013 Recent studies using mice lacking the vanin-1 gene (pantetheinase gene) suggest that pantetheinase is actively involved in the progression of inflammatory reactions by generating cysteamine. Cysteamine 179-189 vanin 1 Mus musculus 38-45 23978960-4 2013 Recent studies using mice lacking the vanin-1 gene (pantetheinase gene) suggest that pantetheinase is actively involved in the progression of inflammatory reactions by generating cysteamine. Cysteamine 179-189 vanin 1 Mus musculus 52-65 23978960-4 2013 Recent studies using mice lacking the vanin-1 gene (pantetheinase gene) suggest that pantetheinase is actively involved in the progression of inflammatory reactions by generating cysteamine. Cysteamine 179-189 vanin 1 Mus musculus 85-98 23890358-11 2013 The messenger RNA expressions of cyclooxygenase-2 and inducible nitric oxide synthase were remarkably decreased in the yam group compared with the cysteamine group, and the serum levels of proinflammatory cytokines including interleukin-1beta, interleukin-6, and tumor necrosis factor were significantly attenuated in the yam group. Cysteamine 147-157 prostaglandin-endoperoxide synthase 2 Rattus norvegicus 33-85 25427467-2 2013 Glucose oxidase (GOx) was used as a model enzyme and was immobilized onto the gold surface forming a self assembled monolayer via FcSH and cysteamine. Cysteamine 139-149 hydroxyacid oxidase 1 Homo sapiens 17-20 22684023-8 2012 OCT1 mRNA was markedly expressed in the rat duodenum and in IEC-6, and transfection of IEC-6 with OCT1 siRNA decreased OCT1 mRNA expression and inhibited [(14)C]cysteamine uptake. Cysteamine 161-171 solute carrier family 22 member 1 Rattus norvegicus 0-4 23588842-3 2013 Cysteamine bitartrate (Cystagon) has been shown to reduce the storage material in PPT1 deficient cells. Cysteamine 0-21 palmitoyl-protein thioesterase 1 Homo sapiens 82-86 23588842-3 2013 Cysteamine bitartrate (Cystagon) has been shown to reduce the storage material in PPT1 deficient cells. Cysteamine 23-31 palmitoyl-protein thioesterase 1 Homo sapiens 82-86 23536773-1 2013 BACKGROUND: The aim of this study was to investigate the molecular mechanisms involved in the production of Th1 cytokines, namely IL-12 and IL-27, when the intra-macrophage redox state was altered by different chemical entities such as GSH-C4, which is reduced glutathione carrying an aliphatic chain, or I-152, a pro-drug of N-acetyl-cysteine (NAC) and beta-mercaptoethylamine. Cysteamine 354-377 negative elongation factor complex member C/D, Th1l Mus musculus 108-111 23536773-1 2013 BACKGROUND: The aim of this study was to investigate the molecular mechanisms involved in the production of Th1 cytokines, namely IL-12 and IL-27, when the intra-macrophage redox state was altered by different chemical entities such as GSH-C4, which is reduced glutathione carrying an aliphatic chain, or I-152, a pro-drug of N-acetyl-cysteine (NAC) and beta-mercaptoethylamine. Cysteamine 354-377 interleukin 27 Mus musculus 140-145 23169667-0 2012 Heptahelical protein PQLC2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy. Cysteamine 96-106 solute carrier family 66 member 1 Homo sapiens 21-26 23169667-6 2012 Finally, PQLC2 transports a lysine-like mixed disulfide that serves as a chemical intermediate in cysteamine therapy of cystinosis, and PQLC2 gene silencing trapped this intermediate in cystinotic cells. Cysteamine 98-108 solute carrier family 66 member 1 Homo sapiens 9-14 23169667-8 2012 The elucidation of PQLC2 function may help improve cysteamine therapy. Cysteamine 51-61 solute carrier family 66 member 1 Homo sapiens 19-24 22946046-6 2012 Furthermore, CGN(-/-) mice show an exacerbated response to the ulcerogenic action of cysteamine, whereas acute injury of the colon by dextran sodium sulfate elicits undistinguishable responses in CGN(-/-) and CGN(+/+) mice. Cysteamine 85-95 cingulin Mus musculus 13-16 22633783-0 2012 The effect of cysteamine bitartrate on adiponectin multimerization in non-alcoholic fatty liver disease and healthy subjects. Cysteamine 14-35 adiponectin, C1Q and collagen domain containing Homo sapiens 39-50 22633783-1 2012 OBJECTIVE: To determine the effects of cysteamine on adiponectin multimerization in sera of patients with nonalcoholic fatty liver disease (NAFLD). Cysteamine 39-49 adiponectin, C1Q and collagen domain containing Homo sapiens 53-64 22633783-5 2012 RESULTS: Following 24 weeks of cysteamine therapy, the mean percentage increase for high, medium (MMW), and low (LMW) molecular weight multimers and total adiponectin from baseline was 53% (P = .02), 19% (P = .02), 29.4% (P = .03), and 49.3% (P = .05), respectively. Cysteamine 31-41 adiponectin, C1Q and collagen domain containing Homo sapiens 155-166 22633783-7 2012 Sera from 0 week, incubated in cysteamine for 1 hour, showed a significant mean percent increase in LMW adiponectin levels and a mean percent reduction in MMW levels compared with baseline in adults with and without NAFLD. Cysteamine 31-41 adiponectin, C1Q and collagen domain containing Homo sapiens 104-115 22633783-8 2012 CONCLUSIONS: Cysteamine impacts adiponectin multimerization. Cysteamine 13-23 adiponectin, C1Q and collagen domain containing Homo sapiens 32-43 22633783-10 2012 Cysteamine may be a potential therapeutic agent for conditions associated with insulin-resistance, oxidative stress, and depressed adiponectin levels. Cysteamine 0-10 adiponectin, C1Q and collagen domain containing Homo sapiens 131-142 23598025-0 2013 Cu2+-modulated cysteamine-capped CdS quantum dots as a turn-on fluorescence sensor for cyanide recognition. Cysteamine 15-25 CDP-diacylglycerol synthase 1 Homo sapiens 33-36 23598025-1 2013 A new fluorescence sensor for detection of cyanide ions (CN(-)) in aqueous media based on the recovered fluorescence of cysteamine capped CdS quantum dots [Cys-CdS QDs]-Cu(2+) system was proposed. Cysteamine 120-130 CDP-diacylglycerol synthase 1 Homo sapiens 138-141 23598025-1 2013 A new fluorescence sensor for detection of cyanide ions (CN(-)) in aqueous media based on the recovered fluorescence of cysteamine capped CdS quantum dots [Cys-CdS QDs]-Cu(2+) system was proposed. Cysteamine 120-130 CDP-diacylglycerol synthase 1 Homo sapiens 160-163 23598025-2 2013 The fluorescence intensity of Cys-CdS QDs was quenched by Cu(2+) due to the binding of Cu(2+) to cysteamine on the surface of the QDs. Cysteamine 97-107 CDP-diacylglycerol synthase 1 Homo sapiens 34-37 22898660-3 2013 Here we describe development of a new sensitive label free impedimetric immunosensor for the detection of MDM2 based on cysteamine self assembled monolayers on a clean polycrystalline Au electrode surface. Cysteamine 120-130 transformed mouse 3T3 cell double minute 2 Mus musculus 106-110 22452597-0 2012 Oxygen concentration and cysteamine supplementation during in vitro production of buffalo (Bubalus bubalis) embryos affect mRNA expression of BCL-2, BCL-XL, MCL-1, BAX and BID. Cysteamine 25-35 apoptosis regulator Bcl-2 Bubalus bubalis 142-147 22452597-0 2012 Oxygen concentration and cysteamine supplementation during in vitro production of buffalo (Bubalus bubalis) embryos affect mRNA expression of BCL-2, BCL-XL, MCL-1, BAX and BID. Cysteamine 25-35 bcl-2-like protein 1 Bubalus bubalis 149-155 22452597-0 2012 Oxygen concentration and cysteamine supplementation during in vitro production of buffalo (Bubalus bubalis) embryos affect mRNA expression of BCL-2, BCL-XL, MCL-1, BAX and BID. Cysteamine 25-35 induced myeloid leukemia cell differentiation protein Mcl-1 Bubalus bubalis 157-162 22452597-0 2012 Oxygen concentration and cysteamine supplementation during in vitro production of buffalo (Bubalus bubalis) embryos affect mRNA expression of BCL-2, BCL-XL, MCL-1, BAX and BID. Cysteamine 25-35 apoptosis regulator BAX Bubalus bubalis 164-167 22452597-0 2012 Oxygen concentration and cysteamine supplementation during in vitro production of buffalo (Bubalus bubalis) embryos affect mRNA expression of BCL-2, BCL-XL, MCL-1, BAX and BID. Cysteamine 25-35 BH3-interacting domain death agonist Bubalus bubalis 172-175 22452597-4 2012 Following cysteamine supplementation, the blastocyst rate and the relative mRNA abundance of BCL-XL and MCL-1 was significantly higher (p < 0.05) and that of BAX but not BID was lower (p < 0.05) at many stages of embryonic development, although it did not affect the percentage of TUNEL positive cells in the blastocysts significantly. Cysteamine 10-20 bcl-2-like protein 1 Bubalus bubalis 93-99 22452597-4 2012 Following cysteamine supplementation, the blastocyst rate and the relative mRNA abundance of BCL-XL and MCL-1 was significantly higher (p < 0.05) and that of BAX but not BID was lower (p < 0.05) at many stages of embryonic development, although it did not affect the percentage of TUNEL positive cells in the blastocysts significantly. Cysteamine 10-20 induced myeloid leukemia cell differentiation protein Mcl-1 Bubalus bubalis 104-109 22452597-4 2012 Following cysteamine supplementation, the blastocyst rate and the relative mRNA abundance of BCL-XL and MCL-1 was significantly higher (p < 0.05) and that of BAX but not BID was lower (p < 0.05) at many stages of embryonic development, although it did not affect the percentage of TUNEL positive cells in the blastocysts significantly. Cysteamine 10-20 apoptosis regulator BAX Bubalus bubalis 161-164 22452597-4 2012 Following cysteamine supplementation, the blastocyst rate and the relative mRNA abundance of BCL-XL and MCL-1 was significantly higher (p < 0.05) and that of BAX but not BID was lower (p < 0.05) at many stages of embryonic development, although it did not affect the percentage of TUNEL positive cells in the blastocysts significantly. Cysteamine 10-20 BH3-interacting domain death agonist Bubalus bubalis 173-176 23001131-5 2012 Treatment with cysteamine, a TG2 inhibitor, ameliorated disease severity in WT mice. Cysteamine 15-25 transglutaminase 2, C polypeptide Mus musculus 29-32 23170042-3 2012 Vanin-1 is a ubiquitous epithelial ectoenzyme that has pantetheinase activity and produces cysteamine, a potent endogenous antioxidant. Cysteamine 91-101 vanin 1 Mus musculus 0-7 22684023-8 2012 OCT1 mRNA was markedly expressed in the rat duodenum and in IEC-6, and transfection of IEC-6 with OCT1 siRNA decreased OCT1 mRNA expression and inhibited [(14)C]cysteamine uptake. Cysteamine 161-171 solute carrier family 22 member 1 Rattus norvegicus 98-102 22684023-8 2012 OCT1 mRNA was markedly expressed in the rat duodenum and in IEC-6, and transfection of IEC-6 with OCT1 siRNA decreased OCT1 mRNA expression and inhibited [(14)C]cysteamine uptake. Cysteamine 161-171 solute carrier family 22 member 1 Rattus norvegicus 98-102 22684023-9 2012 Cysteamine-induced duodenal ulcers were decreased in OCT1/2 knockout mice. Cysteamine 0-10 solute carrier family 22 (organic cation transporter), member 1 Mus musculus 53-57 22822152-5 2012 In mutants of ctns-1 (C. elegans homolog of CTNS), LAAT-1 was required to reduce lysosomal cystine levels and suppress lysosome enlargement by cysteamine, a drug that alleviates cystinosis by converting cystine to a lysine analog. Cysteamine 143-153 Cystinosin homolog Caenorhabditis elegans 14-20 21777509-5 2012 We found that cysteamine administration (150 mg/kg.d, through drinking water) for 30 d significantly ameliorated the decreases in GAD67, mature BDNF and full-length TrkB protein levels found in frontal cortex and hippocampus of HRM. Cysteamine 14-24 brain derived neurotrophic factor Mus musculus 144-148 21777509-5 2012 We found that cysteamine administration (150 mg/kg.d, through drinking water) for 30 d significantly ameliorated the decreases in GAD67, mature BDNF and full-length TrkB protein levels found in frontal cortex and hippocampus of HRM. Cysteamine 14-24 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 165-169 21777509-6 2012 A significant attenuation of the increased levels of truncated BDNF in frontal cortex and hippocampus, as well as truncated TrkB in frontal cortex of HRM was also observed following cysteamine treatment. Cysteamine 182-192 brain derived neurotrophic factor Mus musculus 63-67 21777509-6 2012 A significant attenuation of the increased levels of truncated BDNF in frontal cortex and hippocampus, as well as truncated TrkB in frontal cortex of HRM was also observed following cysteamine treatment. Cysteamine 182-192 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 124-128 21777509-9 2012 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in GAD67 expression suggesting that TrkB signalling plays an important role in GAD67 regulation by cysteamine. Cysteamine 62-72 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 27-31 21777509-9 2012 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in GAD67 expression suggesting that TrkB signalling plays an important role in GAD67 regulation by cysteamine. Cysteamine 62-72 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 109-113 21777509-9 2012 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in GAD67 expression suggesting that TrkB signalling plays an important role in GAD67 regulation by cysteamine. Cysteamine 172-182 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 27-31 21777509-9 2012 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in GAD67 expression suggesting that TrkB signalling plays an important role in GAD67 regulation by cysteamine. Cysteamine 172-182 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 109-113 22822152-5 2012 In mutants of ctns-1 (C. elegans homolog of CTNS), LAAT-1 was required to reduce lysosomal cystine levels and suppress lysosome enlargement by cysteamine, a drug that alleviates cystinosis by converting cystine to a lysine analog. Cysteamine 143-153 Lysosomal amino acid transporter 1 Caenorhabditis elegans 51-57 22822152-7 2012 Thus, LAAT-1 is the lysosomal lysine/arginine transporter, which suggests a molecular explanation for how cysteamine alleviates a lysosomal storage disease. Cysteamine 106-116 Lysosomal amino acid transporter 1 Caenorhabditis elegans 6-12 22236828-7 2012 At 35 d of age, piglets treated with cysteamine showed increased (P < 0.05) ghrelin and gastrin and decreased (P < 0.05) somatostatin mRNA expression in gastric mucosa. Cysteamine 37-47 gastrin Sus scrofa 91-98 22236828-8 2012 Moreover, dietary cysteamine treatment increased serum concentration of gastrin (P < 0.05). Cysteamine 18-28 gastrin Sus scrofa 72-79 22534700-0 2012 Ghrelin accelerates the healing of cysteamine-induced duodenal ulcers in rats. Cysteamine 35-45 ghrelin and obestatin prepropeptide Rattus norvegicus 0-7 22534700-2 2012 The aim of the present investigation was to examine the influence of ghrelin administration on the course of cysteamine-induced duodenal ulcers, as well as effects on mucosal production of oxygen free radicals and duodenal antioxidant defense. Cysteamine 109-119 ghrelin and obestatin prepropeptide Rattus norvegicus 69-76 22534700-6 2012 RESULTS: Induction of ulcers by cysteamine was accompanied by a reduction in duodenal blood flow, mucosal DNA synthesis and mucosal activity of superoxide dismutase (SOD); whereas mucosal concentration of interleukin-1beta and malonyldialdehyde (MDA - an index of lipid peroxidation) were increased. Cysteamine 32-42 interleukin 1 beta Rattus norvegicus 205-222 22397924-2 2012 Aiming at the modification of their size, topology and lipophilicity, Tc1-Tc6 were obtained based on an S,N,O-donor bifunctional chelator (BFC) derived from cysteamine and on pyridyl- and pyrazolyl-containing N,N,O-donor BFCs. Cysteamine 157-167 transcobalamin 1 Homo sapiens 70-73 22369897-3 2012 The MARS-115 CatG peptidyl inhibitor containing the 1-aminoalkylphosphonate diaryl ester moiety at the C terminus and N-succinamide with a free carboxylic function was synthesized and covalently immobilized onto the gold chip surface via the thiol group (cysteamine). Cysteamine 255-265 cathepsin G Homo sapiens 13-17 22266295-0 2012 An impedimetric vascular endothelial growth factor biosensor-based PAMAM/cysteamine-modified gold electrode for monitoring of tumor growth. Cysteamine 73-83 vascular endothelial growth factor A Homo sapiens 16-50 22196880-4 2012 Novel immunosensors have been fabricated using polyclonal antibodies raised against a human Ad (Ad5) capsid protein, which were selectively cleaved into antibody fragments by 2-mercaptoethylamine. Cysteamine 175-195 Alzheimer disease, familial, type 5 Homo sapiens 96-99 22561175-9 2012 RESULTS: In crude analyses, low AAC (odds ratio [OR], 2.05 [1.27-3.30]; p=.003) and high AAC (OR, 2.24 [1.38-3.62]; p=.001) were strongly associated with DHL, when compared with the reference group of no AAC. Cysteamine 154-157 glycine-N-acyltransferase Homo sapiens 89-92 22561175-9 2012 RESULTS: In crude analyses, low AAC (odds ratio [OR], 2.05 [1.27-3.30]; p=.003) and high AAC (OR, 2.24 [1.38-3.62]; p=.001) were strongly associated with DHL, when compared with the reference group of no AAC. Cysteamine 154-157 glycine-N-acyltransferase Homo sapiens 89-92 22561175-11 2012 Adjustment for age, sex, and BMI markedly attenuated the associations between DHL and low AAC (OR, 1.20 [0.69-2.09]; p=.51) and high AAC (OR, 0.74 [0.36-1.53]; p=.42). Cysteamine 78-81 glycine-N-acyltransferase Homo sapiens 90-93 22561175-14 2012 However, the association of AAC with DHL was explained by the effects of age, sex, and BMI. Cysteamine 37-40 glycine-N-acyltransferase Homo sapiens 28-31 22281827-2 2012 The authors investigated whether TG2 is involved in selenite-induced cataract formation in rats and whether cysteamine, a chemical inhibitor of TG2, can prevent cataract formation in this model. Cysteamine 108-118 transglutaminase 2 Rattus norvegicus 144-147 22486866-0 2012 Attenuation of cysteamine-induced duodenal ulcer with Cochinchina momordica seed extract through inhibiting cytoplasmic phospholipase A2/5-lipoxygenase and activating gamma-glutamylcysteine synthetase. Cysteamine 15-25 phospholipase A2 group IB Rattus norvegicus 120-136 22486866-0 2012 Attenuation of cysteamine-induced duodenal ulcer with Cochinchina momordica seed extract through inhibiting cytoplasmic phospholipase A2/5-lipoxygenase and activating gamma-glutamylcysteine synthetase. Cysteamine 15-25 arachidonate 5-lipoxygenase Rattus norvegicus 137-151 22486866-0 2012 Attenuation of cysteamine-induced duodenal ulcer with Cochinchina momordica seed extract through inhibiting cytoplasmic phospholipase A2/5-lipoxygenase and activating gamma-glutamylcysteine synthetase. Cysteamine 15-25 glutamate-cysteine ligase, catalytic subunit Rattus norvegicus 167-200 22486866-6 2012 RESULTS: Cochinchina momordica seed extract effectively prevented cysteamine-induced duodenal ulcer in a dose-dependent manner as reflected with significant decreases in either duodenal ulcerogenesis or perforation accompanied with significantly decreased in serum gastrin in addition to inflammatory mediators including cPLA(2), COX-2, and 5-lipoxygenase. Cysteamine 66-76 gastrin Rattus norvegicus 265-272 22486866-6 2012 RESULTS: Cochinchina momordica seed extract effectively prevented cysteamine-induced duodenal ulcer in a dose-dependent manner as reflected with significant decreases in either duodenal ulcerogenesis or perforation accompanied with significantly decreased in serum gastrin in addition to inflammatory mediators including cPLA(2), COX-2, and 5-lipoxygenase. Cysteamine 66-76 phospholipase A2 group IVA Rattus norvegicus 321-328 22486866-6 2012 RESULTS: Cochinchina momordica seed extract effectively prevented cysteamine-induced duodenal ulcer in a dose-dependent manner as reflected with significant decreases in either duodenal ulcerogenesis or perforation accompanied with significantly decreased in serum gastrin in addition to inflammatory mediators including cPLA(2), COX-2, and 5-lipoxygenase. Cysteamine 66-76 prostaglandin-endoperoxide synthase 2 Rattus norvegicus 330-335 22486866-6 2012 RESULTS: Cochinchina momordica seed extract effectively prevented cysteamine-induced duodenal ulcer in a dose-dependent manner as reflected with significant decreases in either duodenal ulcerogenesis or perforation accompanied with significantly decreased in serum gastrin in addition to inflammatory mediators including cPLA(2), COX-2, and 5-lipoxygenase. Cysteamine 66-76 arachidonate 5-lipoxygenase Rattus norvegicus 341-355 22486866-9 2012 CONCLUSION: Cochinchina momordica seed extracts exerted significantly protective effect against cysteamine-induced duodenal ulcer by either cPLA2 inhibition or glutathione preservation. Cysteamine 96-106 phospholipase A2 group IVA Rattus norvegicus 140-145 22720042-1 2012 The pantetheinase vanin-1 generates cysteamine, which inhibits reduced glutathione (GSH) synthesis. Cysteamine 36-46 vanin 1 Mus musculus 18-25 22127389-7 2012 Finally, treating Mecp2-deficient mice with cysteamine, a molecule increasing the secretion of Bdnf vesicles, improved the lifespan and reduced motor defects, suggesting a new therapeutic strategy for Rett syndrome. Cysteamine 44-54 brain derived neurotrophic factor Mus musculus 95-99 22059229-0 2012 Sensitive and selective voltammetric measurement of Hg2+ by rational covalent functionalization of graphene oxide with cysteamine. Cysteamine 119-129 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 52-55 21864497-4 2011 The presence of sodium chloride and a nonionic detergent Brij-35 in a reaction solution led to the lower collagenolytic activity of MMP-9, whereas they suppressed the nonspecific interaction between MMP-9 and a cysteamine-modified chip. Cysteamine 211-221 matrix metallopeptidase 9 Homo sapiens 199-204 22532830-5 2012 To study mechanism of action, we examined cell viability and matrix metalloproteinases (MMPs) activity in the cysteamine-treated cells. Cysteamine 110-120 matrix metallopeptidase 9 Homo sapiens 88-92 22238597-12 2012 From our studies, a number of possible substrates with relatively high k(cat)/K(m) have been discovered, including dopamine and cysteamine, which may implicate a role for adipocyte AOC3 in insulin-signaling and fatty acid metabolism, respectively. Cysteamine 128-138 amine oxidase copper containing 3 Homo sapiens 181-185 22238597-12 2012 From our studies, a number of possible substrates with relatively high k(cat)/K(m) have been discovered, including dopamine and cysteamine, which may implicate a role for adipocyte AOC3 in insulin-signaling and fatty acid metabolism, respectively. Cysteamine 128-138 insulin Homo sapiens 189-196 22099650-1 2011 An electrochemical biosensor for detection of fructose in food samples was developed by immobilization of fructose dehydrogenase (FDH) on cysteamine and poly(amidoamine) dendrimers (PAMAM)-modified gold electrode surface. Cysteamine 138-148 aldehyde dehydrogenase 1 family member L1 Homo sapiens 106-128 22099650-1 2011 An electrochemical biosensor for detection of fructose in food samples was developed by immobilization of fructose dehydrogenase (FDH) on cysteamine and poly(amidoamine) dendrimers (PAMAM)-modified gold electrode surface. Cysteamine 138-148 aldehyde dehydrogenase 1 family member L1 Homo sapiens 130-133 21663400-1 2011 Alkaline phosphatase (ALP) was immobilized with cross-linking agents glutaraldehyde and cysteamine by forming a self-assembled monolayer on a screen printed gold electrode. Cysteamine 88-98 alkaline phosphatase, placental Homo sapiens 0-20 24309308-8 2011 Additionally, the effect of cysteamine on P-gp transport activity and phosphate uptake was determined; demonstrating increased P-gp activity in cystinotic cells, and further decrease of proximal tubular phosphate uptake. Cysteamine 28-38 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 24309308-8 2011 Additionally, the effect of cysteamine on P-gp transport activity and phosphate uptake was determined; demonstrating increased P-gp activity in cystinotic cells, and further decrease of proximal tubular phosphate uptake. Cysteamine 28-38 ATP binding cassette subfamily B member 1 Homo sapiens 127-131 21437649-6 2011 The pantetheinase product cysteamine is an inexpensive and non-toxic aminothiol that is approved for lifelong clinical management of nephropathic cystinosis. Cysteamine 26-36 vanin 1 Mus musculus 4-17 21395631-16 2011 CONCLUSIONS: Enteric-coated cysteamine reduces ALT and AST levels in children with NAFLD without reduction in body mass index. Cysteamine 28-38 solute carrier family 17 member 5 Homo sapiens 55-58 21671870-4 2011 Involvement of somatostatin and the sstR4 was revealed by using pretreatment with somatostatin antibody, depletion of somatostatin with cysteamine, measuring the plasma somatostatin-like immunoreactivity, release from nerves in vitro from isolated trachea, detection of sstR4 receptors in animal and human tissue specimens, using sstR4 gene-deleted mice and investigating in detail effects of a stable peptide analogue of somatostatin (TT-232) and of an ultrapotent non-peptide agonist of sstR4 receptors. Cysteamine 136-146 somatostatin receptor 4 Homo sapiens 36-41 21128610-1 2011 Di-(N-butanoic acid-1,8-naphthalimide)-piperazine dithienylethene was covalently linked to a cysteamine monolayer associated with a Au surface to yield a photoisomerizable monolayer composed of the open or closed dithienylcyclopentene isomers (3a or 3b), respectively. Cysteamine 93-103 mediator complex subunit 25 Homo sapiens 15-21 21548866-6 2011 Indeed, daily treatment of rats with bFGF, PDGF or VEGF markedly improved the healing of cysteamine-induced chronic duodenal ulcers, without any reduction in gastric acid secretion. Cysteamine 89-99 fibroblast growth factor 2 Rattus norvegicus 37-41 21548866-6 2011 Indeed, daily treatment of rats with bFGF, PDGF or VEGF markedly improved the healing of cysteamine-induced chronic duodenal ulcers, without any reduction in gastric acid secretion. Cysteamine 89-99 vascular endothelial growth factor A Rattus norvegicus 51-55 21628860-2 2011 It is considered that BCL2 translocation precedes MYC events in lymphomagenesis of DHL. Cysteamine 83-86 BCL2 apoptosis regulator Homo sapiens 22-26 21628860-2 2011 It is considered that BCL2 translocation precedes MYC events in lymphomagenesis of DHL. Cysteamine 83-86 MYC proto-oncogene, bHLH transcription factor Homo sapiens 50-53 20881007-9 2011 Mass spectrometry and site-directed mutagenesis indicate that SIGC(-cysteamine) specifically and efficiently leads to cysteamine (half-cystamine) modification of a single site on Gbeta, likely GbetaCys204, and inhibits Gbetagamma more than a hundred times more potently than cystamine. Cysteamine 68-78 succinate-CoA ligase GDP-forming subunit beta Homo sapiens 179-184 22065917-7 2011 CONCLUSIONS: Measurement of CVI shows that there is a progressive increase in cystine crystal volume up to 8 months of age and that cysteamine eyedrops significantly inhibits progression in the Ctns(-/-) mouse. Cysteamine 132-142 cystinosis, nephropathic Mus musculus 194-198 22219632-8 2011 CONCLUSIONS: This study showed that CYS decreased PBMC proliferation, IL-6 and TGF-beta1 levels via ROS formation. Cysteamine 36-39 interleukin 6 Homo sapiens 70-74 22219632-8 2011 CONCLUSIONS: This study showed that CYS decreased PBMC proliferation, IL-6 and TGF-beta1 levels via ROS formation. Cysteamine 36-39 transforming growth factor beta 1 Homo sapiens 79-88 20881007-9 2011 Mass spectrometry and site-directed mutagenesis indicate that SIGC(-cysteamine) specifically and efficiently leads to cysteamine (half-cystamine) modification of a single site on Gbeta, likely GbetaCys204, and inhibits Gbetagamma more than a hundred times more potently than cystamine. Cysteamine 118-128 succinate-CoA ligase GDP-forming subunit beta Homo sapiens 179-184 22039440-0 2011 Cysteamine attenuates the decreases in TrkB protein levels and the anxiety/depression-like behaviors in mice induced by corticosterone treatment. Cysteamine 0-10 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 39-43 22039440-5 2011 RESULTS: Cysteamine administration (150 mg/kg/day, through drinking water) for 21 days significantly ameliorated chronic corticosterone-induced decreases in TrkB protein levels in frontal cortex and hippocampus. Cysteamine 9-19 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 157-161 22039440-7 2011 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in behavioral tests, suggesting that TrkB signaling plays an important role in the antidepressant effects of cysteamine. Cysteamine 62-72 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 27-31 22039440-7 2011 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in behavioral tests, suggesting that TrkB signaling plays an important role in the antidepressant effects of cysteamine. Cysteamine 62-72 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 110-114 22039440-7 2011 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in behavioral tests, suggesting that TrkB signaling plays an important role in the antidepressant effects of cysteamine. Cysteamine 182-192 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 27-31 22039440-7 2011 Finally, mice deficient in TrkB, showed a reduced response to cysteamine in behavioral tests, suggesting that TrkB signaling plays an important role in the antidepressant effects of cysteamine. Cysteamine 182-192 neurotrophic tyrosine kinase, receptor, type 2 Mus musculus 110-114 23646236-1 2010 We report step-wise changing of magnetic behavior of iron oxide core gold shell nanoparticles from super paramagnetic to permanent magnetism at room temperature, on step-wise bio-functionalization with leutenizing hormone and releasing hormone (LHRH) through cysteamine linker. Cysteamine 259-269 gonadotropin releasing hormone 1 Homo sapiens 202-243 20848033-7 2010 In addition, the introduction of a latent thiol group in the form of protected cysteamine at the C-terminus of the CD52 glycoforms will enable site-specific conjugation to a carrier protein to provide immunogens for generating CD52 glycoform-specific antibodies for functional studies. Cysteamine 79-89 CD52 molecule Homo sapiens 115-119 20848033-7 2010 In addition, the introduction of a latent thiol group in the form of protected cysteamine at the C-terminus of the CD52 glycoforms will enable site-specific conjugation to a carrier protein to provide immunogens for generating CD52 glycoform-specific antibodies for functional studies. Cysteamine 79-89 CD52 molecule Homo sapiens 227-231 20165931-4 2010 Cysteamine (400 mg kg(-1) body weight(-1), two doses at 4 h interval) orally given to rats resulted in high ulcer index, increased TBARS with concomitant depletion of antioxidants such as superoxide dismutase, glutathione, glutathione peroxidase, and inflammatory markers cathepsin D, and myeloperoxidase (p < 0.01). Cysteamine 0-10 cathepsin D Rattus norvegicus 272-283 20165931-4 2010 Cysteamine (400 mg kg(-1) body weight(-1), two doses at 4 h interval) orally given to rats resulted in high ulcer index, increased TBARS with concomitant depletion of antioxidants such as superoxide dismutase, glutathione, glutathione peroxidase, and inflammatory markers cathepsin D, and myeloperoxidase (p < 0.01). Cysteamine 0-10 myeloperoxidase Rattus norvegicus 289-304 20219464-0 2010 Cysteamine, the natural metabolite of pantetheinase, shows specific activity against Plasmodium. Cysteamine 0-10 vanin 1 Mus musculus 38-51 20716238-10 2010 This study compares the pharmacokinetics and gastrin production following cysteamine bitartrate non-enteric-coated and cysteamine bitartrate enteric-coated in normal healthy subjects. Cysteamine 74-95 gastrin Homo sapiens 45-52 20716238-10 2010 This study compares the pharmacokinetics and gastrin production following cysteamine bitartrate non-enteric-coated and cysteamine bitartrate enteric-coated in normal healthy subjects. Cysteamine 74-84 gastrin Homo sapiens 45-52 20219464-2 2010 Treatment of mice with the pantetheinase metabolite cysteamine reduces blood-stage replication of P. chabaudi and significantly increases survival. Cysteamine 52-62 vanin 1 Mus musculus 27-40 19324348-7 2010 RESULT(S): The addition of Cys to DMM supplemented with EGF and IGF-I improved the mean blastocyst formation compared medium without Cys. Cysteamine 27-30 EGF Ovis aries 56-59 20380823-7 2010 In addition, the inhibited secretion of the brain-derived neurotrophic factor (BDNF) by neurons derived from substantia nigra pars compact (SNpc) of MPTP-treated mice was significantly restored by cysteamine administration. Cysteamine 197-207 brain derived neurotrophic factor Mus musculus 44-77 20380823-7 2010 In addition, the inhibited secretion of the brain-derived neurotrophic factor (BDNF) by neurons derived from substantia nigra pars compact (SNpc) of MPTP-treated mice was significantly restored by cysteamine administration. Cysteamine 197-207 brain derived neurotrophic factor Mus musculus 79-83 19324348-7 2010 RESULT(S): The addition of Cys to DMM supplemented with EGF and IGF-I improved the mean blastocyst formation compared medium without Cys. Cysteamine 27-30 insulin-like growth factor I Ovis aries 64-69 20018163-1 2010 Vanin-1 is a pantetheinase that catalyzes the hydrolysis of pantetheine to produce pantothenic acid (vitamin B5) and cysteamine. Cysteamine 117-127 vanin 1 Homo sapiens 0-7 20104912-0 2010 SERS study of rotational isomerization of cysteamine induced by magnetic pulling force. Cysteamine 42-52 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 0-4 20118770-16 2010 Familiarity with the morphologic and immunophenotypic spectrum of DHL is important in directing testing to detect concurrent IGH-BCL2 and MYC rearrangements when a karyotype is unavailable. Cysteamine 66-69 immunoglobulin heavy locus Homo sapiens 125-128 20118770-16 2010 Familiarity with the morphologic and immunophenotypic spectrum of DHL is important in directing testing to detect concurrent IGH-BCL2 and MYC rearrangements when a karyotype is unavailable. Cysteamine 66-69 BCL2 apoptosis regulator Homo sapiens 129-133 20118770-16 2010 Familiarity with the morphologic and immunophenotypic spectrum of DHL is important in directing testing to detect concurrent IGH-BCL2 and MYC rearrangements when a karyotype is unavailable. Cysteamine 66-69 MYC proto-oncogene, bHLH transcription factor Homo sapiens 138-141 19572375-1 2010 BACKGROUND: Vanin-1 is an epithelial pantetheinase that provides cysteamine to tissue and regulates response to stress. Cysteamine 65-75 vanin 1 Mus musculus 12-19 18805469-1 2008 Pantetheinase (EC 3.5.1.92) is an enzyme that hydrolyzes pantetheine, an intermediate metabolite of coenzyme A, into pantothenic acid (vitamin B(5)) and cysteamine, a potent antioxidant. Cysteamine 153-163 vanin 2 Homo sapiens 0-13 19775699-11 2010 Mean serum gastrin levels were similar after ingestion of cysteamine and enteric-release cysteamine. Cysteamine 58-68 gastrin Homo sapiens 11-18 18620823-11 2009 The highest cleavage rate recorded in the IGF-1+cysteamine treatment (71.9%) which was significantly higher (P<0.05) than the IGF-1+beta-ME (45.2%) and EGF+beta-ME (46.4%) treatments, but not significantly differ from the control (63.8%) and EGF+cysteamine treatment (60.7%). Cysteamine 249-259 insulin like growth factor 1 Homo sapiens 42-47 18620823-12 2009 The proportion of cleaved oocytes those developed to blastocyst stage was significantly higher in the IGF-1+cysteamine treatment (52.2%; P<0.05) than in the control (23.3%), the EGF+cysteamine (13.5%) or the EGF+beta-ME (7.7%) treatments, but did not differ significantly from the IGF-1+beta-ME (28.6%) treatment. Cysteamine 108-118 insulin like growth factor 1 Homo sapiens 102-107 18620823-12 2009 The proportion of cleaved oocytes those developed to blastocyst stage was significantly higher in the IGF-1+cysteamine treatment (52.2%; P<0.05) than in the control (23.3%), the EGF+cysteamine (13.5%) or the EGF+beta-ME (7.7%) treatments, but did not differ significantly from the IGF-1+beta-ME (28.6%) treatment. Cysteamine 108-118 insulin like growth factor 1 Homo sapiens 284-289 18620823-12 2009 The proportion of cleaved oocytes those developed to blastocyst stage was significantly higher in the IGF-1+cysteamine treatment (52.2%; P<0.05) than in the control (23.3%), the EGF+cysteamine (13.5%) or the EGF+beta-ME (7.7%) treatments, but did not differ significantly from the IGF-1+beta-ME (28.6%) treatment. Cysteamine 185-195 insulin like growth factor 1 Homo sapiens 102-107 19342511-9 2009 Cysteamine also enhanced activation of mucosal iron regulatory protein 1 and increased the expression of divalent metal transporter 1 mRNA and protein. Cysteamine 0-10 aconitase 1 Rattus norvegicus 47-72 18980225-5 2009 Following terminal differentiation, the myotubes cultured on cysteamine-coated gold resemble myotube cultures obtained on plastic for the size and orientation of the myotube bundles retaining most of myosin expression; on the contrary, the myotube cultures on gold show a clumped morphology, likely due to repulsive cell-substratum interaction resulting in aberrant differentiation. Cysteamine 61-71 myosin heavy chain 14 Homo sapiens 200-206 19650499-2 2009 Nano gold particles were immobilized with cysteamine layer by self-assembly, whose surfaces were chemically coupled with anti-transferrin antibodies by using EDCX, forming the anti-transferrin-Au immuno-probes. Cysteamine 42-52 transferrin Homo sapiens 181-192 19437977-0 2009 Acetylcholinesterase biosensor based on gold nanoparticles and cysteamine self assembled monolayer for determination of monocrotophos. Cysteamine 63-73 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 19437977-1 2009 In this paper, a simple method for immobilization of acetylcholinesterase (AChE) on cysteamine assembled glassy carbon electrode coupled with gold nanoparticles (GNPs) was proposed and thus a sensitive, fast and stable amperometric biosensor for quantitative determination of monocrotophos was developed. Cysteamine 84-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-73 19437977-1 2009 In this paper, a simple method for immobilization of acetylcholinesterase (AChE) on cysteamine assembled glassy carbon electrode coupled with gold nanoparticles (GNPs) was proposed and thus a sensitive, fast and stable amperometric biosensor for quantitative determination of monocrotophos was developed. Cysteamine 84-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-79 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 222-232 cysteine dioxygenase type 1 Rattus norvegicus 65-85 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 222-232 cysteine dioxygenase type 1 Rattus norvegicus 87-90 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 222-232 cysteine sulfinic acid decarboxylase Rattus norvegicus 190-194 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 236-246 cysteine dioxygenase type 1 Rattus norvegicus 65-85 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 236-246 cysteine dioxygenase type 1 Rattus norvegicus 87-90 19106324-2 2009 Taurine is synthesized either from the oxidation of cysteine via cysteine dioxygenase (CDO), which generates cysteinesulfinate that is decarboxylated by cysteinesulfinic acid decarboxylase (CSAD), or from the oxidation of cysteamine by cysteamine (2-aminoethanethiol) dioxygenase (ADO). Cysteamine 236-246 cysteine sulfinic acid decarboxylase Rattus norvegicus 190-194 19106324-7 2009 CDO mRNA levels also responded robustly to cysteine or cysteamine treatment in adipocytes but not in undifferentiated 3T3-L1 cells. Cysteamine 55-65 cysteine dioxygenase 1, cytosolic Mus musculus 0-3 19860701-7 2009 Decreased levels of gastric CGRP-like immunoreactivity (li) were observed during acetic acid-, cysteamine-, concentrated ethanol- or water immersion stress-ulcers. Cysteamine 95-105 calcitonin/calcitonin-related polypeptide, alpha Mus musculus 28-32 18463844-2 2008 The epithelial pantetheinase vanin-1 is proinflammatory and cytoprotective via cysteamine release in some tissues. Cysteamine 79-89 vanin 1 Mus musculus 15-28 18786174-6 2008 The results indicated that CYS as well as cysteamine (the FDA-approved precursor of CYS) increased BDNF protein levels in mouse frontal cortex 7 days after treatment. Cysteamine 42-52 brain derived neurotrophic factor Mus musculus 99-103 18582526-0 2008 Potential antidepressant properties of cysteamine on hippocampal BDNF levels and behavioral despair in mice. Cysteamine 39-49 brain derived neurotrophic factor Mus musculus 65-69 18582526-2 2008 Recent work has found that cysteamine and its related agent, cystamine, are neuroprotective in Huntington"s disease mice, and act by enhancing the secretion of central BDNF. Cysteamine 27-37 brain derived neurotrophic factor Mus musculus 168-172 18582526-8 2008 A significant increase in hippocampal BDNF levels was found in the cysteamine 200-mg/kg group (P<0.05). Cysteamine 67-77 brain derived neurotrophic factor Mus musculus 38-42 18582526-9 2008 Our findings suggested that cysteamine may possess an antidepressant-like effect, which may be mediated by increasing central BDNF levels. Cysteamine 28-38 brain derived neurotrophic factor Mus musculus 126-130 18553891-8 2008 CS supplementation has tissue-specific regulation of GHR, IGF-I, IGF-IR, and IGFBP-3 mRNA levels. Cysteamine 0-2 insulin-like growth factor-binding protein 3 Sus scrofa 77-84 18558621-9 2008 With the addition of LPS to mesangial cells, the expressions of tTG and TGF-beta1 were up-regulated, whilst the addition of cysteamine, tTG inhibitor, attenuated the expression of tTG and TGF-beta1 as well as the cellular proliferation which was further induced by LPS. Cysteamine 124-134 transglutaminase 2, C polypeptide Mus musculus 136-139 18558621-9 2008 With the addition of LPS to mesangial cells, the expressions of tTG and TGF-beta1 were up-regulated, whilst the addition of cysteamine, tTG inhibitor, attenuated the expression of tTG and TGF-beta1 as well as the cellular proliferation which was further induced by LPS. Cysteamine 124-134 transglutaminase 2, C polypeptide Mus musculus 136-139 18558621-9 2008 With the addition of LPS to mesangial cells, the expressions of tTG and TGF-beta1 were up-regulated, whilst the addition of cysteamine, tTG inhibitor, attenuated the expression of tTG and TGF-beta1 as well as the cellular proliferation which was further induced by LPS. Cysteamine 124-134 transforming growth factor, beta 1 Mus musculus 188-197 18803177-1 2008 An analytical procedure enabling routine analysis of human plasma for total cysteamine (CASH) has been developed and validated. Cysteamine 76-86 CASP8 and FADD like apoptosis regulator Homo sapiens 88-92 18753449-0 2008 Leptin is involved in the effects of cysteamine on egg laying of hens, characteristics of eggs, and posthatch growth of broiler offspring. Cysteamine 37-47 leptin Gallus gallus 0-6 18753449-7 2008 Serum concentrations of total thyroxine (P < 0.01) and leptin (P < 0.01) were significantly lower in cysteamine-treated hens, whereas total triiodothyronine (T(3)), free T(3), and glucagon were not affected. Cysteamine 107-117 leptin Gallus gallus 58-64 18753449-9 2008 Cysteamine did not affect the yolk content of T(3), thyroxine, estradiol, or glucagon, but significantly increased leptin content in liver of hens (P < 0.05), as well as in yolk (P < 0.05) and albumin (P < 0.05) of eggs. Cysteamine 0-10 leptin Gallus gallus 115-121 18585282-0 2008 Immobilization of cytochrome c on cysteamine-modified gold electrodes with EDC as coupling agent. Cysteamine 34-44 cytochrome c, somatic Equus caballus 18-30 18585282-1 2008 Cyclic voltammetry has been applied for the characterization of cross-linked horse heart cytochrome c (HHC) on cysteamine-modified gold electrodes. Cysteamine 111-121 cytochrome c, somatic Equus caballus 89-101 18553891-0 2008 Effects of dietary supplementation with cysteamine on growth hormone receptor and insulin-like growth factor system in finishing pigs. Cysteamine 40-50 growth hormone receptor Sus scrofa 54-77 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 insulin like growth factor 1 Sus scrofa 117-151 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 growth hormone receptor Sus scrofa 171-199 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 insulin like growth factor 1 receptor Sus scrofa 230-236 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 insulin-like growth factor-binding protein 3 Sus scrofa 239-268 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 insulin receptor Sus scrofa 274-290 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 68-78 insulin receptor Sus scrofa 234-236 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 80-82 insulin like growth factor 1 Sus scrofa 117-151 18553891-1 2008 The present study was conducted to test the hypothesis that chronic cysteamine (CS) supplementation may affect serum insulin-like growth factor (IGF)-I concentrations and growth hormone (GH) receptor (GHR), IGF-I, IGF-I receptor (IGF-IR), IGF binding protein (IGFBP)-3, and insulin receptor (IR) mRNA levels in different tissues of finishing pigs. Cysteamine 80-82 growth hormone receptor Sus scrofa 171-199 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 ADG Sus scrofa 91-94 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 insulin like growth factor 1 Sus scrofa 106-111 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 growth hormone receptor Sus scrofa 146-149 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 insulin like growth factor 1 Sus scrofa 154-159 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 insulin like growth factor 1 receptor Sus scrofa 186-192 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 insulin-like growth factor-binding protein 3 Sus scrofa 226-233 18553891-4 2008 The results indicated that CS supplementation (70 mg/kg) increased the average daily gain (ADG) and serum IGF-I level, upregulated mRNA levels of GHR and IGF-I (liver, stomach, muscle), IGF-IR (stomach, duodenum, muscle), and IGFBP-3 (liver) but downregulated IGFBP-3 (stomach, duodenum, muscle). Cysteamine 27-29 insulin-like growth factor-binding protein 3 Sus scrofa 260-267 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 growth hormone receptor Sus scrofa 45-48 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 insulin like growth factor 1 Sus scrofa 61-66 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 insulin like growth factor 1 receptor Sus scrofa 72-78 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 insulin-like growth factor-binding protein 3 Sus scrofa 135-142 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 insulin receptor Sus scrofa 76-78 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 ADG Sus scrofa 209-212 18553891-6 2008 CS supplementation (140 mg/kg) downregulated GHR (duodenum), IGF-I, and IGF-IR mRNA (liver, stomach, duodenum, muscle) but upregulated IGFBP-3 and IR mRNA (liver, stomach, duodenum, muscle) and did not affect ADG and serum IGF-I concentration. Cysteamine 0-2 insulin like growth factor 1 Sus scrofa 72-77 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 insulin like growth factor 1 Sus scrofa 99-104 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 growth hormone receptor Sus scrofa 148-151 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 insulin like growth factor 1 Sus scrofa 153-158 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 insulin like growth factor 1 receptor Sus scrofa 160-166 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 insulin-like growth factor-binding protein 3 Sus scrofa 168-175 18553891-7 2008 Collectively, the results suggest that dietary CS supplementation modulates the growth rate, serum IGF-I concentrations, and the gene expression of GHR, IGF-I, IGF-IR, IGFBP-3, and IR in a dose-dependent manner. Cysteamine 47-49 insulin receptor Sus scrofa 164-166 18553891-8 2008 CS supplementation has tissue-specific regulation of GHR, IGF-I, IGF-IR, and IGFBP-3 mRNA levels. Cysteamine 0-2 growth hormone receptor Sus scrofa 53-56 18553891-8 2008 CS supplementation has tissue-specific regulation of GHR, IGF-I, IGF-IR, and IGFBP-3 mRNA levels. Cysteamine 0-2 insulin like growth factor 1 Sus scrofa 58-63 18553891-8 2008 CS supplementation has tissue-specific regulation of GHR, IGF-I, IGF-IR, and IGFBP-3 mRNA levels. Cysteamine 0-2 insulin like growth factor 1 receptor Sus scrofa 65-71 18463844-2 2008 The epithelial pantetheinase vanin-1 is proinflammatory and cytoprotective via cysteamine release in some tissues. Cysteamine 79-89 vanin 1 Mus musculus 29-36 18463844-6 2008 RESULTS: The vanin-1/cysteamine pathway contributes to the protection of islet beta cells from streptozotocin-induced death in vitro and in vivo. Cysteamine 21-31 vanin 1 Mus musculus 13-20 18463844-10 2008 CONCLUSIONS/INTERPRETATION: This study unravels a major cytoprotective role of cysteamine for islet cells and suggests that modulation of pantetheinase activity may offer alternative strategies to maintain islet cell homeostasis. Cysteamine 79-89 vanin 1 Mus musculus 138-151 18391186-5 2008 Both the behavioral and the electrophysiological phenotypes were mimicked in wild-type mice through application of the somatostatin-depleting substance cysteamine prior to fear training, whereas no further deficits were observed upon application in the somatostatin null mutants. Cysteamine 152-162 somatostatin Mus musculus 119-131 18486145-6 2008 Similar to hQC, h-isoQC was competitively inhibited by imidazoles and cysteamines. Cysteamine 70-81 glutaminyl-peptide cyclotransferase like Homo sapiens 16-23 18006287-1 2008 The cysteamine (CA) was bound onto surface of the pretreated glassy carbon electrode (GC) with cyclic voltammetry (CV). Cysteamine 4-14 S100 calcium binding protein A12 Homo sapiens 16-18 18006287-1 2008 The cysteamine (CA) was bound onto surface of the pretreated glassy carbon electrode (GC) with cyclic voltammetry (CV). Cysteamine 4-14 S100 calcium binding protein A12 Homo sapiens 86-88 18006287-2 2008 Gold nanoparticles were self-assembled to the electrode binding with cysteamine via strong Au-S covalent bond to fabricate the nano-Au self-assembled modified electrode (nano-Au/CA/GC). Cysteamine 69-79 S100 calcium binding protein A12 Homo sapiens 178-183 17676396-4 2008 In comparison with ethanolamine, these 40 genes changed by cysteamine only may represent ulcer-associated genes, such as endothelin receptor B, endothelin 1, caspase 3, transcription factors egr-1, Sp1, the angiogenic growth factors vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF), and especially egr-1 and endothelin receptor B (ETRB) showed no changes in ileum and colon. Cysteamine 59-69 endothelin 1 Rattus norvegicus 144-156 18206125-1 2008 Free cysteamine levels in mouse tissues have been strictly correlated to the presence of membrane-bound pantetheinase activity encoded by Vanin-1. Cysteamine 5-15 vanin 1 Mus musculus 138-145 17676396-4 2008 In comparison with ethanolamine, these 40 genes changed by cysteamine only may represent ulcer-associated genes, such as endothelin receptor B, endothelin 1, caspase 3, transcription factors egr-1, Sp1, the angiogenic growth factors vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF), and especially egr-1 and endothelin receptor B (ETRB) showed no changes in ileum and colon. Cysteamine 59-69 caspase 3 Rattus norvegicus 158-167 17676396-4 2008 In comparison with ethanolamine, these 40 genes changed by cysteamine only may represent ulcer-associated genes, such as endothelin receptor B, endothelin 1, caspase 3, transcription factors egr-1, Sp1, the angiogenic growth factors vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF), and especially egr-1 and endothelin receptor B (ETRB) showed no changes in ileum and colon. Cysteamine 59-69 early growth response 1 Rattus norvegicus 191-196 17676396-4 2008 In comparison with ethanolamine, these 40 genes changed by cysteamine only may represent ulcer-associated genes, such as endothelin receptor B, endothelin 1, caspase 3, transcription factors egr-1, Sp1, the angiogenic growth factors vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF), and especially egr-1 and endothelin receptor B (ETRB) showed no changes in ileum and colon. Cysteamine 59-69 vascular endothelial growth factor A Rattus norvegicus 269-273 17676396-4 2008 In comparison with ethanolamine, these 40 genes changed by cysteamine only may represent ulcer-associated genes, such as endothelin receptor B, endothelin 1, caspase 3, transcription factors egr-1, Sp1, the angiogenic growth factors vascular endothelial growth factor (VEGF) and platelet-derived growth factor (PDGF), and especially egr-1 and endothelin receptor B (ETRB) showed no changes in ileum and colon. Cysteamine 59-69 early growth response 1 Rattus norvegicus 333-338 17656571-4 2007 Namely, we found an enhanced expression and release of ET-1 within 15-30 min after the administration of duodenal ulcerogen cysteamine, resulting in local ischemia that triggers the expression of hypoxia-inducible factors (HIF-1alpha). Cysteamine 124-134 endothelin 1 Homo sapiens 55-59 17638022-5 2008 Increased serum growth hormone levels were attributed to enhanced growth hormone production by the prolactinoma and somatostatin inhibition by cysteamine. Cysteamine 143-153 growth hormone 1 Homo sapiens 16-30 17999914-2 2008 Cystamine, an oxidized dimer of cysteamine inhibits the transamidation activity of TGase2. Cysteamine 32-42 transglutaminase 2 Rattus norvegicus 83-89 17656571-4 2007 Namely, we found an enhanced expression and release of ET-1 within 15-30 min after the administration of duodenal ulcerogen cysteamine, resulting in local ischemia that triggers the expression of hypoxia-inducible factors (HIF-1alpha). Cysteamine 124-134 hypoxia inducible factor 1 subunit alpha Homo sapiens 223-233 17696487-0 2007 Tissue-specific effect of dietary cysteamine on expression of adiponectin receptors in rats. Cysteamine 34-44 adiponectin, C1Q and collagen domain containing Rattus norvegicus 62-73 17696487-3 2007 The objective of the present study was therefore to investigate the effect of dietary cysteamine on the expression of AdipoR1/R2 in different tissues, in association with the alterations in endocrine and metabolic status. Cysteamine 86-96 adiponectin receptor 1 Rattus norvegicus 118-125 17696487-8 2007 Cysteamine supplementation increased mRNA expression of AdipoR1 in adipose tissue, gastrocnemius, and soleus muscle as well as that of AdipoR2 in soleus muscle and adipose tissue. Cysteamine 0-10 adiponectin receptor 2 Rattus norvegicus 135-142 17696487-11 2007 In conclusion, dietary supplementation of cysteamine modulates the endocrine and metabolic status of rats, which may involve the tissue-specific responses of adiponectin receptors at the level of mRNA transcription. Cysteamine 42-52 adiponectin, C1Q and collagen domain containing Rattus norvegicus 158-169 17696487-8 2007 Cysteamine supplementation increased mRNA expression of AdipoR1 in adipose tissue, gastrocnemius, and soleus muscle as well as that of AdipoR2 in soleus muscle and adipose tissue. Cysteamine 0-10 adiponectin receptor 1 Rattus norvegicus 56-63 17712144-0 2007 Effect of thiol-containing molecule cysteamine on the induction of inducible nitric oxide synthase in hepatocytes. Cysteamine 36-46 nitric oxide synthase 2 Rattus norvegicus 67-98 17712144-5 2007 We examined whether cysteamine influences the induction of iNOS in hepatocytes. Cysteamine 20-30 nitric oxide synthase 2 Rattus norvegicus 59-63 17712144-10 2007 Cysteamine also decreased the levels of iNOS protein and mRNA. Cysteamine 0-10 nitric oxide synthase 2 Rattus norvegicus 40-44 17712144-11 2007 Transfection experiments revealed that cysteamine decreased the transactivation activity of the iNOS promoter. Cysteamine 39-49 nitric oxide synthase 2 Rattus norvegicus 96-100 17712144-13 2007 Furthermore, cysteamine decreased the mRNA levels of the NFkappaB subunit p65 but increased those of the inhibitory protein IkappaB. Cysteamine 13-23 synaptotagmin 1 Rattus norvegicus 74-77 17712144-14 2007 CONCLUSIONS: These findings suggest that cysteamine inhibits iNOS induction at the step of NFkappaB activation. Cysteamine 41-51 nitric oxide synthase 2 Rattus norvegicus 61-65 17477978-5 2007 Depletion of both somatostatin and serotonin in naive rats impaired performance, with differences in the impairments that depended on the dose of cysteamine. Cysteamine 146-156 somatostatin Rattus norvegicus 18-30 17312006-8 2007 Vanin genes code for a pantetheinase involved in the production of cysteamine, a key regulator of host responses to inflammatory stimuli. Cysteamine 67-77 vanin 1 Mus musculus 23-36 17585979-8 2007 Vanin-1 could be important for CFB-mediated hepatoprotection because this protein is involved in the synthesis of cysteamine and cystamine. Cysteamine 114-124 vanin 1 Mus musculus 0-7 17575178-4 2007 Cysteamine (CS) is a sulfhydryl reducing agent that is known as a depletory agent of somatostatin. Cysteamine 0-10 somatostatin 1 Gallus gallus 85-97 17575178-4 2007 Cysteamine (CS) is a sulfhydryl reducing agent that is known as a depletory agent of somatostatin. Cysteamine 12-14 somatostatin 1 Gallus gallus 85-97 17575178-8 2007 The number of somatostatin-positive cells in the duodenum was reduced (P < 0.05) after CS treatment. Cysteamine 90-92 somatostatin 1 Gallus gallus 14-26 17575178-10 2007 The expression of somatostatin mRNA increased (P < 0.05) compared with that of the control group at 5 wk after immunization in broilers receiving CS+NDV or NDV alone. Cysteamine 149-151 somatostatin 1 Gallus gallus 18-30 17575178-11 2007 The results suggest that CS can induce proliferation and differentiation of IgA-positive cells and iIEL in the intestinal mucosa of chickens by reducing the number of somatostatin-positive cells. Cysteamine 25-27 somatostatin 1 Gallus gallus 167-179 17254730-3 2007 The cTnT receptor molecule was covalently immobilized on a gold substrate via a self-assembled monolayer (SAM) of thiols by using cysteamine-coupling chemistry. Cysteamine 130-140 troponin T2, cardiac type Homo sapiens 4-8 17383978-4 2007 In the folding procedure, it was found that cysteamine and cystamine with positive charge were effective to improve the folding yield of human Fab. Cysteamine 44-54 FA complementation group B Homo sapiens 143-146 17279683-2 2007 The objective of this work was to assess the intracellular Cd2+ concentration in human breast cancer MCF-7 cells treated with cadmium telluride (CdTe) and core/shell cadmium selenide/zinc sulfide (CdSe/ZnS) nanoparticles capped with mercaptopropionic acid (MPA), cysteamine (Cys), or N-acetylcysteine (NAC) conjugated to cysteamine. Cysteamine 263-273 CD2 molecule Homo sapiens 59-62 17279683-2 2007 The objective of this work was to assess the intracellular Cd2+ concentration in human breast cancer MCF-7 cells treated with cadmium telluride (CdTe) and core/shell cadmium selenide/zinc sulfide (CdSe/ZnS) nanoparticles capped with mercaptopropionic acid (MPA), cysteamine (Cys), or N-acetylcysteine (NAC) conjugated to cysteamine. Cysteamine 275-278 CD2 molecule Homo sapiens 59-62 17279683-2 2007 The objective of this work was to assess the intracellular Cd2+ concentration in human breast cancer MCF-7 cells treated with cadmium telluride (CdTe) and core/shell cadmium selenide/zinc sulfide (CdSe/ZnS) nanoparticles capped with mercaptopropionic acid (MPA), cysteamine (Cys), or N-acetylcysteine (NAC) conjugated to cysteamine. Cysteamine 321-331 CD2 molecule Homo sapiens 59-62 17166669-6 2007 In addition, cysteamine showed neuroprotective effects by way of enhancing central and serum brain derived neurotrophic factor (BDNF) that has been proved to be altered in patients with schizophrenia. Cysteamine 13-23 brain derived neurotrophic factor Homo sapiens 93-126 17229997-8 2007 Interestingly, up-regulation of Lcn2 expression after H(2)O(2) treatment was canceled by the addition of the anti-oxidants, dimethylsulfoxide or cysteamine. Cysteamine 145-155 lipocalin 2 Homo sapiens 32-36 17166669-6 2007 In addition, cysteamine showed neuroprotective effects by way of enhancing central and serum brain derived neurotrophic factor (BDNF) that has been proved to be altered in patients with schizophrenia. Cysteamine 13-23 brain derived neurotrophic factor Homo sapiens 128-132 17166669-11 2007 Finally, cysteamine treatment was found to decrease weight gain, cataleptic behavior, and serum prolactin levels, which are the major beneficial properties of contemporary atypical antipsychotics. Cysteamine 9-19 prolactin Homo sapiens 96-105 17101082-0 2006 [Cysteamine restores intracellular dynamics and BDNF secretion in Huntington"s disease]. Cysteamine 1-11 brain derived neurotrophic factor Homo sapiens 48-52 16933927-1 2006 The combination of HgF2 and 2-aminoethanethiol (AET, with some AET.HCl present) yielded a cyclic tetranuclear thiolate, [Hg4Cl4(SCH2CH2NH2)4] (1), with alternating Hg and S atoms. Cysteamine 48-51 GINGF2 Homo sapiens 19-23 16413736-4 2006 In the developed method the two main decomposition products of sodium cysteamine phosphate, cystamine and cysteamine, can be determined with LOQs of 30 microg/ml (0.2%) and 16 microg/ml (0.1%), respectively. Cysteamine 70-80 TARBP2 subunit of RISC loading complex Homo sapiens 141-145 16604191-0 2006 Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase. Cysteamine 14-24 brain derived neurotrophic factor Mus musculus 50-54 16484680-1 2006 Previously, we demonstrated that cysteamine releases endothelin-1 in the rat duodenal mucosa, followed by increased expression of early growth response factor-1 (egr-1). Cysteamine 33-43 endothelin 1 Rattus norvegicus 53-65 16484680-1 2006 Previously, we demonstrated that cysteamine releases endothelin-1 in the rat duodenal mucosa, followed by increased expression of early growth response factor-1 (egr-1). Cysteamine 33-43 early growth response 1 Rattus norvegicus 130-160 16484680-1 2006 Previously, we demonstrated that cysteamine releases endothelin-1 in the rat duodenal mucosa, followed by increased expression of early growth response factor-1 (egr-1). Cysteamine 33-43 early growth response 1 Rattus norvegicus 162-167 16484680-4 2006 An antisense oligonucleotide to egr-1 was used to inhibit the synthesis of Egr-1 and to determine its effect on ulcer formation in the rat model of cysteamine-induced duodenal ulceration. Cysteamine 148-158 early growth response 1 Rattus norvegicus 32-37 16484680-7 2006 Cysteamine induced phosphorylation of ERK1/2 and enhanced the synthesis of bFGF, PDGF, and VEGF in the preulcerogenic stages of duodenal ulceration, whereas egr-1 antisense oligonucleotide markedly decreased the expression of these growth factors in the duodenal mucosa. Cysteamine 0-10 mitogen activated protein kinase 3 Rattus norvegicus 38-44 16484680-7 2006 Cysteamine induced phosphorylation of ERK1/2 and enhanced the synthesis of bFGF, PDGF, and VEGF in the preulcerogenic stages of duodenal ulceration, whereas egr-1 antisense oligonucleotide markedly decreased the expression of these growth factors in the duodenal mucosa. Cysteamine 0-10 fibroblast growth factor 2 Rattus norvegicus 75-79 16484680-7 2006 Cysteamine induced phosphorylation of ERK1/2 and enhanced the synthesis of bFGF, PDGF, and VEGF in the preulcerogenic stages of duodenal ulceration, whereas egr-1 antisense oligonucleotide markedly decreased the expression of these growth factors in the duodenal mucosa. Cysteamine 0-10 vascular endothelial growth factor A Rattus norvegicus 91-95 16484680-8 2006 We also demonstrated that Egr-1 expression relates to the ulcerogenic effect of cysteamine because these actions were not exerted by the toxic analog ethanolamine. Cysteamine 80-90 early growth response 1 Rattus norvegicus 26-31 16604191-0 2006 Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase. Cysteamine 14-24 DnaJ heat shock protein family (Hsp40) member B2 Homo sapiens 81-86 16604191-7 2006 We demonstrate that cysteamine, the FDA-approved reduced form of cystamine, is neuroprotective in HD mice by increasing BDNF levels in brain. Cysteamine 20-30 brain derived neurotrophic factor Mus musculus 120-124 16604191-8 2006 Finally, cysteamine increases serum levels of BDNF in mouse and primate models of HD. Cysteamine 9-19 brain derived neurotrophic factor Mus musculus 46-50 15958186-6 2005 For comparison purposes, the same hCBS reaction was monitored via a radioactive single time point assay using 14C-(C-1)-labeled L-serine and cysteamine as substrates, counting the thialysine product, following ion exchange chromatography. Cysteamine 141-151 cystathionine beta-synthase Homo sapiens 34-38 16157371-7 2006 The NH2-PEG-Acr monomer can be formed by coupling cysteamine to PEG-DA by a conjugate addition reaction. Cysteamine 50-60 acrosin Homo sapiens 12-15 16139950-8 2005 CRFR1 antagonist (CP154526) or SS antagonist (cysteamine) markedly blocked hypoxia-reduced pituitary GH mRNA and hypoxia-activated hepatic IGF-I mRNA, and further reduced hypoxia-reduced plasma IGF. Cysteamine 46-56 insulin-like growth factor 1 Rattus norvegicus 139-144 16139950-8 2005 CRFR1 antagonist (CP154526) or SS antagonist (cysteamine) markedly blocked hypoxia-reduced pituitary GH mRNA and hypoxia-activated hepatic IGF-I mRNA, and further reduced hypoxia-reduced plasma IGF. Cysteamine 46-56 insulin-like growth factor 1 Rattus norvegicus 139-142 15778430-0 2005 Enhanced ghrelin secretion in rats with cysteamine-induced duodenal ulcers. Cysteamine 40-50 ghrelin and obestatin prepropeptide Rattus norvegicus 9-16 15778430-2 2005 Cysteamine inhibits the release of somatostatin and induces the formation of duodenal ulcers in rats. Cysteamine 0-10 somatostatin Rattus norvegicus 35-47 15778430-3 2005 The present study was conducted to investigate the dynamics of ghrelin secretion in rats treated with cysteamine. Cysteamine 102-112 ghrelin and obestatin prepropeptide Rattus norvegicus 63-70 15778430-6 2005 Even at the time points of 2 and 10 h after the first dose of cysteamine, at which time no significant ulcer formation or antral neutrophil accumulation was yet noted, a significant increase in the plasma ghrelin level and decrease in the gastric ghrelin level were observed. Cysteamine 62-72 ghrelin and obestatin prepropeptide Rattus norvegicus 205-212 15778430-6 2005 Even at the time points of 2 and 10 h after the first dose of cysteamine, at which time no significant ulcer formation or antral neutrophil accumulation was yet noted, a significant increase in the plasma ghrelin level and decrease in the gastric ghrelin level were observed. Cysteamine 62-72 ghrelin and obestatin prepropeptide Rattus norvegicus 247-254 15778430-9 2005 In conclusion, an increase in the plasma ghrelin level precedes the formation of duodenal ulcers in rats treated with cysteamine. Cysteamine 118-128 ghrelin and obestatin prepropeptide Rattus norvegicus 41-48 15987120-3 2005 The PT group immobilized on the SAM of AET acts as an effective mediator for the electron transfer (ET) between the electrode and the FAD center of freely diffusing GOx in solution. Cysteamine 39-42 hydroxyacid oxidase 1 Homo sapiens 165-168 16601878-3 2006 In the current study, we compared the catalytic rate constants for the conversion of palmitoyl-CoA (a PPT substrate) and cystine (which accumulates in cystinosis) by cysteamine. Cysteamine 166-176 palmitoyl-protein thioesterase 1 Homo sapiens 102-105 16601878-6 2006 A modest effect of cysteamine (and two related aminothiols, WR 1065 and dimethylaminoethanethiol, DMAET) on PPT substrate accumulation in INCL lymphoblasts was observed. Cysteamine 19-29 palmitoyl-protein thioesterase 1 Homo sapiens 108-111 16797865-0 2006 Cysteamine-related agents could be potential antidepressants through increasing central BDNF levels. Cysteamine 0-10 brain derived neurotrophic factor Mus musculus 88-92 16797865-6 2006 Cysteamine is a natural product of cells and constitutes the terminal region of the CoA molecule. Cysteamine 0-10 HPS3, biogenesis of lysosomal organelles complex 2 subunit 1 Mus musculus 84-87 16797865-7 2006 Recent work has found that cysteamine and a related agent, cystamine, have neuroprotective effects in Huntington"s disease (HD) mice, through enhancing central BDNF levels. Cysteamine 27-37 brain derived neurotrophic factor Mus musculus 160-164 16797865-8 2006 Furthermore, cystamine or cysteamine injection could increase serum BDNF levels in wild-type mice as well as HD mice. Cysteamine 26-36 brain derived neurotrophic factor Mus musculus 68-72 16133039-6 2005 Cysteamine ingestion resulted in mean MAO and PAO significantly higher than mean BAO, both before and during esomeprazole therapy. Cysteamine 0-10 spermine oxidase Homo sapiens 46-49 16133039-7 2005 PAO was usually within 60 min of cysteamine ingestion. Cysteamine 33-43 spermine oxidase Homo sapiens 0-3 15958186-2 2005 This assay relies upon the finding that hCBS will take cysteamine in place of L-homocysteine, thereby producing thialysine. Cysteamine 55-65 cystathionine beta-synthase Homo sapiens 40-44 15958186-5 2005 Using this four-enzyme couple, we find that Km(app) = 1.2+/-0.2 mM for L-serine and 5.6+/-2.2 mM for cysteamine, with kcat = 1.3+/-0.1s(-1) for the formation of thialysine by hCBS. Cysteamine 101-111 cystathionine beta-synthase Homo sapiens 175-179 15958186-8 2005 These numbers indicate that, although it possesses a shortened carbon chain and lacks a carboxyl group, cysteamine displays a catalytic efficiency (kcat/Km) with hCBS that is within an order of magnitude of that observed with its natural thiol cosubstrate, L-homocysteine. Cysteamine 104-114 cystathionine beta-synthase Homo sapiens 162-166 15581620-4 2004 The pre-incubation with glutathione ethyl ester or cysteamine recovered oxidative status and was effective in significantly reducing glutamate-increased tissue TGase. Cysteamine 51-61 transglutaminase 1 Homo sapiens 160-165 15626613-2 2005 Mono-enzyme (GOx) and monolayer/bilayer bienzyme (GOx/HRP) bioelectrodes were prepared by immobilizing the enzymes onto gold nanotubes surfaces modified with mercaptoethylamine. Cysteamine 158-176 hydroxyacid oxidase 1 Homo sapiens 50-53 18969709-1 2004 The suitability of colloidal-gold cysteamine-modified carbon paste electrodes (nAu-Cyst-CPE) for the electrochemical determination of sulphur-containing compounds is illustrated in this work by determining the amino acid methionine in real samples, as well as a methionine-based peptide. Cysteamine 34-44 carboxypeptidase E Homo sapiens 88-91 14644768-3 2004 The cysteine analog, cysteamine, but not cysteine metabolites or thiol reagents, was also effective in increasing CDO. Cysteamine 21-31 cysteine dioxygenase type 1 Rattus norvegicus 114-117 15282320-2 2004 Here we show that Vanin-1(-/-) mice, which lack cysteamine in tissues, exhibit resistance to oxidative injury induced by whole-body gamma-irradiation or paraquat. Cysteamine 48-58 vanin 1 Mus musculus 18-25 15282320-4 2004 The better tolerance of the Vanin-1(-/-) mice is associated with an enhanced gamma-glutamylcysteine synthetase activity in liver, probably due to the absence of cysteamine and leading to elevated stores of glutathione (GSH), the most potent cellular antioxidant. Cysteamine 161-171 vanin 1 Mus musculus 28-35 15047156-0 2004 Cysteamine alters redox state, HIF-1alpha transcriptional interactions and reduces duodenal mucosal oxygenation: novel insight into the mechanisms of duodenal ulceration. Cysteamine 0-10 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 31-41 15047156-1 2004 Our recent studies demonstrated a critical role of enhanced transcriptional activity of early growth response factor-1 (Egr-1) in early stages of cysteamine-induced duodenal ulcer in rats. Cysteamine 146-156 early growth response 1 Rattus norvegicus 88-118 15047156-1 2004 Our recent studies demonstrated a critical role of enhanced transcriptional activity of early growth response factor-1 (Egr-1) in early stages of cysteamine-induced duodenal ulcer in rats. Cysteamine 146-156 early growth response 1 Rattus norvegicus 120-125 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 21-31 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 hypoxia inducible factor 1 subunit alpha Rattus norvegicus 81-91 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 early growth response 1 Rattus norvegicus 110-115 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 YY1 transcription factor Rattus norvegicus 177-182 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 nuclear factor, erythroid 2 Rattus norvegicus 184-189 15047156-4 2004 Cysteamine increased HIF-1alpha expression, its binding to DNA, and enhanced the HIF-1alpha interactions with Egr-1 and other transcription factors (e.g., AP-1, AP-2, L-III BP, NF-E1, NF-E2, STAT4, and MRE), their binding to DNA. Cysteamine 0-10 signal transducer and activator of transcription 4 Rattus norvegicus 191-196 13679060-1 2003 Recent studies from our laboratory demonstrated that Egr-1 is upregulated in the rat duodenal mucosa during cysteamine-induced duodenal ulceration and that antisense egr-1 oligonucleotide aggravates the duodenal ulcers. Cysteamine 108-118 early growth response 1 Rattus norvegicus 53-58 14966568-5 2004 To explore this point, we developed Vanin-1-deficient mice that lack free cysteamine. Cysteamine 74-84 vanin 1 Mus musculus 36-43 14651726-5 2003 RESULTS: Cysteamine was rapidly cleared from the plasma (mean CL/F = 32.3 ml min(-1) kg(-1), range = 17.3-52.2), appeared to be extensively distributed (mean Vss/F = 15.1 l, range 2.7-32.3) and exhibited a mean Tmax of 1.4 h. White blood cell cystine content post-dosing was significantly decreased compared with pre- and post-dose values (average decrement approximately 47%). Cysteamine 9-19 CD59 molecule (CD59 blood group) Homo sapiens 77-83 13679060-1 2003 Recent studies from our laboratory demonstrated that Egr-1 is upregulated in the rat duodenal mucosa during cysteamine-induced duodenal ulceration and that antisense egr-1 oligonucleotide aggravates the duodenal ulcers. Cysteamine 108-118 early growth response 1 Rattus norvegicus 166-171 13679060-2 2003 This study was aimed to determine the effects of cysteamine on redox-sensitive Egr-1 transcriptional activity and on other thiol-containing proteins such as redox factor-1 (Ref-1) and thioredoxin (Trx). Cysteamine 49-59 early growth response 1 Rattus norvegicus 79-84 13679060-3 2003 Here we demonstrate for the first time that cysteamine increases the expression and nuclear translocation of Egr-1, Ref-1, and Trx, and activates binding of Egr-1 to DNA. Cysteamine 44-54 early growth response 1 Rattus norvegicus 109-114 13679060-3 2003 Here we demonstrate for the first time that cysteamine increases the expression and nuclear translocation of Egr-1, Ref-1, and Trx, and activates binding of Egr-1 to DNA. Cysteamine 44-54 apurinic/apyrimidinic endodeoxyribonuclease 1 Rattus norvegicus 116-121 13679060-3 2003 Here we demonstrate for the first time that cysteamine increases the expression and nuclear translocation of Egr-1, Ref-1, and Trx, and activates binding of Egr-1 to DNA. Cysteamine 44-54 thioredoxin 1 Rattus norvegicus 127-130 13679060-3 2003 Here we demonstrate for the first time that cysteamine increases the expression and nuclear translocation of Egr-1, Ref-1, and Trx, and activates binding of Egr-1 to DNA. Cysteamine 44-54 early growth response 1 Rattus norvegicus 157-162 13679060-4 2003 Moreover, we also show that Egr-1 forms a complex with other redox-sensitive transcription factors (e.g., AP-1, AP-2, NFATc, Sp1, PAX-5, MTF-1, c-Myb, and CREB) in rat duodenal mucosa and that cysteamine enhances the formation of these complexes. Cysteamine 193-203 early growth response 1 Rattus norvegicus 28-33 12713918-2 2003 Glucose oxidase (Gox) was immobilised onto preformed self-assembled monolayers (SAMs) (mercaptoethylamine or mercaptopropionic acid) on electroless gold via cross-linking with glutaraldehyde or covalent attachment by carbodiimide coupling. Cysteamine 87-105 hydroxyacid oxidase 1 Homo sapiens 0-15 14674462-5 2003 Comparative studies with short-chain alkanethiols, e.g., cysteamine and 2-mercaptoethanol, revealed an evidently different mode of adsorption of SOx on these layers, onto which SOx was not catalytically active. Cysteamine 57-67 sulfite oxidase Gallus gallus 145-148 12713918-2 2003 Glucose oxidase (Gox) was immobilised onto preformed self-assembled monolayers (SAMs) (mercaptoethylamine or mercaptopropionic acid) on electroless gold via cross-linking with glutaraldehyde or covalent attachment by carbodiimide coupling. Cysteamine 87-105 hydroxyacid oxidase 1 Homo sapiens 17-20 12419525-0 2002 Cysteamine pre-treatment reduces pentylenetetrazol-induced plasticity and epileptiform discharge in the CA1 region of rat hippocampal slices. Cysteamine 0-10 carbonic anhydrase 1 Rattus norvegicus 104-107 12504379-3 2003 Deprotection furnished the allyl glycosides which were converted into cysteamine-spacered ligands, activated with thiophosgene and subsequently linked to bovine serum albumin. Cysteamine 70-80 albumin Homo sapiens 161-174 12419525-1 2002 The effects of prior treatment of cysteamine, a somatostatin inhibitor, on pentylenetetrazol (PTZ) induced epileptic and plastic changes in CA1 excitability were examined. Cysteamine 34-44 carbonic anhydrase 1 Rattus norvegicus 140-143 12419525-4 2002 Cysteamine pre-treatment decreased baseline CA1 population spike amplitude following high intensity stimulation of Schaffer collaterals. Cysteamine 0-10 carbonic anhydrase 1 Rattus norvegicus 44-47 16290723-1 2002 Liquid-liquid interface of water-hexane provides a unique reaction environment in which CdS nanoparticles capped with mercaptoethylamine could be linked together to form a homodimer with a divalent acid chloride, sebacoyl chloride. Cysteamine 118-136 CDP-diacylglycerol synthase 1 Homo sapiens 88-91 12370309-12 2002 A preliminary therapeutic trial using an oral administration of cysteamine was carried out and demonstrated the efficiency of this treatment for cystine clearance in Ctns(-/-) mice. Cysteamine 64-74 cystinosis, nephropathic Mus musculus 166-170 12372700-0 2002 The ability of hippocampal CA1 area for induction of long-term potentiation is persistently reduced by prior treatment with cysteamine: an in vitro study. Cysteamine 124-134 carbonic anhydrase 1 Rattus norvegicus 27-30 12372700-1 2002 Using field potential recording in the CA1 region of hippocampal slices from rats injected with cysteamine (200 mg/kg, s.c.), changes in activity and plasticity of Schaffer collateral-CA1 pyramidal cell synapses were examined. Cysteamine 96-106 carbonic anhydrase 1 Rattus norvegicus 39-42 12372700-1 2002 Using field potential recording in the CA1 region of hippocampal slices from rats injected with cysteamine (200 mg/kg, s.c.), changes in activity and plasticity of Schaffer collateral-CA1 pyramidal cell synapses were examined. Cysteamine 96-106 carbonic anhydrase 1 Rattus norvegicus 184-187 12372700-4 2002 It is concluded that cysteamine can entail lasting modifications in susceptibility of hippocampal CA1 for synaptic plasticity induced by tetanus. Cysteamine 21-31 carbonic anhydrase 1 Rattus norvegicus 98-101 16290723-2 2002 Prior to the reaction, mercaptoethylamine-capped CdS in aqueous solution was purified by dialysis and freeze-drying. Cysteamine 23-41 CDP-diacylglycerol synthase 1 Homo sapiens 49-52 11961490-7 2002 The glucose (18 mM)-enhanced CCK-stimulated secretions were much higher in the cysteamine-treated pancreas than in the normal pancreas, which was dose-dependently reduced by exogenous somatostatin (30, 100 pM). Cysteamine 79-89 cholecystokinin Rattus norvegicus 29-32 11642020-4 2001 In these experimental conditions, a prodrug of N-acetylcysteine and beta-mercaptoethylamine, I-152 demonstrated a potent anti-HIV activity, increased intracellular GSH level, and decreased TNF-alpha production. Cysteamine 68-91 tumor necrosis factor Homo sapiens 189-198 11698397-4 2002 Cysteine and cysteamine were highly reactive: the K(m) for cysteine was 1.4 mm and V(max) (with 40 microg/ml SOD) 35 microm/min; the equivalent values for cysteamine (with 20 microg/ml SOD) were 1.4 mm and 36 microm/min. Cysteamine 13-23 superoxide dismutase 1 Homo sapiens 109-112 11698397-4 2002 Cysteine and cysteamine were highly reactive: the K(m) for cysteine was 1.4 mm and V(max) (with 40 microg/ml SOD) 35 microm/min; the equivalent values for cysteamine (with 20 microg/ml SOD) were 1.4 mm and 36 microm/min. Cysteamine 13-23 superoxide dismutase 1 Homo sapiens 185-188 12232504-2 2002 We previously demonstrated that, in cultured rat astroglia, cysteamine (CSH) upregulates heme oxygenase-1 (HO-1) and promotes the transformation of normal mitochondria into CA-like inclusions. Cysteamine 60-70 heme oxygenase 1 Rattus norvegicus 89-105 12232504-2 2002 We previously demonstrated that, in cultured rat astroglia, cysteamine (CSH) upregulates heme oxygenase-1 (HO-1) and promotes the transformation of normal mitochondria into CA-like inclusions. Cysteamine 60-70 heme oxygenase 1 Rattus norvegicus 107-111 11042271-1 2000 Pantetheinase (EC 3.5.1.-) is an ubiquitous enzyme which in vitro has been shown to recycle pantothenic acid (vitamin B5) and to produce cysteamine, a potent anti-oxidant. Cysteamine 137-147 vanin 1 Mus musculus 0-13 11325259-2 2001 N-Allyl glycosides of various oligosaccharides were photochemically coupled with cysteamine to yield amino-terminated thioether spacers, which were accepted by transglutaminase to transamidate the side-chain gamma-carboxamide group in the dipeptide Z-Gln-Gly. Cysteamine 81-91 transglutaminase 1 Homo sapiens 160-176 11595457-3 2001 The initial molecular event in duodenal ulceration seems to be the organ-specific early release of ET-1 in the pre-ulcerogenic stages after the administration of duodenal ulcerogen cysteamine in rats. Cysteamine 181-191 endothelin 1 Rattus norvegicus 99-103 11595457-7 2001 Cysteamine enhanced ET-B receptor gene expression in 30 min, while transcription factors (MAX, STAT 3) showed increased expression in 12 h. We recently also initiated gene therapy studies to enhance the local synthesis of PDGF and VEGF to accelerate duodenal ulcer healing, using a single dose of naked DNA (ND) or adenoviral (AV) vectors of VEGF and PDGF in rats with cysteamine-induced duodenal ulcers. Cysteamine 0-10 endothelin receptor type B Rattus norvegicus 20-24 11087332-6 2000 Next, these reagents were applied to the anchoring of a C-terminally cysteamine-modified 8 kDa polypeptide that comprises the extracellular N-terminal domain of the human thrombin receptor, a transmembrane protease-activated receptor (PAR-1). Cysteamine 69-79 coagulation factor II thrombin receptor Homo sapiens 235-240 11438495-4 2001 Cysteamine-induced ulceration in EGF(-/-) mice was used to examine its role in mucosal cytoprotection. Cysteamine 0-10 epidermal growth factor Mus musculus 33-36 11438495-8 2001 Adult EGF(-/-) mice displayed more severe lesions in response to cysteamine treatment compared with wild-type counterparts, although triple null mice were not more susceptible to dextran sulfate sodium-induced colitis, suggesting a differential role for these ligands in the injury response. Cysteamine 65-75 epidermal growth factor Mus musculus 6-9 11595429-0 2001 Susceptibility of dopamine D5 receptor targeted mice to cysteamine. Cysteamine 56-66 dopamine receptor D5 Mus musculus 18-38 10583725-1 1999 Cysteamine, a potent depletor of prolactin and somatostatin, was used to determine the role of prolactin and somatostatin in the control of central dopamine neurones in prepubertal rats. Cysteamine 0-10 prolactin Rattus norvegicus 33-42 10884527-3 2000 Both the prevention of this inhibitory effect by cysteamine pretreatment and the stimulation-evoked rise of plasma somatostatin-like immunoreactivity in the two species suggest a mediator role of neural somatostatin. Cysteamine 49-59 somatostatin Rattus norvegicus 203-215 11037578-1 2000 Previously, we reported that X-irradiation enhanced the signal decay of a spin probe injected into whole mice measured by in vivo ESR, and that the observed enhancement was suppressed by the pre-administration of cysteamine, a radioprotector [Miura, Y., Anzai, K., Urano, S. and Ozawa, T. (1997) Free Rad. Cysteamine 213-223 esterase 5 regulator Mus musculus 130-133 11037578-1 2000 Previously, we reported that X-irradiation enhanced the signal decay of a spin probe injected into whole mice measured by in vivo ESR, and that the observed enhancement was suppressed by the pre-administration of cysteamine, a radioprotector [Miura, Y., Anzai, K., Urano, S. and Ozawa, T. (1997) Free Rad. Cysteamine 213-223 Ras-related associated with diabetes Mus musculus 301-304 10807401-2 2000 Our experiments revealed accelerated healing, without decreased gastric acid secretion, of chronic cysteamine-induced duodenal ulcers in rats treated daily for 3 weeks with intragastric administration of bFGF, PDGF or VEGF. Cysteamine 99-109 fibroblast growth factor 2 Rattus norvegicus 204-208 10807401-2 2000 Our experiments revealed accelerated healing, without decreased gastric acid secretion, of chronic cysteamine-induced duodenal ulcers in rats treated daily for 3 weeks with intragastric administration of bFGF, PDGF or VEGF. Cysteamine 99-109 vascular endothelial growth factor A Rattus norvegicus 218-222 10807401-6 2000 Indeed, the duodenal ulcerogen cysteamine, but not its nonulcerogen and toxic analogue ethanolamine, rapidly increased duodenal (but not gastric) mucosal levels of ET-1, which was followed by enhanced expression of Egr-1 and a decrease in Sp1 in the preulcerogenic stage of duodenal ulceration. Cysteamine 31-41 endothelin 1 Rattus norvegicus 164-168 10807401-6 2000 Indeed, the duodenal ulcerogen cysteamine, but not its nonulcerogen and toxic analogue ethanolamine, rapidly increased duodenal (but not gastric) mucosal levels of ET-1, which was followed by enhanced expression of Egr-1 and a decrease in Sp1 in the preulcerogenic stage of duodenal ulceration. Cysteamine 31-41 early growth response 1 Rattus norvegicus 215-220 10583725-6 1999 A single injection of rat prolactin (0.01, 0.1 or 1 mg/kg) significantly increased DOPAC or DOPA levels in the median eminence, nucleus accumbens and striatum, but not in the paraventricular nucleus or A14 at 14 h later in 28-day old female rats or in 40-day-old rats pretreated with cysteamine. Cysteamine 284-294 prolactin Rattus norvegicus 26-35 11089894-0 2000 Cysteamine, the most potent ulcerogenic drug known so far, powerfully activates carbonic anhydrase I, II and IV. Cysteamine 0-10 carbonic anhydrase 1 Rattus norvegicus 80-111 11089894-6 2000 In vitro, we followed the effect of cysteamine on CA I, CA II and CA IV isolated from the gastric mucosa parietal cells and from kidneys using the Maren technique. Cysteamine 36-46 carbonic anhydrase 1 Rattus norvegicus 50-54 11089894-6 2000 In vitro, we followed the effect of cysteamine on CA I, CA II and CA IV isolated from the gastric mucosa parietal cells and from kidneys using the Maren technique. Cysteamine 36-46 carbonic anhydrase 4 Rattus norvegicus 66-71 11089894-11 2000 The results show that in vitro cysteamine activated the purified CA I and CA II, as well as gastric mucosa parietal cell CA IV by a direct mechanism of action. Cysteamine 31-41 carbonic anhydrase 1 Rattus norvegicus 65-69 11089894-11 2000 The results show that in vitro cysteamine activated the purified CA I and CA II, as well as gastric mucosa parietal cell CA IV by a direct mechanism of action. Cysteamine 31-41 carbonic anhydrase 2 Rattus norvegicus 74-79 11089894-11 2000 The results show that in vitro cysteamine activated the purified CA I and CA II, as well as gastric mucosa parietal cell CA IV by a direct mechanism of action. Cysteamine 31-41 carbonic anhydrase 4 Rattus norvegicus 121-126 11089894-13 2000 In vivo cysteamine activated gastric mucosa CA I, CA II and CA IV and did not modify the activity of the same isozyme from the kidneys. Cysteamine 8-18 carbonic anhydrase 1 Rattus norvegicus 44-48 11089894-13 2000 In vivo cysteamine activated gastric mucosa CA I, CA II and CA IV and did not modify the activity of the same isozyme from the kidneys. Cysteamine 8-18 carbonic anhydrase 2 Rattus norvegicus 50-55 11089894-13 2000 In vivo cysteamine activated gastric mucosa CA I, CA II and CA IV and did not modify the activity of the same isozyme from the kidneys. Cysteamine 8-18 carbonic anhydrase 4 Rattus norvegicus 60-65 11089894-14 2000 In vivo and in vitro CA I activation had confirmed our results, and this fact proved the enzyme"s involvement in the vasocontrictive process cysteamine-induced. Cysteamine 141-151 carbonic anhydrase 1 Rattus norvegicus 21-25 11089894-15 2000 The powerful activation of gastric CA II and CA IV through the H+ source, could explain the HCl excess produced by cysteamine. Cysteamine 115-125 carbonic anhydrase 2 Rattus norvegicus 35-40 11089894-15 2000 The powerful activation of gastric CA II and CA IV through the H+ source, could explain the HCl excess produced by cysteamine. Cysteamine 115-125 carbonic anhydrase 4 Rattus norvegicus 45-50 11089894-17 2000 The results suggested the involvement of gastric mucosa CA I, II and IV in the experimental cysteamine ulcerogenesis. Cysteamine 92-102 carbonic anhydrase 1 Rattus norvegicus 56-60 10942521-3 2000 We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. Cysteamine 28-38 heme oxygenase 1 Rattus norvegicus 87-103 10942521-3 2000 We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. Cysteamine 28-38 heme oxygenase 1 Rattus norvegicus 105-109 10942521-3 2000 We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. Cysteamine 28-38 superoxide dismutase 2 Rattus norvegicus 175-180 11053673-3 2000 Our laboratory has shown that cysteamine, dopamine, beta-amyloid, IL-1beta and TNF-alpha up-regulate HO-1 followed by mitochondrial sequestration of non-transferrin-derived 55Fe in cultured rat astroglia. Cysteamine 30-40 heme oxygenase 1 Rattus norvegicus 101-105 11053673-3 2000 Our laboratory has shown that cysteamine, dopamine, beta-amyloid, IL-1beta and TNF-alpha up-regulate HO-1 followed by mitochondrial sequestration of non-transferrin-derived 55Fe in cultured rat astroglia. Cysteamine 30-40 transferrin Rattus norvegicus 153-164 10620110-5 2000 In contrast, tyrosinase activity in an amelanotic melanoma cell line (MM96L) was rapidly inhibited without consumption of cystamine/cysteamine, in association with the generation of free thiol in the culture medium, and could be enhanced by the cystine transport inhibitor, glutamate. Cysteamine 132-142 tyrosinase Homo sapiens 13-23 10583725-4 1999 Cysteamine lowered serum prolactin concentrations to 20%, and median eminence DOPAC and dopamine levels to 32-50% of control levels in both studies. Cysteamine 0-10 prolactin Rattus norvegicus 25-34 10424464-6 1999 To modify the cysteinyl group of apoE3, the VLDL from the apoE3/3 subject was pretreated with cysteamine before the TBA assay and electrophoresis. Cysteamine 94-104 apolipoprotein E Homo sapiens 33-38 12835114-2 1999 In rat primary astrocyte cultures, we demonstrated that dopamine, cysteamine, H(2)O(2) and menadione rapidly induce heme oxygenase-1 (HO-1) expression (mRNA and protein) followed by sequestration of non-transferrin-derived (55)Fe by the mitochondrial compartment. Cysteamine 66-76 heme oxygenase 1 Rattus norvegicus 116-132 12835114-2 1999 In rat primary astrocyte cultures, we demonstrated that dopamine, cysteamine, H(2)O(2) and menadione rapidly induce heme oxygenase-1 (HO-1) expression (mRNA and protein) followed by sequestration of non-transferrin-derived (55)Fe by the mitochondrial compartment. Cysteamine 66-76 heme oxygenase 1 Rattus norvegicus 134-138 18031160-2 1999 Our initial experiments revealed that intragastric administration of bFGF-w, acid-resistant bFGF-CS23 and PDGF-BB healed chronic cysteamine (mercaptamine)-induced duodenal ulcer in rats, without decreasing gastric acid secretion or concentration. Cysteamine 129-139 fibroblast growth factor 2 Rattus norvegicus 69-73 18031160-2 1999 Our initial experiments revealed that intragastric administration of bFGF-w, acid-resistant bFGF-CS23 and PDGF-BB healed chronic cysteamine (mercaptamine)-induced duodenal ulcer in rats, without decreasing gastric acid secretion or concentration. Cysteamine 129-139 fibroblast growth factor 2 Rattus norvegicus 92-96 18031160-2 1999 Our initial experiments revealed that intragastric administration of bFGF-w, acid-resistant bFGF-CS23 and PDGF-BB healed chronic cysteamine (mercaptamine)-induced duodenal ulcer in rats, without decreasing gastric acid secretion or concentration. Cysteamine 141-153 fibroblast growth factor 2 Rattus norvegicus 69-73 18031160-2 1999 Our initial experiments revealed that intragastric administration of bFGF-w, acid-resistant bFGF-CS23 and PDGF-BB healed chronic cysteamine (mercaptamine)-induced duodenal ulcer in rats, without decreasing gastric acid secretion or concentration. Cysteamine 141-153 fibroblast growth factor 2 Rattus norvegicus 92-96 10424464-6 1999 To modify the cysteinyl group of apoE3, the VLDL from the apoE3/3 subject was pretreated with cysteamine before the TBA assay and electrophoresis. Cysteamine 94-104 apolipoprotein E Homo sapiens 58-63 10424464-10 1999 The apoE3/3 pretreated with cysteamine showed the patterns of apoE3/4 in IEF and SDS-PAGE with immunoblotting, but it did not show the shortened lag time in the TBA assay. Cysteamine 28-38 apolipoprotein E Homo sapiens 4-9 10424464-10 1999 The apoE3/3 pretreated with cysteamine showed the patterns of apoE3/4 in IEF and SDS-PAGE with immunoblotting, but it did not show the shortened lag time in the TBA assay. Cysteamine 28-38 apolipoprotein E Homo sapiens 62-67 10218809-2 1999 In the present study, infusion of cysteamine into the lateral ventricle of young, adult rats (1 mg/day for three weeks followed by a one-month drug "washout" period) significantly increased numbers of peroxidase-positive astrocytic granules in the stratum oriens of the CA1 hippocampus relative to saline-infused controls. Cysteamine 34-44 carbonic anhydrase 1 Rattus norvegicus 270-273 9711824-4 1998 The trisaccharide which corresponds to a structural motif occurring in N-glycoprotein glycans from human urokinase, human recombinant protein C, phospholipase A2 as well as O-glycans, was converted into a neoglycoprotein following introduction of a cysteamine-derived spacer group and subsequent activation with thiophosgene. Cysteamine 249-259 phospholipase A2 group IB Homo sapiens 145-161 9753225-6 1998 The severity of cysteamine-induced duodenal ulcers was dose-dependently decreased by pretreatment with ET-1 antibodies or antagonist bosentan. Cysteamine 16-26 endothelin 1 Homo sapiens 103-107 9537290-6 1998 Both acrosin (EC 3.4.21.10) and hyaluronidase (EC 3.2.1.35) were reversibly inhibited by cysteamine. Cysteamine 89-99 acrosin Homo sapiens 5-12 9535023-17 1998 or the selective somatostatin depleting agent cysteamine (280 mg kg(-1), s.c.) prevented the anti-inflammatory effect of sciatic nerve stimulation (5 Hz, 5 min) on a subsequent neurogenic plasma extravasation of the contralateral paw skin. Cysteamine 46-56 somatostatin Rattus norvegicus 17-29 9329060-2 1997 Low concentrations of cysteamine selectively depletes somatostatin and has been used to investigate the role of endogenous somatostatin in lieu of an available selective receptor antagonist. Cysteamine 22-32 somatostatin Homo sapiens 123-135 9247075-0 1997 Long-term effects of cysteamine on cognitive and locomotor behavior in rats: relationship to hippocampal glial pathology and somatostatin levels. Cysteamine 21-31 somatostatin Rattus norvegicus 125-137 9329060-2 1997 Low concentrations of cysteamine selectively depletes somatostatin and has been used to investigate the role of endogenous somatostatin in lieu of an available selective receptor antagonist. Cysteamine 22-32 somatostatin Homo sapiens 54-66 9344547-5 1997 In the present study, we demonstrate that cysteamine suppresses cathepsin B mRNA levels and immunoreactive protein in cultured astroglia, whereas cathepsin D mRNA and protein levels are significantly augmented by CSH exposure in these cells. Cysteamine 42-52 cathepsin B Homo sapiens 64-75 9323287-12 1997 Cysteamine has a marked effect on gastric acid production and serum gastrin, even at the dose used in children with nephropathic cystinosis. Cysteamine 0-10 gastrin Homo sapiens 68-75 9263585-2 1997 Rat pups received a daily injection of cysteamine which, when applied at low concentrations, most selectively depletes somatostatin. Cysteamine 39-49 somatostatin Rattus norvegicus 119-131 9403786-0 1997 Growth hormone and somatostatin interaction in the ulcerogenic effect of cysteamine in female rats. Cysteamine 73-83 gonadotropin releasing hormone receptor Rattus norvegicus 0-14 9403786-0 1997 Growth hormone and somatostatin interaction in the ulcerogenic effect of cysteamine in female rats. Cysteamine 73-83 somatostatin Rattus norvegicus 19-31 9403786-1 1997 It is known that cysteamine"s ulcerogenic effect depends, among others, on a depletion of somatostatin (SRIH). Cysteamine 17-27 somatostatin Rattus norvegicus 90-102 9403786-7 1997 The combined administration of GH and SRIH revealed that cysteamine ulcerogenic action remained unchanged. Cysteamine 57-67 gonadotropin releasing hormone receptor Rattus norvegicus 31-33 9403786-8 1997 It is possible that high levels of plasma GH, as induced by exogenous GH administration, may decrease the release of gastro-intestinal SRIH and this in turn may potentiate the ulcerogenic activity of cysteamine. Cysteamine 200-210 gonadotropin releasing hormone receptor Rattus norvegicus 42-44 9403786-8 1997 It is possible that high levels of plasma GH, as induced by exogenous GH administration, may decrease the release of gastro-intestinal SRIH and this in turn may potentiate the ulcerogenic activity of cysteamine. Cysteamine 200-210 gonadotropin releasing hormone receptor Rattus norvegicus 70-72 9479631-0 1997 Evidence for a significant role of gastrin in cysteamine-induced hypersecretion of gastric acid. Cysteamine 46-56 gastrin Rattus norvegicus 35-42 9061006-5 1997 Using as a probe cysteamine, an aminothiol compound with both antioxidant and antiproliferative activity, we have identified erk2, a key element of the MAP kinase pathway, as being responsive to oxidative signalling during lymphocyte activation. Cysteamine 17-27 mitogen-activated protein kinase 1 Homo sapiens 125-129 9214592-6 1997 Because GFAP transcription in cultured glia is increased by oxidative stress in response to hydrogen peroxide and cysteamine whether or not microglia were present, we conclude that responses of GFAP to oxidative stress in astrocytes do not depend on microglial activation. Cysteamine 114-124 glial fibrillary acidic protein Rattus norvegicus 8-12 9479631-2 1997 We investigated the role of gastrin in cysteamine-induced acid hypersecretion in the perfused rat stomach. Cysteamine 39-49 gastrin Rattus norvegicus 28-35 9479631-3 1997 Intravenous infusion of cysteamine (75 mg/kg/h) resulted in a significant increase in acid secretion, which was accompanied by a marked increase in the plasma gastrin concentration. Cysteamine 24-34 gastrin Rattus norvegicus 159-166 9479631-7 1997 infusion of a CCK-B/gastrin receptor antagonist (L-365,260) (1 mg/kg/h) also suppressed the cysteamine-induced increase in acid secretion. Cysteamine 92-102 gastrin Rattus norvegicus 20-27 9479631-9 1997 The elevated plasma gastrin levels induced by cysteamine were unaffected by atropine and L-365,260. Cysteamine 46-56 gastrin Rattus norvegicus 20-27 9479631-10 1997 In conclusion, cysteamine-induced acid hypersecretion is mediated mainly by cysteamine-induced gastrin release and partially by cholinergic factors. Cysteamine 15-25 gastrin Rattus norvegicus 95-102 9479631-10 1997 In conclusion, cysteamine-induced acid hypersecretion is mediated mainly by cysteamine-induced gastrin release and partially by cholinergic factors. Cysteamine 76-86 gastrin Rattus norvegicus 95-102 9479631-11 1997 Furthermore, gastrin release caused by cysteamine appears to be independent of cholinergic tone. Cysteamine 39-49 gastrin Rattus norvegicus 13-20 9200665-1 1997 It is known that cysteamine ulcerogenic effect depends, among others, on a depletion of somatostatin in the gastro-intestinal tract. Cysteamine 17-27 somatostatin Rattus norvegicus 88-100 9200665-2 1997 Since growth hormone (GH) causes the release of hypothalamic somatostatin (SRIH) and potentiates the ulcerogenic action of cysteamine we have studied the influence of GH on gastro-duodenal mucosa levels of SRIH, and its relevance for the ulcerogenic action of cysteamine. Cysteamine 123-133 gonadotropin releasing hormone receptor Rattus norvegicus 6-20 8961948-11 1996 Lipophilic thiols such as mercaptoethanol or cysteamine could partially reverse the CCl4-induced calcium release, whereas GSH was ineffective. Cysteamine 45-55 C-C motif chemokine ligand 4 Rattus norvegicus 84-88 9027638-0 1996 Effect of cysteamine on gastric nerve fibers containing gastrin-releasing peptide in the rat. Cysteamine 10-20 gastrin releasing peptide Rattus norvegicus 56-81 9027638-1 1996 In rats, changes in gastric nerve fibers containing gastrin-releasing peptide (GRP) in cysteamine-induced duodenal ulcer were investigated in relation to the dynamics of gastrin-producing cells (G-cells). Cysteamine 87-97 gastrin releasing peptide Rattus norvegicus 52-77 9027638-1 1996 In rats, changes in gastric nerve fibers containing gastrin-releasing peptide (GRP) in cysteamine-induced duodenal ulcer were investigated in relation to the dynamics of gastrin-producing cells (G-cells). Cysteamine 87-97 gastrin releasing peptide Rattus norvegicus 79-82 9027638-1 1996 In rats, changes in gastric nerve fibers containing gastrin-releasing peptide (GRP) in cysteamine-induced duodenal ulcer were investigated in relation to the dynamics of gastrin-producing cells (G-cells). Cysteamine 87-97 gastrin Rattus norvegicus 52-59 9027638-2 1996 Marked increases in gastric acid secretion and serum gastrin level were observed from 2 h after the administration of cysteamine. Cysteamine 118-128 gastrin Rattus norvegicus 53-60 9027638-5 1996 Circulating GRP levels were significantly elevated from 2 h after the administration of cysteamine. Cysteamine 88-98 gastrin releasing peptide Rattus norvegicus 12-15 9027638-7 1996 Eight h after the administration of cysteamine, there was depleted GRP immunoreactivity, evidenced by a markedly decreased number of vesicles, with large electron-dense cores, in the oxyntic mucosa. Cysteamine 36-46 gastrin releasing peptide Rattus norvegicus 67-70 9027638-8 1996 These findings suggest that, in cysteamine-induced duodenal ulcer, alterations in gastric nerve fibers containing GRP may be related to hypergastrinemia. Cysteamine 32-42 gastrin releasing peptide Rattus norvegicus 114-117 8874886-0 1996 Brain somatostatin depletion by cysteamine attenuates the penile erection induced by serotonergic and dopaminergic, but not by cholinergic, activation in rats. Cysteamine 32-42 somatostatin Rattus norvegicus 6-18 8830931-5 1996 Cysteamine modification resulted in a shift of apoE1 to the apoE2 isoform position, indicating that the mutation leading to apoE1-Hammersmith occurred on an apoE3 background. Cysteamine 0-10 apolipoprotein E Homo sapiens 60-65 8830931-5 1996 Cysteamine modification resulted in a shift of apoE1 to the apoE2 isoform position, indicating that the mutation leading to apoE1-Hammersmith occurred on an apoE3 background. Cysteamine 0-10 apolipoprotein E Homo sapiens 157-162 8874886-7 1996 Neurochemical measures revealed that cysteamine pretreatment significantly reduced the somatostatin content in all brain regions examined. Cysteamine 37-47 somatostatin Rattus norvegicus 87-99 8744334-2 1996 Experiments demonstrated that a thiol-containing reducing agent, mercaptoethylamine (MEA or cysteamine), was the most effective, among other commonly known radical quenchers or singlet oxygen scavengers, in suppressing photobleaching of fluorescein while not reducing the fluorescence quantum yield. Cysteamine 65-83 male-enhanced antigen 1 Homo sapiens 85-88 8744334-2 1996 Experiments demonstrated that a thiol-containing reducing agent, mercaptoethylamine (MEA or cysteamine), was the most effective, among other commonly known radical quenchers or singlet oxygen scavengers, in suppressing photobleaching of fluorescein while not reducing the fluorescence quantum yield. Cysteamine 92-102 male-enhanced antigen 1 Homo sapiens 85-88 8529029-6 1995 Cysteamine administration increased GH pulse amplitude (quadratic, P = .15), with the greatest magnigtude of change occurring with 50 mg/kg BW CSH on day 0 and 3. Cysteamine 0-10 somatotropin Ovis aries 36-38 8737284-1 1996 This study was performed in order to establish whether selective depletion of somatostatin (SS) in the rat primary visual cortex obtained by cysteamine (CSH) administration results in changes of visual evoked potentials (VEPs). Cysteamine 141-151 somatostatin Rattus norvegicus 78-90 8750834-0 1995 Time course of the induction of VGF mRNA in the dorsal vagal complex in rats with cysteamine-induced peptic ulcers. Cysteamine 82-92 VGF nerve growth factor inducible Rattus norvegicus 32-35 8750834-1 1995 The time course of induction of VGF mRNA in the dorsal vagal complex of the medulla oblongata was investigated in rats with duodenal ulcer induced with cysteamine by in situ hybridization histochemistry. Cysteamine 152-162 VGF nerve growth factor inducible Rattus norvegicus 32-35 8750834-3 1995 After the cysteamine administration (450 mg/kg, s.c.), VGF mRNA signals began to increase after 3 h, reached at peak level at 12 h, and decreased slightly at 24 h, but remained high after 48 h. The time course of duodenal ulcer score was absent at 3 h, very low at 6 h, about grade 1 at 12 h, and grade 2 or more at 24 and 48 h. The present results support the hypothesis that the increase of the central neuronal activity of the vagus nerve precedes ulcer generation in the duodenum. Cysteamine 10-20 VGF nerve growth factor inducible Rattus norvegicus 55-58 8732303-2 1996 Our initial animal model experiment revealed a potent healing of chronic cysteamine-induced duodenal ulcer in rats treated by intragastric administration of bFGF-w, the acid-resistant bFGF-CS23 or PDGF-BB without decreasing gastric acid secretion or concentration. Cysteamine 73-83 fibroblast growth factor 2 Rattus norvegicus 157-161 8732303-2 1996 Our initial animal model experiment revealed a potent healing of chronic cysteamine-induced duodenal ulcer in rats treated by intragastric administration of bFGF-w, the acid-resistant bFGF-CS23 or PDGF-BB without decreasing gastric acid secretion or concentration. Cysteamine 73-83 fibroblast growth factor 2 Rattus norvegicus 184-188 8848261-0 1996 Cysteamine impairs the development of the acoustic startle response in rats: possible role of somatostatin. Cysteamine 0-10 somatostatin Rattus norvegicus 94-106 8848261-3 1996 Cysteamine treatment drastically reduced somatostatin immunoreactivity in the cochlear nuclear complex and the caudal pontine reticular nucleus, i.e. in structures mediating the ASR. Cysteamine 0-10 somatostatin Rattus norvegicus 41-53 8529029-0 1995 Effects of cysteamine on pulsatile growth hormone release and plasma insulin concentrations in sheep. Cysteamine 11-21 somatotropin Ovis aries 35-49 8538870-11 1995 The inhibitory activity of AMY on GH secretion elicited by GHRH seems to be independent of hypothalamic somatostatin; in fact, AMY was still active in rats treated with cysteamine. Cysteamine 169-179 islet amyloid polypeptide Rattus norvegicus 27-30 8538870-11 1995 The inhibitory activity of AMY on GH secretion elicited by GHRH seems to be independent of hypothalamic somatostatin; in fact, AMY was still active in rats treated with cysteamine. Cysteamine 169-179 islet amyloid polypeptide Rattus norvegicus 127-130 7640301-6 1995 Taking the IL-2 gene as a candidate, we examined the effect of cysteamine treatment on early gene expression during lymphocyte activation, and on the activity of transcription factors AP-1, NF-kappa B, NF-AT and Oct1, whose functions are required for expression of the IL-2 mRNA. Cysteamine 63-73 interleukin 2 Homo sapiens 11-15 8674812-9 1995 However, the oxidation-reduction system cystamine (1.34 mM) and cysteamine (7.3 mM) facilitated both the refolding of rNG-hCGalpha and reconstitution of rNG-hCGalpha with native hCGbeta to regain partially correct conformation. Cysteamine 64-74 chromogranin A Homo sapiens 122-130 8674812-9 1995 However, the oxidation-reduction system cystamine (1.34 mM) and cysteamine (7.3 mM) facilitated both the refolding of rNG-hCGalpha and reconstitution of rNG-hCGalpha with native hCGbeta to regain partially correct conformation. Cysteamine 64-74 chromogranin A Homo sapiens 157-165 8674812-11 1995 Cystamine and cysteamine were more effective in the recombination of rNG-hCGalpha with oFSHbeta as indicated by a 22-36-fold decrease in the amount required to cause a 50% competitive inhibition in radioreceptor assay. Cysteamine 14-24 chromogranin A Homo sapiens 73-81 7640301-7 1995 Cysteamine treatment inhibited both expression of the IL-2 mRNA and secretion of IL-2 into the culture medium. Cysteamine 0-10 interleukin 2 Homo sapiens 54-58 7494463-0 1995 Induction of VGF mRNA in neurons of the rat nucleus tractus solitarius and the dorsal motor nucleus of vagus in duodenal ulceration by cysteamine. Cysteamine 135-145 VGF nerve growth factor inducible Rattus norvegicus 13-16 7640301-7 1995 Cysteamine treatment inhibited both expression of the IL-2 mRNA and secretion of IL-2 into the culture medium. Cysteamine 0-10 interleukin 2 Homo sapiens 81-85 7640301-8 1995 The inhibitory effect of cysteamine may be mediated at least in part by an effect on transcription factor function, as the DNA binding activities of AP-1 and NF-kappa B extracted from mitogen-stimulated cells were significantly inhibited by cysteamine treatment. Cysteamine 25-35 nuclear factor kappa B subunit 1 Homo sapiens 158-168 7640301-8 1995 The inhibitory effect of cysteamine may be mediated at least in part by an effect on transcription factor function, as the DNA binding activities of AP-1 and NF-kappa B extracted from mitogen-stimulated cells were significantly inhibited by cysteamine treatment. Cysteamine 241-251 nuclear factor kappa B subunit 1 Homo sapiens 158-168 7500382-9 1995 When astrocytes were exposed to known HSP27 inducers, hydrogen peroxide and cysteamine reduced the synthesis of HSP27, while estradiol showed no effects. Cysteamine 76-86 heat shock protein family B (small) member 1 Homo sapiens 38-43 7500382-9 1995 When astrocytes were exposed to known HSP27 inducers, hydrogen peroxide and cysteamine reduced the synthesis of HSP27, while estradiol showed no effects. Cysteamine 76-86 heat shock protein family B (small) member 1 Homo sapiens 112-117 7494463-1 1995 To investigate the possible role of the brainstem in cysteamine-induced peptic ulceration, we examined the expression of VGF mRNA, which is induced in PC12 cells following application of nerve growth factor [23], in the nucleus tractus solitarius (NTS)/dorsal motor nucleus of vagus (DMV) complex of the medulla oblongata by in situ hybridization histochemistry. Cysteamine 53-63 VGF nerve growth factor inducible Rattus norvegicus 121-124 7494463-3 1995 After 12 h of cysteamine administration (450 mg/kg, s.c.), the time at which duodenal ulcer was detected in all cases, heavily labeled VGF mRNA-expressing neurons appeared in the NTS and DMV. Cysteamine 14-24 VGF nerve growth factor inducible Rattus norvegicus 135-138 7494463-4 1995 By quantitative analysis on macroautoradiogram, the VGF mRNA signals of the NTS/DMV complex in cysteamine-treated rats were twice as much as those in saline-treated rats. Cysteamine 95-105 VGF nerve growth factor inducible Rattus norvegicus 52-55 7601757-0 1995 Cysteamine-induced depletion of somatostatin in sheep: time course of depletion and changes in plasma metabolites, insulin, and growth hormone. Cysteamine 0-10 LOC105613195 Ovis aries 115-122 7637967-1 1995 Authors investigated the role of endogenous bFGF in the development of experimental duodenal ulcer induced by cysteamine. Cysteamine 110-120 fibroblast growth factor 2 Rattus norvegicus 44-48 7637967-3 1995 A significant decrease was found in the immunoreactivity of bFGF in rat duodenal mucosa 12 and 24 hr after the administration of the duodenal ulcerogen cysteamine. Cysteamine 152-162 fibroblast growth factor 2 Rattus norvegicus 60-64 7644025-6 1995 On the other hand, treatment with cysteamine significantly reduced the contents of somatostatin in all the brain regions examined, but minimally affected choline acetyltransferase activity. Cysteamine 34-44 choline O-acetyltransferase Rattus norvegicus 154-179 7617135-5 1995 Depletion of tissue SRIF by 10(-3) M cysteamine increased K(+)-stimulated GRH release 2-fold without altering basal GRH secretion. Cysteamine 37-47 somatostatin Mus musculus 20-24 7617135-5 1995 Depletion of tissue SRIF by 10(-3) M cysteamine increased K(+)-stimulated GRH release 2-fold without altering basal GRH secretion. Cysteamine 37-47 growth hormone releasing hormone Mus musculus 74-77 7617135-10 1995 Combined perifusion with cysteamine and 10(-9) M SRIF also resulted in a GRH response to K+ that did not differ from the response observed during cysteamine alone. Cysteamine 25-35 growth hormone releasing hormone Mus musculus 73-76 7617135-10 1995 Combined perifusion with cysteamine and 10(-9) M SRIF also resulted in a GRH response to K+ that did not differ from the response observed during cysteamine alone. Cysteamine 146-156 somatostatin Mus musculus 49-53 7775651-6 1995 The GH response to KP-102 alone or KP-102 with GRF was significantly augmented when cysteamine HCl was previously administered. Cysteamine 84-98 growth hormone releasing hormone Rattus norvegicus 47-50 7836377-4 1995 Cysteamine uptake into fibroblast lysosomes displays complete saturability with a Km of 0.88 mM and Vmax of 1410 pmol of beta-N-acetylhexosaminidase/min at pH 7.0 and 37 degrees C. Analog inhibition studies demonstrated that all analogs recognized thus far by the cysteamine carrier are either aminothiols or aminosulfides and contain an amino group and sulfur atom separated by a carbon chain, 2 carbon atoms in length. Cysteamine 0-10 O-GlcNAcase Homo sapiens 121-148 7601757-0 1995 Cysteamine-induced depletion of somatostatin in sheep: time course of depletion and changes in plasma metabolites, insulin, and growth hormone. Cysteamine 0-10 somatotropin Ovis aries 128-142 7601757-7 1995 Cysteamine administration decreased (P < .05) tissue SRIF on d 0 (2, 4, and 8 h), 1, and 3; maximal depletion (42 to 55% of Pre-treatment; Pre-trt) occurred during the initial 24 h, returning to Pre-trt by d 10. Cysteamine 0-10 somatostatin Ovis aries 56-60 7777801-3 1995 METHODS AND RESULTS: Oral treatment of rats with bFGF or PDGF accelerated the healing of chronic cysteamine-induced duodenal ulcers without decreasing gastric secretion. Cysteamine 97-107 fibroblast growth factor 2 Rattus norvegicus 49-53 7807413-3 1994 Intraperitoneal administration of cysteamine (200 mg/kg), a somatostatin depletor, significantly reduced somatostatin level in the in vivo SCN 5 min after injection and kept low level as long as 3 to 4 days. Cysteamine 34-44 somatostatin Rattus norvegicus 60-72 7807413-3 1994 Intraperitoneal administration of cysteamine (200 mg/kg), a somatostatin depletor, significantly reduced somatostatin level in the in vivo SCN 5 min after injection and kept low level as long as 3 to 4 days. Cysteamine 34-44 somatostatin Rattus norvegicus 105-117 18618447-5 1994 The rates of these folding events were determined with and without protein disulfide isomerase (PDI) using two different types of redox reagents: cysteamine and its oxidized equivalent, cystamine, and reduced and oxidized glutathione. Cysteamine 146-156 prolyl 4-hydroxylase subunit beta Homo sapiens 96-99 7957261-1 1994 The mammalian enzyme pantetheinase, which hydrolyzes pantetheine to pantothenic acid and cysteamine, is inhibited by many thiol reagents and activated by thiols. Cysteamine 89-99 vanin 1 Homo sapiens 21-34 7866298-0 1994 Thioltransferase can utilize cysteamine as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity. Cysteamine 29-39 glutaredoxin Homo sapiens 0-16 7866298-0 1994 Thioltransferase can utilize cysteamine as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity. Cysteamine 29-39 glucose-6-phosphate dehydrogenase Homo sapiens 122-155 7866298-3 1994 The inactivated-G6PD is restored its activity by the treatment of thioltransferase with 1 mM cysteamine or reduced glutathione (GSH) much more effectively than only by thiols. Cysteamine 93-103 glucose-6-phosphate dehydrogenase Homo sapiens 16-20 7866298-3 1994 The inactivated-G6PD is restored its activity by the treatment of thioltransferase with 1 mM cysteamine or reduced glutathione (GSH) much more effectively than only by thiols. Cysteamine 93-103 glutaredoxin Homo sapiens 66-82 7866298-4 1994 For the first time, we suggested thioltransferase can utilize cysteamine in stead of GSH during its thiol/disulfide exchange reaction activity. Cysteamine 62-72 glutaredoxin Homo sapiens 33-49 7841300-9 1994 Immunoblotting analysis with a rabbit antiserum against human serum albumin indicated that albumin was not linked to the odd sulphydryl group of fibrinogen Milano V. Treatment of fibrinogen Milano V with cysteamine, that is surmised to convert the mutant cysteine to a positively charged lysine analogue, did not improve the clotting properties of fibrinogen Milano V. Cysteamine 204-214 fibrinogen beta chain Homo sapiens 179-189 7841300-9 1994 Immunoblotting analysis with a rabbit antiserum against human serum albumin indicated that albumin was not linked to the odd sulphydryl group of fibrinogen Milano V. Treatment of fibrinogen Milano V with cysteamine, that is surmised to convert the mutant cysteine to a positively charged lysine analogue, did not improve the clotting properties of fibrinogen Milano V. Cysteamine 204-214 fibrinogen beta chain Homo sapiens 179-189 18618447-7 1994 Optimal conditions for hCG-beta folding were attained in a 2 mM glutathione buffer, pH 7.4, that contained 1 mg/mL PDI and in 10 microM cysteamine/cystamine, pH 8.7, without PDI. Cysteamine 136-146 chorionic gonadotropin subunit beta 3 Homo sapiens 23-31 7908140-1 1994 The drug cysteamine (CHS) induces a profound loss of somatostatin-14 (SS-14) biological and immunological (SS-14 LI) activity from somatostatin cells in vivo and in vitro. Cysteamine 9-19 somatostatin Rattus norvegicus 53-68 7914816-1 1994 Administration of a somatostatin (SS) depletor, cysteamine, markedly reduced SS levels in rat suprachiasmatic nucleus (SCN). Cysteamine 48-58 somatostatin Rattus norvegicus 20-32 7914816-2 1994 At the same time, cysteamine administration induced a circadian rhythm of vasoactive intestinal polypeptide (VIP) content in the SCN, which otherwise remains constant under constant environmental conditions. Cysteamine 18-28 vasoactive intestinal peptide Rattus norvegicus 74-107 7914816-2 1994 At the same time, cysteamine administration induced a circadian rhythm of vasoactive intestinal polypeptide (VIP) content in the SCN, which otherwise remains constant under constant environmental conditions. Cysteamine 18-28 vasoactive intestinal peptide Rattus norvegicus 109-112 8159271-0 1994 Effect of cysteamine injection on vasopressin and oxytocin biosynthesis in rat hypothalamus. Cysteamine 10-20 arginine vasopressin Rattus norvegicus 34-45 8159271-1 1994 Cysteamine (CSH), a sulfhydryl agent that promotes disulfide-exchange reactions, was studied for its effects on the immunoreactive (IR) levels and synthesis of oxytocin and vasopressin in the hypothalamus. Cysteamine 0-10 arginine vasopressin Rattus norvegicus 173-184 7951574-0 1994 Effects of cysteamine, a somatostatin depleter, on the renin-angiotensin-aldosterone axis and glomerulosa cell growth in rats. Cysteamine 11-21 renin Rattus norvegicus 55-60 7951574-1 1994 Cysteamine, a specific somatostatin depleter, was given to male rats to clarify its role in relation to the renin-angiotensin-aldosterone (RAA) axis and glomerulosa cell growth. Cysteamine 0-10 renin Rattus norvegicus 108-113 7908140-1 1994 The drug cysteamine (CHS) induces a profound loss of somatostatin-14 (SS-14) biological and immunological (SS-14 LI) activity from somatostatin cells in vivo and in vitro. Cysteamine 9-19 somatostatin Rattus norvegicus 70-75 7915573-6 1994 We conclude that an increase of oxygen-derived free radicals and a decrease of Cu,Zn-SOD activity in the duodenal mucosa may be involved in the pathogenesis of cysteamine-induced duodenal ulcers in rats. Cysteamine 160-170 superoxide dismutase 1 Rattus norvegicus 79-88 7908712-1 1994 The effects were investigated of cysteamine--a well known somatostatin depletor--on the pain induced by chemical stimuli in mice. Cysteamine 33-43 somatostatin Mus musculus 58-70 7908712-5 1994 Intrathecally injected somatostatin was able to revert the cysteamine antinociceptive effects in the second phase of the formalin test and in the writhing test, whereas intracerebroventricularly injected somatostatin reduced the antinociceptive effects induced by cysteamine in the second phase of the formalin test. Cysteamine 59-69 somatostatin Mus musculus 23-35 7908712-5 1994 Intrathecally injected somatostatin was able to revert the cysteamine antinociceptive effects in the second phase of the formalin test and in the writhing test, whereas intracerebroventricularly injected somatostatin reduced the antinociceptive effects induced by cysteamine in the second phase of the formalin test. Cysteamine 264-274 somatostatin Mus musculus 204-216 7908712-6 1994 Intrathecally injected cyclo(7-aminoheptanoyl-Phe-D-Trp-Lys-Thr[Bzl])--a reported somatostatin antagonist--increased cysteamine antinociceptive effects in the second phase of the formalin test and in the writhing test. Cysteamine 117-127 somatostatin Mus musculus 82-94 7908712-7 1994 These results suggest that somatostatin is involved in the effects of cysteamine on the nociceptive threshold. Cysteamine 70-80 somatostatin Mus musculus 27-39 7904712-7 1994 A dose-dependent protection (cysteamine) and/or partial positive effect (related to treatment conditions) (ethanol), was obtained with glucagon, NPY and secretin whereas CCK/26-30/was not effective. Cysteamine 29-39 neuropeptide Y Rattus norvegicus 145-148 7904712-7 1994 A dose-dependent protection (cysteamine) and/or partial positive effect (related to treatment conditions) (ethanol), was obtained with glucagon, NPY and secretin whereas CCK/26-30/was not effective. Cysteamine 29-39 secretin Rattus norvegicus 153-161 7937348-4 1994 In addition, ICV-injected amylin inhibited insulin-stimulated acid gastric secretion and was effective in suppressing acid gastric secretion in rats depleted of somatostatin by pretreatment with cysteamine. Cysteamine 195-205 islet amyloid polypeptide Rattus norvegicus 26-32 7901036-6 1993 In hippocampal slices from animals treated with cysteamine, which was shown to deplete hippocampal somatostatin, FR121196 (10(-7) M) hardly affected long-term potentiation generation, whereas physostigmine (10(-6) M) and methamphetamine (10(-7) M) augmented it significantly. Cysteamine 48-58 somatostatin Cavia porcellus 99-111 7688275-1 1993 Cysteamine is known to deplete somatostatin from pancreatic D cells. Cysteamine 0-10 somatostatin Rattus norvegicus 31-43 8375622-3 1993 In cysteamine-treated rats (250 mg/kg weight, intramuscular injection), mucosal alkaline secretion by intravenous EGF (10 micrograms/kg/hr) increased significantly only at levels of high luminal acidity, whereas that by intraduodenal EGF (10 micrograms/kg/hr) increased greatly at both high and low luminal acidities. Cysteamine 3-13 epidermal growth factor like 1 Rattus norvegicus 114-117 8375622-3 1993 In cysteamine-treated rats (250 mg/kg weight, intramuscular injection), mucosal alkaline secretion by intravenous EGF (10 micrograms/kg/hr) increased significantly only at levels of high luminal acidity, whereas that by intraduodenal EGF (10 micrograms/kg/hr) increased greatly at both high and low luminal acidities. Cysteamine 3-13 epidermal growth factor like 1 Rattus norvegicus 234-237 8104917-5 1993 These findings support the suggestion that the physiological substrate for D-amino acid oxidase may be D,L-thiazolidine-2-carboxylic acid, the adduct of cysteamine and glyoxylic acid. Cysteamine 153-163 D-amino-acid oxidase Rattus norvegicus 75-95 7688275-3 1993 Cysteamine, 10 mM, released somatostatin, but had no effect on CCK-stimulated amylase secretion. Cysteamine 0-10 somatostatin Rattus norvegicus 28-40 8095378-3 1993 Cysteamine was used to block endogenous somatostatin release before endotoxin treatment. Cysteamine 0-10 somatostatin Rattus norvegicus 40-52 8405073-3 1993 These protective effects of CGRP were not present when rats were pretreated with cysteamine. Cysteamine 81-91 calcitonin-related polypeptide alpha Rattus norvegicus 28-32 8394877-2 1993 In the present study, systemic cysteamine administration over a 3 week period induced HSP27, 72, 90, and GRP94 (stress proteins) in astrocytes and significantly increased numbers of peroxidase-positive astrocytic inclusions in the various brain regions relative to controls. Cysteamine 31-41 heat shock protein family B (small) member 1 Homo sapiens 86-91 8394877-2 1993 In the present study, systemic cysteamine administration over a 3 week period induced HSP27, 72, 90, and GRP94 (stress proteins) in astrocytes and significantly increased numbers of peroxidase-positive astrocytic inclusions in the various brain regions relative to controls. Cysteamine 31-41 heat shock protein 90 beta family member 1 Homo sapiens 105-110 8510013-0 1993 The gastrin/cholecystokinin-B receptor antagonist L-365,260 reduces basal acid secretion and prevents gastrointestinal damage induced by aspirin, ethanol and cysteamine in the rat. Cysteamine 158-168 gastrin Rattus norvegicus 4-11 8510013-0 1993 The gastrin/cholecystokinin-B receptor antagonist L-365,260 reduces basal acid secretion and prevents gastrointestinal damage induced by aspirin, ethanol and cysteamine in the rat. Cysteamine 158-168 cholecystokinin B receptor Rattus norvegicus 12-38 7683557-2 1993 Pretreatments with neostigmine and cysteamine blunted the GAL-induced GH secretion. Cysteamine 35-45 galanin and GMAP prepropeptide Rattus norvegicus 58-61 7683557-2 1993 Pretreatments with neostigmine and cysteamine blunted the GAL-induced GH secretion. Cysteamine 35-45 gonadotropin releasing hormone receptor Rattus norvegicus 70-72 7683557-4 1993 On the contrary, GH-releasing hormone-induced GH secretion was significantly enhanced with cysteamine and anti-somatostatin serum. Cysteamine 91-101 gonadotropin releasing hormone receptor Rattus norvegicus 17-19 7683557-4 1993 On the contrary, GH-releasing hormone-induced GH secretion was significantly enhanced with cysteamine and anti-somatostatin serum. Cysteamine 91-101 gonadotropin releasing hormone receptor Rattus norvegicus 46-48 8449936-7 1993 Catalytic similarity to the native FMO 1B1 was demonstrated by the ability of the expressed enzymes to metabolize methimazole, thiourea, dimethylaniline, and cysteamine, but not chlorpromazine or imipramine. Cysteamine 158-168 dimethylaniline monooxygenase [N-oxide-forming] 2 Oryctolagus cuniculus 35-42 1315979-0 1992 Cysteamine induced-duodenal ulcers are associated with a selective depletion in gastric and duodenal calcitonin gene-related peptide-like immunoreactivity in rats. Cysteamine 0-10 calcitonin-related polypeptide alpha Rattus norvegicus 101-132 8479612-0 1993 Characterization of cysteamine induction of the 22K prolactin variant in the rat pituitary. Cysteamine 20-30 prolactin Rattus norvegicus 52-61 1336994-0 1992 Prolactin and prolactin secretagogues reverse immunosuppression in mice treated with cysteamine, glucocorticoids, or cyclosporin-A. Cysteamine 85-95 prolactin Mus musculus 0-9 1336994-0 1992 Prolactin and prolactin secretagogues reverse immunosuppression in mice treated with cysteamine, glucocorticoids, or cyclosporin-A. Cysteamine 85-95 prolactin Mus musculus 14-23 1359114-1 1992 Cysteamine, a potent duodenal ulcerogen, stimulates gastric acid and gastrin secretion and decreases immunoreactive somatostatin (IRS) from the gut and hypothalamus of the rat. Cysteamine 0-10 gastrin Rattus norvegicus 69-76 1578305-1 1992 Three patients with nephropathic cystinosis and chronic renal disease, treated since early childhood with orally administered cysteamine, had an accelerated rate of rise of serum creatinine values after receiving recombinant human growth hormone. Cysteamine 126-136 growth hormone 1 Homo sapiens 231-245 8420757-4 1993 At 10 mM, however, cysteamine released somatostatin (380 +/- 70 vs 100 +/- 20 fmol/20 min), inhibited insulin output (890 +/- 120 vs 13210 +/- 3260 mu units/20 min) and reduced exocrine pancreatic secretion (volume: 12 +/- 2 vs 20 +/- 2 microliters/20 min; lipase: 31 +/- 3 vs 60 +/- 7 units/20 min). Cysteamine 19-29 somatostatin Rattus norvegicus 39-85 8502123-0 1993 Contribution of gastrin to cysteamine-induced gastric acid secretion in rats. Cysteamine 27-37 gastrin Rattus norvegicus 16-23 8502123-1 1993 The role of circulating gastrin in cysteamine induced gastric acid secretion was examined in conscious male Wistar rats, provided with a portal vein catheter, a jugular vein catheter and a pyloric drainage tube. Cysteamine 35-45 gastrin Rattus norvegicus 24-31 8502123-4 1993 Intravenous bolus administration of 125 mg/kg of cysteamine induced increases in serum gastrin concentration (864 +/- 96 pg/ml) and gastric acid outputs (107 +/- 27 mumol H+/kg.30 min) not significantly different from the gastrin 17-l infusion experiments. Cysteamine 49-59 gastrin Rattus norvegicus 87-94 8502123-4 1993 Intravenous bolus administration of 125 mg/kg of cysteamine induced increases in serum gastrin concentration (864 +/- 96 pg/ml) and gastric acid outputs (107 +/- 27 mumol H+/kg.30 min) not significantly different from the gastrin 17-l infusion experiments. Cysteamine 49-59 gastrin Rattus norvegicus 222-229 8502123-5 1993 Gastrin antiserum abolished cysteamine-induced gastric acid secretion, indicating that gastric acid secretion induced by 125 mg/kg of cysteamine is largely mediated by circulating gastrin in rats. Cysteamine 28-38 gastrin Rattus norvegicus 0-7 8502123-5 1993 Gastrin antiserum abolished cysteamine-induced gastric acid secretion, indicating that gastric acid secretion induced by 125 mg/kg of cysteamine is largely mediated by circulating gastrin in rats. Cysteamine 28-38 gastrin Rattus norvegicus 180-187 8502123-5 1993 Gastrin antiserum abolished cysteamine-induced gastric acid secretion, indicating that gastric acid secretion induced by 125 mg/kg of cysteamine is largely mediated by circulating gastrin in rats. Cysteamine 134-144 gastrin Rattus norvegicus 0-7 8502123-5 1993 Gastrin antiserum abolished cysteamine-induced gastric acid secretion, indicating that gastric acid secretion induced by 125 mg/kg of cysteamine is largely mediated by circulating gastrin in rats. Cysteamine 134-144 gastrin Rattus norvegicus 180-187 8469739-3 1993 Cysteamine was shown to produce a radioprotective effect in somatic cells of mus(2)201G1 and the control strain of drosophila which was manifested by the decreased incidence of cells with chromosome aberrations and diminished yield of deletions and exchanges. Cysteamine 0-10 Xeroderma pigmentosum, complementation group C Drosophila melanogaster 77-88 1336994-3 1992 The sulfhydryl reducing agent cysteamine (2-aminoethanethiol) is known to reduce pituitary and plasma prolactin levels. Cysteamine 30-40 prolactin Mus musculus 102-111 1336994-3 1992 The sulfhydryl reducing agent cysteamine (2-aminoethanethiol) is known to reduce pituitary and plasma prolactin levels. Cysteamine 42-60 prolactin Mus musculus 102-111 1336994-4 1992 Treatment of mice with cysteamine at doses which suppressed circulating PRL levels resulted in suppression of ex vivo blastogenic responses of lymphocytes from treated mice. Cysteamine 23-33 prolactin Mus musculus 72-75 1569180-0 1992 Cysteamine enhances the procoagulant activity of Factor VIII-East Hartford, a dysfunctional protein due to a light chain thrombin cleavage site mutation (arginine-1689 to cysteine). Cysteamine 0-10 cytochrome c oxidase subunit 8A Homo sapiens 56-60 1569180-0 1992 Cysteamine enhances the procoagulant activity of Factor VIII-East Hartford, a dysfunctional protein due to a light chain thrombin cleavage site mutation (arginine-1689 to cysteine). Cysteamine 0-10 coagulation factor II, thrombin Homo sapiens 121-129 1569180-3 1992 Cysteamine concentrations between 0.1 and 10 mM caused dose- and time-dependent increases in FVIII-EH VIII:C activity, as much as 14-fold (to 35 and 62 U/dl for the two patients tested). Cysteamine 0-10 coagulation factor VIII Homo sapiens 93-98 1569180-3 1992 Cysteamine concentrations between 0.1 and 10 mM caused dose- and time-dependent increases in FVIII-EH VIII:C activity, as much as 14-fold (to 35 and 62 U/dl for the two patients tested). Cysteamine 0-10 cytochrome c oxidase subunit 8A Homo sapiens 94-98 1569180-5 1992 Thrombin cleavage of the FVIII-EH light chain in the presence of cysteamine was documented by immunoadsorption and analysis. Cysteamine 65-75 coagulation factor II, thrombin Homo sapiens 0-8 1569180-5 1992 Thrombin cleavage of the FVIII-EH light chain in the presence of cysteamine was documented by immunoadsorption and analysis. Cysteamine 65-75 coagulation factor VIII Homo sapiens 25-30 1569180-7 1992 Cysteamine augmentation of FVIII-EH VIII:C was abolished by the simultaneous addition of N-ethyl maleimide or iodoacetamide, but these sulfhydryl blocking agents did not prevent the VIII:C increase and light chain cleavage by thrombin if the plasma samples were dialyzed to remove the inhibitors before adding the cysteamine. Cysteamine 0-10 coagulation factor VIII Homo sapiens 27-32 1569180-7 1992 Cysteamine augmentation of FVIII-EH VIII:C was abolished by the simultaneous addition of N-ethyl maleimide or iodoacetamide, but these sulfhydryl blocking agents did not prevent the VIII:C increase and light chain cleavage by thrombin if the plasma samples were dialyzed to remove the inhibitors before adding the cysteamine. Cysteamine 0-10 cytochrome c oxidase subunit 8A Homo sapiens 28-32 1569180-7 1992 Cysteamine augmentation of FVIII-EH VIII:C was abolished by the simultaneous addition of N-ethyl maleimide or iodoacetamide, but these sulfhydryl blocking agents did not prevent the VIII:C increase and light chain cleavage by thrombin if the plasma samples were dialyzed to remove the inhibitors before adding the cysteamine. Cysteamine 0-10 cytochrome c oxidase subunit 8A Homo sapiens 36-40 1569180-7 1992 Cysteamine augmentation of FVIII-EH VIII:C was abolished by the simultaneous addition of N-ethyl maleimide or iodoacetamide, but these sulfhydryl blocking agents did not prevent the VIII:C increase and light chain cleavage by thrombin if the plasma samples were dialyzed to remove the inhibitors before adding the cysteamine. Cysteamine 0-10 coagulation factor II, thrombin Homo sapiens 226-234 1569180-10 1992 This bond is cleaved by cysteamine to form a new mixed disulfide, a pseudolysine that restores a thrombin cleavage site that is essential for procoagulant function. Cysteamine 24-34 coagulation factor II, thrombin Homo sapiens 97-105 1325466-1 1992 The thiol groups of leucinthiol, cysteamine and cysteine incorporated into opioid peptides enkephalin and morphiceptin were activated by the 3-nitro-2-pyridinesulphenyl (Npys) group to form mixed disulphides highly reactive to a free thiol. Cysteamine 33-43 proenkephalin Rattus norvegicus 91-101 1315979-2 1992 CGRP-li but not NKA-, galanin-, VIP- or NPY-li was decreased in gastric and duodenal samples following a single ulcerogenic dose of cysteamine (900 mg/kg p.o.). Cysteamine 132-142 calcitonin-related polypeptide alpha Rattus norvegicus 0-4 1315979-7 1992 Duodenal CGRP-li is selectively decreased by the duodenal ulcerogen cysteamine during the acute phase of ulcers formation and might be among the local mediators which afford protection against the ulcerogenic stimuli. Cysteamine 68-78 calcitonin-related polypeptide alpha Rattus norvegicus 9-13 1581851-4 1992 Reducing the dose of NAC or cysteamine by 50% greatly reduced their hepatoprotective effect while the co-administration of the reduced doses of NAC (250 mg/kg) and cysteamine (50 mg/kg) following acetaminophen overdose prevented elevation of serum ALT activity (39.2 +/- 1.17 and 32.5 +/- 5.63 U/mL at 12 and 24 h post-injection, p less than 0.001) and preserved normal mouse hepatic histology. Cysteamine 28-38 glutamic pyruvic transaminase, soluble Mus musculus 248-251 1581851-1 1992 N-Acetylcysteine (NAC) is protective against acetaminophen-induced hepatotoxicity primarily by providing precursor for the glutathione synthetase pathway, while cysteamine has been demonstrated to alter the cytochrome P-450 dependent formation of toxic acetaminophen metabolite. Cysteamine 161-171 cytochrome P450, family 21, subfamily a, polypeptide 1 Mus musculus 207-223 1581851-3 1992 Administration of cysteamine (100 mg/kg) or NAC (500 mg/kg) significantly reduced serum ALT activity (p less than 0.001). Cysteamine 18-28 glutamic pyruvic transaminase, soluble Mus musculus 88-91 1314592-0 1992 Cysteamine selectively enhances neuropeptide Y2 receptor binding activity. Cysteamine 0-10 neuropeptide Y receptor Y2 Bos taurus 45-56 1314592-2 1992 Cysteamine (10 microM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting cross-linking efficiency. Cysteamine 0-10 neuropeptide Y Bos taurus 53-56 1314592-2 1992 Cysteamine (10 microM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting cross-linking efficiency. Cysteamine 0-10 neuropeptide Y receptor Y2 Bos taurus 82-93 1314592-5 1992 These studies suggest that cysteamine may change the conformation of the NPY Y2 receptor and increase its binding activity. Cysteamine 27-37 neuropeptide Y receptor Y2 Bos taurus 73-88 1540621-2 1992 S-Aminoethylcysteine, which could be considered as the natural precursor of the ketimine, is produced from L-serine and cysteamine by the action of the enzyme cystathionine-beta-synthase. Cysteamine 120-130 cystathionine beta-synthase Homo sapiens 159-186 1578802-0 1992 [An experimental study of adrenalin-stimulated gastric acid secretion and gastrin secretion in rats of cysteamine-induced duodenal ulcer]. Cysteamine 103-113 gastrin Rattus norvegicus 74-81 1578802-4 1992 Serum gastrin levels and plasma noradrenaline levels increased by cysteamine administration. Cysteamine 66-76 gastrin Rattus norvegicus 6-13 1358561-8 1992 The functional importance of these receptors was demonstrated by blocking endogenous SRIH action with cysteamine, which resulted in an increase in GHRH mRNA levels and desaturation of SRIH receptors in the ventrolateral part of the arcuate nucleus. Cysteamine 102-112 growth hormone releasing hormone Homo sapiens 147-151 1620722-0 1992 Diamine oxidase activity in the duodenal mucosa of rats with cysteamine-induced ulceration. Cysteamine 61-71 amine oxidase, copper containing 1 Rattus norvegicus 0-15 1620722-2 1992 The effect of cysteamine on the activity of diamine oxidase (DAO, histaminase) in the duodenal mucosa of the rat was investigated. Cysteamine 14-24 amine oxidase, copper containing 1 Rattus norvegicus 44-59 1620722-2 1992 The effect of cysteamine on the activity of diamine oxidase (DAO, histaminase) in the duodenal mucosa of the rat was investigated. Cysteamine 14-24 amine oxidase, copper containing 1 Rattus norvegicus 61-64 1620722-2 1992 The effect of cysteamine on the activity of diamine oxidase (DAO, histaminase) in the duodenal mucosa of the rat was investigated. Cysteamine 14-24 amine oxidase, copper containing 1 Rattus norvegicus 66-77 19215503-11 1991 Cysteamine, which depletes hypothalamic somatostatin, increased serum GH in separated 2-day-old pups, and further increased the suckling-induced levels of serum GH. Cysteamine 0-10 somatostatin Rattus norvegicus 40-52 1687422-1 1991 Single subcutaneous administration of cysteamine (2-aminoethanethiol, CSH) produces duodenal ulceration in rats within 24 h. Depletion of circulating and tissue somatostatin (SOM), hypergastrinemia and gastric acid hypersecretion have all been postulated as the pathophysiological response to CSH leading to ulceration. Cysteamine 38-48 somatostatin Rattus norvegicus 161-173 1687422-1 1991 Single subcutaneous administration of cysteamine (2-aminoethanethiol, CSH) produces duodenal ulceration in rats within 24 h. Depletion of circulating and tissue somatostatin (SOM), hypergastrinemia and gastric acid hypersecretion have all been postulated as the pathophysiological response to CSH leading to ulceration. Cysteamine 38-48 somatostatin Rattus norvegicus 175-178 19215503-11 1991 Cysteamine, which depletes hypothalamic somatostatin, increased serum GH in separated 2-day-old pups, and further increased the suckling-induced levels of serum GH. Cysteamine 0-10 gonadotropin releasing hormone receptor Rattus norvegicus 70-72 19215503-11 1991 Cysteamine, which depletes hypothalamic somatostatin, increased serum GH in separated 2-day-old pups, and further increased the suckling-induced levels of serum GH. Cysteamine 0-10 gonadotropin releasing hormone receptor Rattus norvegicus 161-163 19215503-12 1991 Cysteamine partially prevented the GH-decreasing effect of ATR. Cysteamine 0-10 gonadotropin releasing hormone receptor Rattus norvegicus 35-37 1713245-6 1991 Cysteamine treatment of the very low density lipoproteins indicated that the mutant apoE contained only one cysteine residue, suggesting that apoE3 was the parental form. Cysteamine 0-10 apolipoprotein E Homo sapiens 84-88 1677378-3 1991 Plasmid DNA was irradiated with fast neutrons, and the protection by cysteamine against strand breakage (ssb and dsb) was evaluated in the presence and absence of oxygen. Cysteamine 69-79 small RNA binding exonuclease protection factor La Homo sapiens 105-108 1677378-11 1991 At low ionic strength the PF(ssb) of cysteamine is higher for neutrons than for gamma-irradiation. Cysteamine 37-47 small RNA binding exonuclease protection factor La Homo sapiens 29-32 1685842-2 1991 Such C afferent-induced facilitation was blocked reversibly by cysteamine (50 mg.kg-1), a somatostatin depletor, without affecting the basic mechanisms of flexor reflexes, suggesting an important role played by somatostatin in transmission and/or modulation of nociceptive information in the spinal cord. Cysteamine 63-73 somatostatin Felis catus 90-102 1685842-2 1991 Such C afferent-induced facilitation was blocked reversibly by cysteamine (50 mg.kg-1), a somatostatin depletor, without affecting the basic mechanisms of flexor reflexes, suggesting an important role played by somatostatin in transmission and/or modulation of nociceptive information in the spinal cord. Cysteamine 63-73 somatostatin Felis catus 211-223 1678255-7 1991 Furthermore, peripheral administration of cysteamine and intrastriatal injection of specific somatostatin antisera both cause the eventual disappearance of Peak 5, suggesting that somatostatin (which oxidases in vitro at approx +800 mV), or a structurally related peptide, could be the principal component of striatal Peak 5. Cysteamine 42-52 somatostatin Rattus norvegicus 180-192 19215509-0 1991 Somatostatin depletion by cysteamine increases somatostatin binding and growth hormone-releasing factor messenger ribonucleic Acid in the arcuate nucleus. Cysteamine 26-36 growth hormone releasing hormone Rattus norvegicus 72-103 1713245-6 1991 Cysteamine treatment of the very low density lipoproteins indicated that the mutant apoE contained only one cysteine residue, suggesting that apoE3 was the parental form. Cysteamine 0-10 apolipoprotein E Homo sapiens 142-147 1648719-6 1991 Biological studies on the effects of increased brain somatostatin showed a facilitation in learning behavioural tasks, while brain somatostatin depletion by cysteamine caused memory loss. Cysteamine 157-167 somatostatin Homo sapiens 131-143 1719774-2 1991 Using three duodenal ulcerogens, namely cysteamine, dulcerozine or mepirizole given in a single oral dose, a decrease of duodenal CGRP-li and SP-li was observed. Cysteamine 40-50 calcitonin-related polypeptide alpha Rattus norvegicus 130-134 1719774-3 1991 Time-relationship studies of this phenomenon show that CGRP-li and SP-li were decreased concomitantly to the formation of gastroduodenal ulcers after the administration of cysteamine (900 mg/kg p.o.). Cysteamine 172-182 calcitonin-related polypeptide alpha Rattus norvegicus 55-59 1719774-4 1991 Pretreatment with the selective sensory neurotoxin capsaicin induced CGRP-li decrease in the duodenum, which was not further decreased by an ulcerogenic dose of cysteamine, indicating that cysteamine induced a release of CGRP-li of capsaicin-sensitive origin. Cysteamine 189-199 calcitonin-related polypeptide alpha Rattus norvegicus 69-73 1719774-4 1991 Pretreatment with the selective sensory neurotoxin capsaicin induced CGRP-li decrease in the duodenum, which was not further decreased by an ulcerogenic dose of cysteamine, indicating that cysteamine induced a release of CGRP-li of capsaicin-sensitive origin. Cysteamine 189-199 calcitonin-related polypeptide alpha Rattus norvegicus 221-225 1943468-0 1991 Comparison of efficacy of cysteamine in depleting prolactin immunoreactivity in different hyperprolactinemic animal models. Cysteamine 26-36 prolactin Rattus norvegicus 50-59 1943468-1 1991 We have examined the effects of cysteamine on its ability to deplete prolactin in various states of hyperprolactinemia. Cysteamine 32-42 prolactin Rattus norvegicus 69-78 1943468-2 1991 Administration of subtoxic doses of cysteamine (75 and 150 mg/kg,sc) dramatically reduces serum prolactin levels as well as pituitary prolactin content in a dose-dependent manner in estrogen-primed brown Irish ACI female rats. Cysteamine 36-46 prolactin Rattus norvegicus 96-105 1943468-2 1991 Administration of subtoxic doses of cysteamine (75 and 150 mg/kg,sc) dramatically reduces serum prolactin levels as well as pituitary prolactin content in a dose-dependent manner in estrogen-primed brown Irish ACI female rats. Cysteamine 36-46 prolactin Rattus norvegicus 134-143 1943468-4 1991 However, a significant reduction in serum prolactin levels was seen in these same tumor bearing animals at only the 150 mg/kg dose of cysteamine. Cysteamine 134-144 prolactin Rattus norvegicus 42-51 1943468-5 1991 Interestingly, the prolactin content of each of the prolactin secreting tumors, although reduced by cysteamine administration, the effect was neither dose-dependent nor as dramatic as that observed in the anterior pituitary gland proper. Cysteamine 100-110 prolactin Rattus norvegicus 19-28 1943468-5 1991 Interestingly, the prolactin content of each of the prolactin secreting tumors, although reduced by cysteamine administration, the effect was neither dose-dependent nor as dramatic as that observed in the anterior pituitary gland proper. Cysteamine 100-110 prolactin Rattus norvegicus 52-61 1943468-6 1991 These data demonstrate that cysteamine can significantly lower prolactin concentrations in hyperprolactinemia. Cysteamine 28-38 prolactin Rattus norvegicus 63-72 1943468-7 1991 Further, ectopic prolactin secreting pituitary tissue appears less sensitive to the prolactin-depleting effects of cysteamine. Cysteamine 115-125 prolactin Rattus norvegicus 17-26 1943468-7 1991 Further, ectopic prolactin secreting pituitary tissue appears less sensitive to the prolactin-depleting effects of cysteamine. Cysteamine 115-125 prolactin Rattus norvegicus 84-93 1781077-9 1991 The SSB effect of H2O2 and gamma rays was reduced by addition of the radical scavenger cysteamine to the cells before treatment, but cysteamine did not reduce the SSB effect of direct exposure to ultrasonic cavitation. Cysteamine 87-97 lupus La protein Cricetulus griseus 4-7 1976754-6 1990 Cysteamine, which has been reported to deplete SS content and to increase SS release in brain, augmented the basal and evoked release of ACh from hippocampal slices, without affecting SS-like content and release. Cysteamine 0-10 somatostatin Rattus norvegicus 47-49 1980686-7 1990 administration of cysteamine (300 mg/kg) to 12-week-old birds depleted hypothalamic SRIF stores and decreased the density of 125I-[Tyr1]-SRIF-binding sites in the caudal and cephalic lobes of the chicken pituitary gland. Cysteamine 18-28 somatostatin 1 Gallus gallus 84-88 1980686-7 1990 administration of cysteamine (300 mg/kg) to 12-week-old birds depleted hypothalamic SRIF stores and decreased the density of 125I-[Tyr1]-SRIF-binding sites in the caudal and cephalic lobes of the chicken pituitary gland. Cysteamine 18-28 somatostatin 1 Gallus gallus 137-141 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 79-89 somatostatin 1 Gallus gallus 17-21 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 79-89 somatostatin 1 Gallus gallus 37-41 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 79-89 somatostatin 1 Gallus gallus 37-41 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 164-174 somatostatin 1 Gallus gallus 17-21 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 164-174 somatostatin 1 Gallus gallus 37-41 1980686-8 1990 The reduction in SRIF content and in SRIF-binding sites occurred within 1 h of cysteamine administration and was maintained for at least 24 h. In 6-week-old birds, cysteamine (300 mg/kg) administration suppressed pituitary binding of 125I-[Tyr1]-SRIF for at least 5 days. Cysteamine 164-174 somatostatin 1 Gallus gallus 37-41 1977581-0 1990 Cysteamine-induced enhancement of growth hormone-releasing factor (GRF) immunoreactivity in arcuate neurons: morphological evidence for putative somatostatin/GRF interactions within hypothalamus. Cysteamine 0-10 growth hormone releasing hormone Homo sapiens 34-65 1977581-0 1990 Cysteamine-induced enhancement of growth hormone-releasing factor (GRF) immunoreactivity in arcuate neurons: morphological evidence for putative somatostatin/GRF interactions within hypothalamus. Cysteamine 0-10 growth hormone releasing hormone Homo sapiens 67-70 1977581-0 1990 Cysteamine-induced enhancement of growth hormone-releasing factor (GRF) immunoreactivity in arcuate neurons: morphological evidence for putative somatostatin/GRF interactions within hypothalamus. Cysteamine 0-10 growth hormone releasing hormone Homo sapiens 158-161 1982527-6 1990 Indeed, pretreatment with cysteamine decreased SRIF concentration in the neuronal cultures and twice as many binding sites as in control cultures of 21 DIV were measured. Cysteamine 26-36 somatostatin Mus musculus 47-51 1699833-2 1990 To determine whether cholecystokinin secretion is regulated by endogenous somatostatin, somatostatin deficiency was induced in vivo with cysteamine (250 mg/kg body wt, IV) or anti-somatostatin antiserum in anaesthetized rats and in vitro with cysteamine (30 micrograms/mL) in a rat duodenum-incubation system. Cysteamine 137-147 somatostatin Rattus norvegicus 88-100 1699833-4 1990 Cysteamine induced a marked decrease in duodenal immunoreactive somatostatin both in vivo (50%) and in vitro (60%). Cysteamine 0-10 somatostatin Rattus norvegicus 64-76 1699833-7 1990 The rate of amylase secretion in gastrectomized animals increased from 7.2 +/- 2.0 U to 15.0 +/- 2.2 U 20 minutes after cysteamine administration (P less than 0.01), indicating that the effect was not due to the presence of gastrin. Cysteamine 120-130 gastrin Rattus norvegicus 224-231 2289475-1 1990 The time-dependent pro- and anticonvulsant effects of cysteamine, a depletor of somatostatin, were investigated on the development and expression of amygdaloid kindled seizures. Cysteamine 54-64 somatostatin Homo sapiens 80-92 2289475-6 1990 Since it has been reported that somatostatin is released during generalized seizures, the seizures given 4 h after cysteamine may encourage the somatostatin depletion by cysteamine and thereby potentiate its later anticonvulsant effects. Cysteamine 115-125 somatostatin Homo sapiens 32-44 2289475-6 1990 Since it has been reported that somatostatin is released during generalized seizures, the seizures given 4 h after cysteamine may encourage the somatostatin depletion by cysteamine and thereby potentiate its later anticonvulsant effects. Cysteamine 115-125 somatostatin Homo sapiens 144-156 2289475-6 1990 Since it has been reported that somatostatin is released during generalized seizures, the seizures given 4 h after cysteamine may encourage the somatostatin depletion by cysteamine and thereby potentiate its later anticonvulsant effects. Cysteamine 170-180 somatostatin Homo sapiens 32-44 2289475-6 1990 Since it has been reported that somatostatin is released during generalized seizures, the seizures given 4 h after cysteamine may encourage the somatostatin depletion by cysteamine and thereby potentiate its later anticonvulsant effects. Cysteamine 170-180 somatostatin Homo sapiens 144-156 1976754-6 1990 Cysteamine, which has been reported to deplete SS content and to increase SS release in brain, augmented the basal and evoked release of ACh from hippocampal slices, without affecting SS-like content and release. Cysteamine 0-10 somatostatin Rattus norvegicus 74-76 1976754-6 1990 Cysteamine, which has been reported to deplete SS content and to increase SS release in brain, augmented the basal and evoked release of ACh from hippocampal slices, without affecting SS-like content and release. Cysteamine 0-10 somatostatin Rattus norvegicus 74-76 2280190-7 1990 Cysteamine modification of apoE3 resulted in an apoE4-like distribution, demonstrating that a positive charge at position 112 determined the apoE4 distribution and that the effect was not exclusively due to the presence of arginine at this position. Cysteamine 0-10 apolipoprotein E Homo sapiens 27-32 2289528-6 1990 IL-1 beta also reduced the severity of gastric damage induced by indomethacin and the duodenal ulceration induced by cysteamine. Cysteamine 117-127 interleukin 1 beta Rattus norvegicus 0-9 2280190-7 1990 Cysteamine modification of apoE3 resulted in an apoE4-like distribution, demonstrating that a positive charge at position 112 determined the apoE4 distribution and that the effect was not exclusively due to the presence of arginine at this position. Cysteamine 0-10 apolipoprotein E Homo sapiens 48-53 2280190-7 1990 Cysteamine modification of apoE3 resulted in an apoE4-like distribution, demonstrating that a positive charge at position 112 determined the apoE4 distribution and that the effect was not exclusively due to the presence of arginine at this position. Cysteamine 0-10 apolipoprotein E Homo sapiens 141-146 1978756-0 1990 [Effect of cysteamine on the exhaustion of somatotropin release inhibiting hormone and its mechanism]. Cysteamine 11-21 growth hormone 1 Homo sapiens 43-55 19215388-3 1990 Immunohistochemical examinations revealed a marked decrease of GRF and SRIF immunoreactivity in the median eminence of the cysteamine-treated rats with arcuate nucleus lesions. Cysteamine 123-133 growth hormone releasing hormone Rattus norvegicus 63-66 19215388-4 1990 The intravenous injection of 5 mug of hGRF every 3 h caused equivalent surges of GH in the cysteamine-treated rats with arcuate nucleus lesions. Cysteamine 91-101 growth hormone releasing hormone Homo sapiens 38-42 2110966-3 1990 In intact cells, however, cysteamine inhibited acid prolactin protease activity and beta-galactosidase. Cysteamine 26-36 galactosidase, beta 1 Rattus norvegicus 84-102 1970723-0 1990 Structural studies on the inactivation of gamma-glutamylcysteine synthetase by the disulphide analogues of radioprotective cysteamine derivatives. Cysteamine 123-133 glutamate-cysteine ligase catalytic subunit Homo sapiens 42-75 1972871-5 1990 Inactivation of somatostatin by the addition of cysteamine partially suppressed the inhibitory effect of bombesin on glandular secretion. Cysteamine 48-58 somatostatin Homo sapiens 16-28 1972871-5 1990 Inactivation of somatostatin by the addition of cysteamine partially suppressed the inhibitory effect of bombesin on glandular secretion. Cysteamine 48-58 gastrin releasing peptide Homo sapiens 105-113 2241425-8 1990 The different efficiency of pantethine and its metabolite cysteamine might be connected to the low pantetheinase activity of the brain tissue; however, some direct effects of pantethine cannot be excluded. Cysteamine 58-68 vanin 1 Rattus norvegicus 99-112 34563889-6 2022 The cysteamine layer directly anchored to the gold surface ensured that the packing density of Gly-Met-Fc in the receptor layer was appropriate for the sensitive detection of MMP-9 in its active form. Cysteamine 4-14 matrix metallopeptidase 9 Homo sapiens 175-180 2341812-6 1990 Cysteamine modification and isoelectric focusing showed that, like apoE2(158 Arg----Cys), the second apoE2 isoform also contained two cysteine residues. Cysteamine 0-10 apolipoprotein E Homo sapiens 101-106 1968091-11 1990 While no adequate SS antagonist is available, the greater sensitivity to exogenous SS, in retinas depleted of their SS content (with cysteamine), suggests a role for endogenous SS. Cysteamine 133-143 somatostatin Oryctolagus cuniculus 83-85 1968091-11 1990 While no adequate SS antagonist is available, the greater sensitivity to exogenous SS, in retinas depleted of their SS content (with cysteamine), suggests a role for endogenous SS. Cysteamine 133-143 somatostatin Oryctolagus cuniculus 83-85 1968091-11 1990 While no adequate SS antagonist is available, the greater sensitivity to exogenous SS, in retinas depleted of their SS content (with cysteamine), suggests a role for endogenous SS. Cysteamine 133-143 somatostatin Oryctolagus cuniculus 83-85 2402177-7 1990 Pantethine may act to reduce oxytocin and vasopressin content through intracellular conversion to cysteamine. Cysteamine 98-108 arginine vasopressin Rattus norvegicus 42-53 2277850-2 1990 Cysteamine is formed by degradation of coenzyme A (CoA) and causes somatostatin (SS), prolactin and noradrenaline depletion in the brain and peripheral tissues. Cysteamine 0-10 prolactin Homo sapiens 86-95 2277850-6 1990 Cysteamine has several established (cystinosis, radioprotection, acetaminophen poisoning) and theoretical (Huntington"s disease, prolactin-secreting adenomas) indications in clinical practice. Cysteamine 0-10 prolactin Homo sapiens 129-138 34498746-12 2022 Increased tissue expression of bax and caspase-3 was reversed by cysteamine. Cysteamine 65-75 BCL2 associated X, apoptosis regulator Rattus norvegicus 31-34 34498746-12 2022 Increased tissue expression of bax and caspase-3 was reversed by cysteamine. Cysteamine 65-75 caspase 3 Rattus norvegicus 39-48 2332716-3 1990 Cysteamine itself, specifically reduces plasma and pituitary prolactin. Cysteamine 0-10 prolactin Rattus norvegicus 61-70 2332716-8 1990 However, cysteamine was found to be more efficacious than pantethine on a molar basis with regard to depleting the plasma concentration of prolactin in hyperprolactinaemic rats. Cysteamine 9-19 prolactin Rattus norvegicus 139-148 2310618-0 1990 Histamine, histamine formation capacity and gastrin in cysteamine-induced peptic ulcer. Cysteamine 55-65 gastrin Rattus norvegicus 44-51 2310618-10 1990 A direct relationship was found between plasma gastrin and HFC in rats given cysteamine. Cysteamine 77-87 gastrin Rattus norvegicus 47-54 2297224-5 1990 The enzymatic recovery of GPD activity was observed either without addition of thiols to the medium or by incubation of a sonicated cell mixture with 2 mM cysteine, cystine, cysteamine, or glutathione (GSH); GSSG had no effect. Cysteamine 174-184 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-29 2403372-1 1990 The degradation of native albumin by human spleen cathepsin D was inhibited by GSH, cysteine and cysteamine. Cysteamine 97-107 cathepsin D Homo sapiens 50-61 1976475-0 1990 Effects of cysteamine administration on plasma concentration of metabolites, pancreatic glucagon and insulin in the chicken. Cysteamine 11-21 insulin Gallus gallus 101-108 1976475-4 1990 In the short term (1 hr), cysteamine increased plasma levels of glucose, free fatty acids and insulin, and decreased that of alpha-amino non protein nitrogen. Cysteamine 26-36 insulin Gallus gallus 94-101 1976475-8 1990 The disposal of an oral glucose load was impaired and the glucose-induced inhibition of pancreatic glucagon and stimulation of insulin release were blunted 17 hr after cysteamine administration. Cysteamine 168-178 insulin Gallus gallus 127-134 33801798-0 2021 Electrochemical Immunosensor for the Quantification of S100B at Clinically Relevant Levels Using a Cysteamine Modified Surface. Cysteamine 99-109 S100 calcium binding protein B Homo sapiens 55-60 26629546-10 2015 Cysteamine reduced CF sputum viscoelasticity, sputum spinnbarkeit cysteamine 11.1 mm/s (95% CI 3.95-18.2) vs DNAse 1.69 mm/s (95% CI 0.73-2.65), p = 0.016. Cysteamine 0-10 deoxyribonuclease 1 Homo sapiens 109-116 34842019-3 2022 DHL with concomitant TP53 mutation appears to be associated with a very poor prognosis. Cysteamine 0-3 tumor protein p53 Homo sapiens 21-25 34822973-7 2022 The measurement of melanin and tyrosinase activities was assessed after cells treatment with free and encapsulated cysteamine. Cysteamine 115-125 tyrosinase Homo sapiens 19-41 34822973-12 2022 The free and the encapsulated cysteamine in suspension (either original or freeze-dried) did not show any cytotoxic effect, inhibited the melanin synthesis as well as the tyrosinase activity. Cysteamine 30-40 tyrosinase Homo sapiens 171-181 34587370-0 2022 Cysteamine administration in lambs grazing on mountain pastures: Effects on the body weight, antioxidant capacity, thyroid hormones and growth hormone secretion. Cysteamine 0-10 somatotropin Ovis aries 136-150 34580769-4 2021 Previous spectroscopic characterizations revealed that ADO likely binds substrate cysteamine in a monodentate fashion, while a mass spectrometry study provided evidence that a thioether crosslink can form between Cys206 and Tyr208 (mouse ADO numbering). Cysteamine 82-92 2-aminoethanethiol (cysteamine) dioxygenase Mus musculus 55-58 34580769-7 2021 Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO. Cysteamine 39-49 2-aminoethanethiol (cysteamine) dioxygenase Mus musculus 243-246 34580769-7 2021 Alternatively, cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO to yield a low-spin (S = 1/2) EPR signal that is distinct from that observed for cyanide/Cys-bound Fe(III)CDO, revealing differences in the active-site pockets between ADO and CDO. Cysteamine 39-49 cysteine dioxygenase 1, cytosolic Mus musculus 251-254 34905785-8 2021 Multivariate analysis also indicated a strong association between DHL and general health literacy (HL). Cysteamine 66-69 lipase C, hepatic type Homo sapiens 99-101 34905785-11 2021 Efforts in this area should include general HL, as it is closely related to DHL. Cysteamine 76-79 lipase C, hepatic type Homo sapiens 44-46 34762398-2 2021 The open approach to the active site is consistent with the recent discovery that ADO catalyzes not only the conversion of cysteamine to hypotaurine but also the oxidation of N-terminal cysteine (Nt-Cys) peptides to their corresponding sulfinic acids as part of the eukaryotic N-degron pathway. Cysteamine 123-133 2-aminoethanethiol dioxygenase Homo sapiens 82-85 34762398-3 2021 Whole-protein models of ADO in complex with either cysteamine or an Nt-Cys peptide, generated using molecular dynamics and quantum mechanics/molecular mechanics calculations, suggest occlusion of access to the active site by peptide substrate binding. Cysteamine 51-61 2-aminoethanethiol dioxygenase Homo sapiens 24-27 34428184-0 2021 Propensity of immunoglobulin A self-aggregation via "tailpiece" cysteine-471 and treatment of IgA nephropathy using cysteamine. Cysteamine 116-126 CD79a molecule Homo sapiens 94-97 34850511-2 2022 Herein, by using the sensor of quartz crystal microbalance (QCM) as the sacrificial probe, the etching reaction of gold has been studied in employing cysteamine (CS) as a typical thiol etchant. Cysteamine 150-160 citrate synthase Homo sapiens 162-164 34428184-9 2021 Specifically, cystine-reducing drug cysteamine used for treatment of cystinosis showed a remarkable potency in preventing IgA from self-aggregation. Cysteamine 36-46 CD79a molecule Homo sapiens 122-125 34428184-10 2021 When administrated to rat and mouse models of IgA nephropathy, cysteamine significantly reduced glomerular IgA deposition. Cysteamine 63-73 immunoglobulin heavy constant alpha Mus musculus 107-110 34428184-11 2021 Collectively, our results revealed a novel molecular mechanism for aberrant formation of IgA aggregates, to which repurposed cystinosis drug cysteamine was efficacious in preventing renal IgA deposition. Cysteamine 141-151 immunoglobulin heavy constant alpha Mus musculus 89-92 34428184-11 2021 Collectively, our results revealed a novel molecular mechanism for aberrant formation of IgA aggregates, to which repurposed cystinosis drug cysteamine was efficacious in preventing renal IgA deposition. Cysteamine 141-151 immunoglobulin heavy constant alpha Mus musculus 188-191 34493066-0 2021 Cysteamine Decreases Low-Density Lipoprotein Oxidation, Causes Regression of Atherosclerosis, and Improves Liver and Muscle Function in Low-Density Lipoprotein Receptor-Deficient Mice. Cysteamine 0-10 low density lipoprotein receptor Mus musculus 136-168 34508780-1 2021 Cysteamine dioxygenase (ADO) plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis in humans by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate. Cysteamine 150-160 2-aminoethanethiol dioxygenase Homo sapiens 0-22 34508780-1 2021 Cysteamine dioxygenase (ADO) plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis in humans by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate. Cysteamine 150-160 2-aminoethanethiol dioxygenase Homo sapiens 24-27 34493066-8 2021 The liver lipid levels and expression of cluster of differentiation 68, acetyl-coenzyme A acetyltransferase 2, cytochromes P450 (CYP)27, and proinflammatory cytokines and chemokines were decreased by cysteamine. Cysteamine 200-210 acetyl-Coenzyme A acetyltransferase 2 Mus musculus 72-109 34493066-8 2021 The liver lipid levels and expression of cluster of differentiation 68, acetyl-coenzyme A acetyltransferase 2, cytochromes P450 (CYP)27, and proinflammatory cytokines and chemokines were decreased by cysteamine. Cysteamine 200-210 cytochrome P450, family 27, subfamily a, polypeptide 1 Mus musculus 123-135 2598042-0 1989 Morris water task impairment and hypoactivity following cysteamine-induced reductions of somatostatin-like immunoreactivity. Cysteamine 56-66 somatostatin Rattus norvegicus 89-101 34438677-5 2021 The contents of alkaline phosphatase (ALP), immunoglobulin G (IgG), serine (Ser), and isoleucine (Ile) were elevated (p < 0.05) while the contents of albumin (ALB) and aspartic acid (Asp) were reduced (p < 0.05) in the serum after coated cysteamine supplementation. Cysteamine 238-248 ALPA Sus scrofa 16-36 34438677-5 2021 The contents of alkaline phosphatase (ALP), immunoglobulin G (IgG), serine (Ser), and isoleucine (Ile) were elevated (p < 0.05) while the contents of albumin (ALB) and aspartic acid (Asp) were reduced (p < 0.05) in the serum after coated cysteamine supplementation. Cysteamine 238-248 ALPA Sus scrofa 38-41 34438677-5 2021 The contents of alkaline phosphatase (ALP), immunoglobulin G (IgG), serine (Ser), and isoleucine (Ile) were elevated (p < 0.05) while the contents of albumin (ALB) and aspartic acid (Asp) were reduced (p < 0.05) in the serum after coated cysteamine supplementation. Cysteamine 238-248 IGG Sus scrofa 44-60 34438677-5 2021 The contents of alkaline phosphatase (ALP), immunoglobulin G (IgG), serine (Ser), and isoleucine (Ile) were elevated (p < 0.05) while the contents of albumin (ALB) and aspartic acid (Asp) were reduced (p < 0.05) in the serum after coated cysteamine supplementation. Cysteamine 238-248 IGG Sus scrofa 62-65 34438677-5 2021 The contents of alkaline phosphatase (ALP), immunoglobulin G (IgG), serine (Ser), and isoleucine (Ile) were elevated (p < 0.05) while the contents of albumin (ALB) and aspartic acid (Asp) were reduced (p < 0.05) in the serum after coated cysteamine supplementation. Cysteamine 238-248 albumin Sus scrofa 150-157 34438677-6 2021 Coated cysteamine supplementation resulted in greater (p < 0.05) serum superoxide dismutase (SOD) activity, the expression of interleukin-10 (IL-10) mRNA in the colon, and the CuSOD mRNA expression in the jejunum (p < 0.05) and colon (p = 0.073). Cysteamine 7-17 interleukin 10 Sus scrofa 126-140 34438677-6 2021 Coated cysteamine supplementation resulted in greater (p < 0.05) serum superoxide dismutase (SOD) activity, the expression of interleukin-10 (IL-10) mRNA in the colon, and the CuSOD mRNA expression in the jejunum (p < 0.05) and colon (p = 0.073). Cysteamine 7-17 interleukin 10 Sus scrofa 142-147 34438677-7 2021 Coated cysteamine supplementation showed an increasing trend in villus height (p = 0.060), villus height/crypt depth (V/C) (p = 0.056), the expression levels of zonula occludens-1 (ZO-1) mRNA (p = 0.061), and Occludin mRNA (p = 0.074) in the jejunum. Cysteamine 7-17 zonula occludens 1 Sus scrofa 161-179 34438677-7 2021 Coated cysteamine supplementation showed an increasing trend in villus height (p = 0.060), villus height/crypt depth (V/C) (p = 0.056), the expression levels of zonula occludens-1 (ZO-1) mRNA (p = 0.061), and Occludin mRNA (p = 0.074) in the jejunum. Cysteamine 7-17 zonula occludens 1 Sus scrofa 181-185 34438677-7 2021 Coated cysteamine supplementation showed an increasing trend in villus height (p = 0.060), villus height/crypt depth (V/C) (p = 0.056), the expression levels of zonula occludens-1 (ZO-1) mRNA (p = 0.061), and Occludin mRNA (p = 0.074) in the jejunum. Cysteamine 7-17 occludin Sus scrofa 209-217 34065481-4 2021 It consists of rabbit polyclonal antibody against HE4, covalently attached to a gold chip via cysteamine linker. Cysteamine 94-104 WAP four-disulfide core domain 2 Homo sapiens 50-53 35155380-1 2021 The main effect of Vanin-1/VNN1 is related to its pantetheinase sulfhydrylase activity, which can hydrolyze pantetheine into pantothenic acid and cysteamine. Cysteamine 146-156 vanin 1 Mus musculus 19-26 35155380-1 2021 The main effect of Vanin-1/VNN1 is related to its pantetheinase sulfhydrylase activity, which can hydrolyze pantetheine into pantothenic acid and cysteamine. Cysteamine 146-156 vanin 1 Mus musculus 27-31 34372937-10 2021 Furthermore, the in vitro experiment indicated that CS pre-treatment could significantly reverse the NADPH oxidase 2-ROS-mediated inactivation of signal transducer and activator of transcription-3 (Stat3) signaling pathway induced by H2O2 inhibition of the proliferation, tube formation, and migration of PVECs. Cysteamine 52-54 cytochrome b-245 beta chain Homo sapiens 101-116 34372937-10 2021 Furthermore, the in vitro experiment indicated that CS pre-treatment could significantly reverse the NADPH oxidase 2-ROS-mediated inactivation of signal transducer and activator of transcription-3 (Stat3) signaling pathway induced by H2O2 inhibition of the proliferation, tube formation, and migration of PVECs. Cysteamine 52-54 signal transducer and activator of transcription 3 Homo sapiens 146-196 34372937-10 2021 Furthermore, the in vitro experiment indicated that CS pre-treatment could significantly reverse the NADPH oxidase 2-ROS-mediated inactivation of signal transducer and activator of transcription-3 (Stat3) signaling pathway induced by H2O2 inhibition of the proliferation, tube formation, and migration of PVECs. Cysteamine 52-54 signal transducer and activator of transcription 3 Homo sapiens 198-203 34372937-11 2021 Meanwhile, inhibition of Stat3 significantly decreased the cell viability, tube formation and the VEGF-A protein level in CS pretreated with H2O2-cultured PVECs. Cysteamine 122-124 signal transducer and activator of transcription 3 Homo sapiens 25-30 34372937-11 2021 Meanwhile, inhibition of Stat3 significantly decreased the cell viability, tube formation and the VEGF-A protein level in CS pretreated with H2O2-cultured PVECs. Cysteamine 122-124 vascular endothelial growth factor A Homo sapiens 98-104 34372937-13 2021 The in vitro data showed that the underlying mechanism for the positive effects of CS might be related to the activation of Stat3 in PVECs. Cysteamine 83-85 signal transducer and activator of transcription 3 Homo sapiens 124-129 34275284-2 2021 Vanin-1 can hydrolyze pantetheine to pantothenic acid (vitamin B5) and cysteamine and participate in the synthesis of glutathione (GSH). Cysteamine 71-81 vanin 1 Homo sapiens 0-7 34151245-9 2021 Conclusions: PDIA4 is involved in AATD-mediated liver disease and thus represents a therapeutic target for inhibition by drugs such as cysteamine. Cysteamine 135-145 protein disulfide isomerase family A member 4 Homo sapiens 13-18 34151245-12 2021 PDI inhibition upon cysteamine treatment leads to improvements in features of AATD and hence represents a therapeutic approach for treatment of AATD-mediated liver disease. Cysteamine 20-30 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 35276214-6 2022 The carbonylation reaction was inhibited by SH compounds such as cysteamine in a dose-dependent manner with a concomitant decrease in CaMKP inhibition by ethyl gallate. Cysteamine 65-75 protein phosphatase, Mg2+/Mn2+ dependent 1F Homo sapiens 134-139 35601978-1 2022 We developed an electrochemical biosensing platform using gold-clusters, cysteamine, the spike protein of the severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) antigen and bovine serum albumin on a glassy carbon electrode able to determine the SARS-CoV-2 spike antibody. Cysteamine 73-83 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 89-94 35601978-1 2022 We developed an electrochemical biosensing platform using gold-clusters, cysteamine, the spike protein of the severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) antigen and bovine serum albumin on a glassy carbon electrode able to determine the SARS-CoV-2 spike antibody. Cysteamine 73-83 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 266-271 2606571-4 1989 Histologically, the adenocarcinomas that did develop in rats treated with cysteamine exhibited high mucin-producing activity. Cysteamine 74-84 solute carrier family 13 member 2 Rattus norvegicus 100-105 2598042-1 1989 The effects of cysteamine-induced reductions of somatostatin-like immunoreactivity (SLI) on spatial learning, passive avoidance, and locomotor activity were examined in adult Sprague-Dawley rats. Cysteamine 15-25 somatostatin Rattus norvegicus 48-60 2814066-6 1989 This is in contrast to our previous report which showed that secretin repaired the alkaline secretion in cysteamine-treated rats without affecting it in normal rats. Cysteamine 105-115 secretin Rattus norvegicus 61-69 2804053-6 1989 Cysteamine modification, which adds a positively charged group to cysteine, resulted in a shift of apoE-1Harrisburg from the E-1 to the E-2 isoform position, indicating that there is one cysteine in apoE-1Harrisburg as is the case for apoE-3. Cysteamine 0-10 apolipoprotein E Homo sapiens 99-103 2804053-6 1989 Cysteamine modification, which adds a positively charged group to cysteine, resulted in a shift of apoE-1Harrisburg from the E-1 to the E-2 isoform position, indicating that there is one cysteine in apoE-1Harrisburg as is the case for apoE-3. Cysteamine 0-10 apolipoprotein E Homo sapiens 199-203 2804053-6 1989 Cysteamine modification, which adds a positively charged group to cysteine, resulted in a shift of apoE-1Harrisburg from the E-1 to the E-2 isoform position, indicating that there is one cysteine in apoE-1Harrisburg as is the case for apoE-3. Cysteamine 0-10 apolipoprotein E Homo sapiens 235-241 2570757-4 1989 In week 18, quantitative histological analysis showed that prolonged administration of cysteamine resulted in a significant reduction in the number of GGT-positive and G6PD-positive hepatic lesions. Cysteamine 87-97 gamma-glutamyltransferase 1 Rattus norvegicus 151-154 2570757-5 1989 Histologically, hepatocellular carcinomas were significantly fewer and smaller in GGT-positive and G6PD-positive lesions in rats treated with cysteamine than in untreated rats. Cysteamine 142-152 gamma-glutamyltransferase 1 Rattus norvegicus 82-85 2570757-5 1989 Histologically, hepatocellular carcinomas were significantly fewer and smaller in GGT-positive and G6PD-positive lesions in rats treated with cysteamine than in untreated rats. Cysteamine 142-152 glucose-6-phosphate dehydrogenase Rattus norvegicus 99-103 2620935-0 1989 Effect of ayurvedic medicines on beta-glucuronidase activity of Brunner"s glands during recovery from cysteamine induced duodenal ulcers in rats. Cysteamine 102-112 glucuronidase, beta Rattus norvegicus 33-51 2811360-4 1989 The steroid-binding capacity of the glucocorticoid receptor of the 100,000 g supernatant of rat liver homogenate is preserved/restored by sulfhydryl compounds containing a mercaptoethylamine or mercaptopropylamine subunit. Cysteamine 172-190 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 36-59 2925276-6 1989 Administration of cysteamine caused a significant increase in gastric acid secretion and serum gastrin level, and a significant decrease in the labelling index of the antral mucosa. Cysteamine 18-28 gastrin Rattus norvegicus 95-102 2619420-5 1989 These results suggest that the lower efficacy of pantethine compared to cysteamine on both behavioral and neurochemical parameters is probably due to a rate-limiting activity of the enzyme pantetheinase in the conversion of pantetheine to cysteamine. Cysteamine 72-82 vanin 1 Rattus norvegicus 189-202 2619420-5 1989 These results suggest that the lower efficacy of pantethine compared to cysteamine on both behavioral and neurochemical parameters is probably due to a rate-limiting activity of the enzyme pantetheinase in the conversion of pantetheine to cysteamine. Cysteamine 239-249 vanin 1 Rattus norvegicus 189-202 2724132-1 1989 The sulfhydryl reducing agent, cysteamine, is known to functionally inactive prolactin and other neurohormones that have been recently shown to play a role as immunomodulators. Cysteamine 31-41 prolactin Mus musculus 77-86 2724132-2 1989 Cysteamine was administered to mice to evaluate its effects upon immune organ size and mitogen-induced lymphocyte proliferative responses in relation to corresponding effects on the immunomodulatory hormones, prolactin and corticosterone. Cysteamine 0-10 prolactin Mus musculus 209-218 2724132-4 1989 Serum prolactin levels were also significantly elevated with 12.5 mg/kg cysteamine. Cysteamine 72-82 prolactin Mus musculus 6-15 2724132-7 1989 Levels of both prolactin and corticosterone in the serum were significantly reduced at 400 mg/kg cysteamine. Cysteamine 97-107 prolactin Mus musculus 15-24 2724132-8 1989 A positive correlation was observed between serum prolactin levels and Con A-induced proliferation as well as between serum prolactin and corticosterone levels in cysteamine-treated mice. Cysteamine 163-173 prolactin Mus musculus 124-133 2780846-6 1989 Depleting prolactin from the blood by cysteamine, however, neither reduced the retrieving score nor disturbed ultrasound recognition. Cysteamine 38-48 prolactin Mus musculus 10-19 2587601-16 1989 We postulate that the effects are mediated directly or indirectly through the disinhibition of central appetite-regulating somatostatinergic pathways but, since cysteamine also inhibits dopamine-beta-hydroxylase, an effect on depletion of appetite-regulating central catecholamines cannot be excluded. Cysteamine 161-171 dopamine beta-hydroxylase Rattus norvegicus 186-211 2788098-1 1989 Calcitonin gene-related peptide-like immunoreactivity (CGRP-li) was decreased in duodenal samples from animals treated with ulcerogens such as dulcerozine, cysteamine or mepirizole. Cysteamine 156-166 calcitonin-related polypeptide alpha Rattus norvegicus 55-59 2925276-8 1989 With this treatment, the serum gastrin level was significantly higher than the basal level, but the stimulated serum gastrin level was significantly lower than observed that after administration of cysteamine alone. Cysteamine 198-208 gastrin Rattus norvegicus 117-124 2925276-9 1989 In contrast, concomitant administration of cysteamine and cimetidine caused a significant decrease in gastric acid secretion and significant increase in the serum gastrin level as compared to the levels seen after treatment with cysteamine alone, but had no influence on the labelling index of the antral mucosa. Cysteamine 43-53 gastrin Rattus norvegicus 163-170 2925276-9 1989 In contrast, concomitant administration of cysteamine and cimetidine caused a significant decrease in gastric acid secretion and significant increase in the serum gastrin level as compared to the levels seen after treatment with cysteamine alone, but had no influence on the labelling index of the antral mucosa. Cysteamine 229-239 gastrin Rattus norvegicus 163-170 2568000-4 1989 It is discussed whether the lower potency of pantethine on open-field behaviors and hypothalamic catecholaminergic neurotransmission is connected with the limited activity of pantetheinase, the cysteamine-generating enzyme. Cysteamine 194-204 vanin 1 Rattus norvegicus 175-188 2609341-1 1989 Administration of cysteamine to rats depressed hepatic aryl hydrocarbon hydroxylase (AHH) activity, cytochrome P-450, and total heme at 24 hr. Cysteamine 18-28 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 85-88 2609341-1 1989 Administration of cysteamine to rats depressed hepatic aryl hydrocarbon hydroxylase (AHH) activity, cytochrome P-450, and total heme at 24 hr. Cysteamine 18-28 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 100-116 2609341-0 1989 The role of heme oxygenase and aryl hydrocarbon hydroxylase in the protection by cysteamine from acetaminophen hepatotoxicity. Cysteamine 81-91 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 31-59 2609341-1 1989 Administration of cysteamine to rats depressed hepatic aryl hydrocarbon hydroxylase (AHH) activity, cytochrome P-450, and total heme at 24 hr. Cysteamine 18-28 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 55-83 2609341-6 1989 Our results indicate that cysteamine increases heme oxygenase activity in rat liver, with a subsequent decrease in total heme, AHH activity, and cytochrome P-450 content. Cysteamine 26-36 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 127-130 2609341-6 1989 Our results indicate that cysteamine increases heme oxygenase activity in rat liver, with a subsequent decrease in total heme, AHH activity, and cytochrome P-450 content. Cysteamine 26-36 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 145-161 2521554-10 1989 However, the treatment of hypophysectomized rats with insulin had no effect, and treatment of diabetic rats with growth hormone or a suppressing agent of somatostatin, cysteamine, showed trivial effects on P450-male and P450b. Cysteamine 168-178 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 220-225 3242778-0 1988 Effect of chronic cysteamine treatment on mouse liver aryl hydrocarbon hydroxylase activity. Cysteamine 18-28 cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus 54-82 2491792-1 1989 The inhibition of highly purified rat liver L-threonine dehydratase (L-threonine hydro-lyase (deaminating), EC 4.2.1.16) by aminothiols (L-cysteine, D-cysteine, cysteamine) has been studied. Cysteamine 161-171 serine dehydratase Rattus norvegicus 44-67 2920771-3 1989 Histological examination showed that adenocarcinomas that did develop in rats fed on cysteamine had high mucin-producing activity. Cysteamine 85-95 solute carrier family 13 member 2 Rattus norvegicus 105-110 2920771-4 1989 Furthermore, oral administration of cysteamine caused a significant increase in serum gastrin level and significant decreases in the antral mucosal pH and the labeling indices of the antral mucosa. Cysteamine 36-46 gastrin Rattus norvegicus 86-93 2572245-5 1989 Cysteamine (1.95 or 3.90 mM/kg) decreased the somatostatin levels both in the hypothalamus and in the striatum without influencing neuropeptide Y (NPY) and corticotropin releasing hormone (CRH) concentrations. Cysteamine 0-10 somatostatin Rattus norvegicus 46-58 2572245-5 1989 Cysteamine (1.95 or 3.90 mM/kg) decreased the somatostatin levels both in the hypothalamus and in the striatum without influencing neuropeptide Y (NPY) and corticotropin releasing hormone (CRH) concentrations. Cysteamine 0-10 corticotropin releasing hormone Rattus norvegicus 189-192 2572245-7 1989 These data suggest that the cysteamine-induced behavioural changes are related to the decrease of brain noradrenaline and somatostatin concentrations. Cysteamine 28-38 somatostatin Rattus norvegicus 122-134 2904265-1 1988 The effect of a single injection of cysteamine /CySH/ - a sulfhydryl substance, known to deplete tissue content of somatostatin /SS/ - on 3H-thymidine incorporation into DNA of rat adrenal explants incubated in vitro was investigated. Cysteamine 36-46 somatostatin Rattus norvegicus 115-127 2595299-0 1989 Epidermal growth factor inhibits cysteamine-induced duodenal ulcers in rats. Cysteamine 33-43 epidermal growth factor like 1 Rattus norvegicus 0-23 2595299-6 1989 In the SMR + cysteamine group, serum gastrin increased and the intragastric pH decreased remarkably compared to in the normal control group. Cysteamine 13-23 gastrin Rattus norvegicus 37-44 2595299-8 1989 Mucosal blood flow, the potential difference and hexosamine, as defensive factors, decreased markedly in the SMR + cysteamine group, but the administration of exogenous EGF reversed these changes. Cysteamine 115-125 epidermal growth factor like 1 Rattus norvegicus 169-172 2595299-9 1989 These results suggested that a decrease in EGF is involved in the pathogenesis of cysteamine-induced duodenal ulcers in rats. Cysteamine 82-92 epidermal growth factor like 1 Rattus norvegicus 43-46 3242778-6 1988 A small decrease in liver AHH activity was seen after 1.5 months of treatment with cysteamine. Cysteamine 83-93 cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus 26-29 3242778-9 1988 Incubation of isolated murine hepatocytes with cysteamine significantly inhibited AHH activity compared with controls. Cysteamine 47-57 cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus 82-85 3048161-9 1988 Oral cysteamine lowered leukocyte cystine over 80%, and in patients before transplant, improved growth and preserved renal function (mean creatinine clearance [+/- SE], 0.64 +/- 0.04 mL/s.1.73 m2 [38.5 +/- 2.5 mL/min.1.73 m2] in the cysteamine group compared with 0.50 +/- 0.03 mL/s.1.73 m2 [29.7 +/- 2.0 mL/min.1.73 m2] in controls; 95% CI for the difference, 1.8 to 15.8). Cysteamine 5-15 CD59 molecule (CD59 blood group) Homo sapiens 213-218 3048161-9 1988 Oral cysteamine lowered leukocyte cystine over 80%, and in patients before transplant, improved growth and preserved renal function (mean creatinine clearance [+/- SE], 0.64 +/- 0.04 mL/s.1.73 m2 [38.5 +/- 2.5 mL/min.1.73 m2] in the cysteamine group compared with 0.50 +/- 0.03 mL/s.1.73 m2 [29.7 +/- 2.0 mL/min.1.73 m2] in controls; 95% CI for the difference, 1.8 to 15.8). Cysteamine 5-15 CD59 molecule (CD59 blood group) Homo sapiens 308-313 2845919-5 1988 In analogy with cysteamine, the activities of both cysteine esters were inhibited by superoxide dismutase (less than 5 micrograms/ml) and by catalase and not by the hydroxyl-radical scavenger mannitol. Cysteamine 16-26 catalase Homo sapiens 141-149 3201126-1 1988 The effect of furazolidone, a monoamine oxidase (MAO) inhibitor, on cysteamine-induced duodenal ulcer and gut catecholamines was studied in rats, since previous reports have suggested protective effects of MAO inhibitors against other forms of experimental mucosal injury. Cysteamine 68-78 monoamine oxidase A Rattus norvegicus 49-52 3420112-0 1988 Effects of cysteamine on blood pressure: possible mediation through vasopressin release. Cysteamine 11-21 arginine vasopressin Rattus norvegicus 68-79 2897423-0 1988 Effect of local injection of cysteamine and cystamine on somatostatin and neuropeptide Y levels in the rat striatum. Cysteamine 29-39 somatostatin Rattus norvegicus 57-69 2905659-0 1988 Somatostatin and SMS 201-995 reverse the impairment of cognitive functions induced by cysteamine depletion of brain somatostatin. Cysteamine 86-96 somatostatin Rattus norvegicus 0-12 2905659-0 1988 Somatostatin and SMS 201-995 reverse the impairment of cognitive functions induced by cysteamine depletion of brain somatostatin. Cysteamine 86-96 somatostatin Rattus norvegicus 116-128 2905659-2 1988 We assessed changes in learning and memory processes by studying the effects of cysteamine, a compound that decreases somatostatin-like immunoreactivity in the brain, somatostatin and the potent somatostatin analogue, SMS 201-995, on active avoidance behaviour, assessed with a shuttle box apparatus, or on passive avoidance behaviour. Cysteamine 80-90 somatostatin Rattus norvegicus 118-130 2905659-6 1988 We also investigated the effect of cysteamine treatment on brain somatostatin-sensitive adenylate cyclase. Cysteamine 35-45 somatostatin Rattus norvegicus 65-77 2900049-6 1988 Cysteamine (90 mg/kg) treatment given s.c. produced a 50% depletion of endogenous brain somatostatin-like peptide concentrations. Cysteamine 0-10 somatostatin Homo sapiens 88-100 2900049-7 1988 Pretreatment of animals with cysteamine attenuated hemorrhage-induced elevation of plasma vasopressin levels. Cysteamine 29-39 arginine vasopressin Homo sapiens 90-101 2900014-2 1988 In the present experiments, the effects of cysteamine, a drug which reduces somatostatin levels, on the basal and dopamine-mediated motor activities were examined in the rat. Cysteamine 43-53 somatostatin Rattus norvegicus 76-88 2900014-6 1988 The direct intra-cerebral infusion of cysteamine produced a significant depletion in the levels of somatostatin at the site of injections as measured by radioimmunoassay. Cysteamine 38-48 somatostatin Rattus norvegicus 99-111 2897423-3 1988 Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Cysteamine 92-102 somatostatin Rattus norvegicus 21-33 2897423-3 1988 Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Cysteamine 92-102 somatostatin Rattus norvegicus 169-181 2897423-3 1988 Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Cysteamine 92-102 somatostatin Rattus norvegicus 169-181 2897423-3 1988 Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Cysteamine 92-102 somatostatin Rattus norvegicus 169-181 2897423-3 1988 Maximal reduction of somatostatin (by about 50%) was obtained at a dose of 50 micrograms of cysteamine or cystamine after about 6 h. All three molecular weight forms of somatostatin--somatostatin-14, somatostatin-28, and the 13,000 molecular weight form of somatostatin--were reduced, as shown by size exclusion HPLC. Cysteamine 92-102 somatostatin Rattus norvegicus 169-181 3374761-0 1988 Preferential interaction of [35S]cysteamine with pituitary secretory granule storage forms of prolactin. Cysteamine 33-43 prolactin Bos taurus 94-103 3346107-3 1988 Histological examination showed that the adenocarcinomas that did develop in rats treated with these 2 doses of cysteamine had high mucin-producing activity. Cysteamine 112-122 solute carrier family 13 member 2 Rattus norvegicus 132-137 3346107-4 1988 Furthermore, treatment with cysteamine caused significant increases in serum gastrin level and gastric acid secretion, together with significant decreases in the antral mucosal pH and the labelling indices of pyloric and oxyntic gland mucosae and gastric cancer. Cysteamine 28-38 gastrin Rattus norvegicus 77-84 2465668-7 1988 Cysteamine pre-treatment reduced the normally intense IGF-I and somatostatin immunoreactivities in the D cells. Cysteamine 0-10 insulin-like growth factor 1 Rattus norvegicus 54-59 3162218-0 1988 2-Mercaptoethylamine, a competitive inhibitor of spermidine synthase in mammalian cells. Cysteamine 0-20 spermidine synthase Homo sapiens 49-68 3162218-1 1988 Spermidine synthase from rat ventral prostate was inhibited by 2-mercaptoethylamine (MEA). Cysteamine 63-83 spermidine synthase Rattus norvegicus 0-19 3162218-1 1988 Spermidine synthase from rat ventral prostate was inhibited by 2-mercaptoethylamine (MEA). Cysteamine 85-88 spermidine synthase Rattus norvegicus 0-19 3162218-2 1988 Inhibition of spermidine synthase by MEA was competitive with respect to one of the substrates putrescine, but not competitive with respect to the other substrate decarboxylated S-adenosylmethionine. Cysteamine 37-40 spermidine synthase Homo sapiens 14-33 3162218-3 1988 MEA markedly depressed spermidine and spermine contents in human erythroid leukemia K562 cells, suggesting that these changes resulted from the inhibitory effect of MEA on spermidine synthase in situ. Cysteamine 0-3 spermidine synthase Homo sapiens 172-191 3162218-3 1988 MEA markedly depressed spermidine and spermine contents in human erythroid leukemia K562 cells, suggesting that these changes resulted from the inhibitory effect of MEA on spermidine synthase in situ. Cysteamine 165-168 spermidine synthase Homo sapiens 172-191 3374761-1 1988 Cysteamine (CySH) inhibits the immunodetectability and bioactivity of prolactin (PRL), and we have proposed that it may act by impeding the conversion from secretory granule hormone storage forms to releasable and assayable hormone. Cysteamine 0-10 prolactin Bos taurus 70-79 3374761-1 1988 Cysteamine (CySH) inhibits the immunodetectability and bioactivity of prolactin (PRL), and we have proposed that it may act by impeding the conversion from secretory granule hormone storage forms to releasable and assayable hormone. Cysteamine 0-10 prolactin Bos taurus 81-84 2829860-0 1988 Myeloperoxidase-oxidase oxidation of cysteamine. Cysteamine 37-47 myeloperoxidase Homo sapiens 0-15 2829860-1 1988 Cysteamine oxidation was shown to be catalysed by nanomolar concentrations of myeloperoxidase in a peroxidase-oxidase reaction, i.e. an O2-consuming oxidation of a compound catalysed by peroxidase without H2O2 addition. Cysteamine 0-10 myeloperoxidase Homo sapiens 78-93 2829860-2 1988 When auto-oxidation of the thiol was prevented by the metal-ion chelator diethylenetriaminepenta-acetic acid, native, but not heat-inactivated, myeloperoxidase induced changes in the u.v.-light-absorption spectrum of cysteamine. Cysteamine 217-227 myeloperoxidase Homo sapiens 144-159 2829860-8 1988 A possible reaction pathway for the myeloperoxidase-oxidase oxidation of cysteamine is discussed. Cysteamine 73-83 myeloperoxidase Homo sapiens 36-51 2829860-9 1988 These results indicate that cysteamine is a very useful substrate for studies on myeloperoxidase-oxidase activity. Cysteamine 28-38 myeloperoxidase Homo sapiens 81-96 3683075-0 1987 Effect of cysteamine on suckling-induced prolactin secretion in the rat. Cysteamine 10-20 prolactin Rattus norvegicus 41-50 3053882-5 1988 Intragastric instillation of EGF can prevent gastric ulcerations induced by aspirin as well as cysteamine in rats. Cysteamine 95-105 epidermal growth factor like 1 Rattus norvegicus 29-32 3053882-8 1988 After cysteamine administration, the secretion of EGF from Brunner"s glands decreases and the glands become depleted of mucus. Cysteamine 6-16 epidermal growth factor like 1 Rattus norvegicus 50-53 3053882-9 1988 Intraduodenal instillation of EGF can partly prevent formation of cysteamine-induced duodenal ulcers. Cysteamine 66-76 epidermal growth factor like 1 Rattus norvegicus 30-33 3683075-1 1987 We have examined the effects of the thiol agent cysteamine on physiological prolactin secretion in the female rat. Cysteamine 48-58 prolactin Rattus norvegicus 76-85 3683075-2 1987 Administration of cysteamine completely abolishes suckling-induced prolactin secretion in a dose-dependent manner. Cysteamine 18-28 prolactin Rattus norvegicus 67-76 3683075-4 1987 Further, we have found that the prolactin-depleting ability of cysteamine is not altered by a prior suckling stimulus. Cysteamine 63-73 prolactin Rattus norvegicus 32-41 3683075-5 1987 These results indicate that cysteamine administration inhibits physiologically-induced prolactin secretion with similar potency and efficacy as previously reported for cysteamine effects on basal and pharmacologically-induced prolactin secretion. Cysteamine 28-38 prolactin Rattus norvegicus 87-96 3683075-5 1987 These results indicate that cysteamine administration inhibits physiologically-induced prolactin secretion with similar potency and efficacy as previously reported for cysteamine effects on basal and pharmacologically-induced prolactin secretion. Cysteamine 28-38 prolactin Rattus norvegicus 226-235 3683075-5 1987 These results indicate that cysteamine administration inhibits physiologically-induced prolactin secretion with similar potency and efficacy as previously reported for cysteamine effects on basal and pharmacologically-induced prolactin secretion. Cysteamine 168-178 prolactin Rattus norvegicus 226-235 2883547-0 1987 Regulation of somatostatin-14 and gastrin I binding sites in rat gastrointestinal mucosa by ulcerogenic dose of cysteamine. Cysteamine 112-122 gastrin Rattus norvegicus 34-41 3041147-4 1987 Cysteamine (1 mM) increased gastrin (IRG) secretion to a maximum ranging between 100% and 192% above basal. Cysteamine 0-10 gastrin Rattus norvegicus 28-35 2888645-0 1987 Cysteamine-induced decrease of somatostatin in rat brain synaptosomes in vitro. Cysteamine 0-10 somatostatin Rattus norvegicus 31-43 2888645-1 1987 The mechanism of somatostatin depletion induced by cysteamine [2-mercaptoethylamine (CySH)] was studied in isolated nerve endings (synaptosomes) from rat brain in vitro. Cysteamine 51-61 somatostatin Rattus norvegicus 17-29 2888645-1 1987 The mechanism of somatostatin depletion induced by cysteamine [2-mercaptoethylamine (CySH)] was studied in isolated nerve endings (synaptosomes) from rat brain in vitro. Cysteamine 63-83 somatostatin Rattus norvegicus 17-29 3041147-0 1987 The effect of muscarinic and beta-adrenergic blockade on cysteamine-induced gastrin secretion by the isolated perfused rat stomach. Cysteamine 57-67 gastrin Rattus norvegicus 76-83 3041147-1 1987 Cysteamine-induced duodenal ulceration in rats is accompanied by increased circulating gastrin. Cysteamine 0-10 gastrin Rattus norvegicus 87-94 3041147-2 1987 Although cysteamine appears to exert a direct action on the gastrin cell some groups have provided evidence for an involvement of the autonomic nervous system. Cysteamine 9-19 gastrin Rattus norvegicus 60-67 3041147-3 1987 The current experiments were performed to determine whether beta-adrenergic or cholinergic (muscarinic) pathways are involved in the acute effect of cysteamine on gastrin secretion in the isolated perfused rat stomach. Cysteamine 149-159 gastrin Rattus norvegicus 163-170 3552035-1 1987 Thioredoxin upon reduction with mercaptoethylamine was subjected to covalent modification by the monofunctional organoarsenical reagents H2NPhAsO and HO(CH2)4AsCl2. Cysteamine 32-50 thioredoxin Homo sapiens 0-11 2884925-2 1987 Cysteamine, an agent which selectively and reversibly depletes brain somatostatin stores, had a biphasic action. Cysteamine 0-10 somatostatin Rattus norvegicus 69-81 2884925-7 1987 Intraventricular administration of somatostatin to animals with behavioral seizures attenuated by cysteamine treatment restored the responses to precysteamine levels. Cysteamine 98-108 somatostatin Rattus norvegicus 35-47 3828820-0 1987 Cysteamine-induced depletion of central somatostatin-like immunoactivity: effects on behavior, learning, memory and brain neurochemistry. Cysteamine 0-10 somatostatin Homo sapiens 40-52 3828820-5 1987 Cysteamine in doses of 50 mg/kg and above depleted cortical somatostatin-like immunoactivity by approximately 50%. Cysteamine 0-10 somatostatin Homo sapiens 60-72 3828820-7 1987 In addition to the depletion of somatostatin-like immunoactivity, high doses of cysteamine (150 mg/kg and above) produced changes in cortical levels of norepinephrine and dopamine, reminiscent of dopamine-beta-hydroxylase inhibition. Cysteamine 80-90 somatostatin Homo sapiens 32-44 3828820-7 1987 In addition to the depletion of somatostatin-like immunoactivity, high doses of cysteamine (150 mg/kg and above) produced changes in cortical levels of norepinephrine and dopamine, reminiscent of dopamine-beta-hydroxylase inhibition. Cysteamine 80-90 dopamine beta-hydroxylase Homo sapiens 196-221 3828820-9 1987 It is possible that the amnesia produced by cysteamine may have been due to the release of somatostatin into CSF from tissue stores, rather than somatostatin depletion per se. Cysteamine 44-54 somatostatin Homo sapiens 91-103 3567920-4 1987 The synergistic effect of cysteamine with the conditioning heat treatment at 44 degrees C was blocked by catalase (50 micrograms/ml). Cysteamine 26-36 catalase Cricetulus griseus 105-113 3567920-6 1987 The induction of thermotolerance by cysteamine at 37 degrees C was completely blocked by the addition of catalase (50 micrograms/ml), present during the initial period of drug treatment. Cysteamine 36-46 catalase Cricetulus griseus 105-113 2884649-0 1987 Immunohistochemical analysis of the effects of cysteamine on somatostatin-like immunoreactivity in the rat central nervous system. Cysteamine 47-57 somatostatin Rattus norvegicus 61-73 3815102-1 1987 Local injection of cysteamine into rat striatum results in a rapid but reversible reduction in somatostatin-like immunoreactivity (SLI). Cysteamine 19-29 somatostatin Rattus norvegicus 95-107 3815102-6 1987 These results suggest that the mechanism by which somatostatin is depleted by cysteamine is one of specific biochemical modification, probably affecting the somatostatin disulfide bond, rather than one affecting neuronal metabolism. Cysteamine 78-88 somatostatin Rattus norvegicus 50-62 3815102-6 1987 These results suggest that the mechanism by which somatostatin is depleted by cysteamine is one of specific biochemical modification, probably affecting the somatostatin disulfide bond, rather than one affecting neuronal metabolism. Cysteamine 78-88 somatostatin Rattus norvegicus 157-169 3721502-8 1986 In the VLDL fractions of all affected family members only the presence of apo E3-Leiden could be detected after cysteamine treatment and isoelectric focusing followed by conventional protein staining. Cysteamine 112-122 apolipoprotein E Homo sapiens 74-80 2874017-4 1986 Cysteamine also caused large reductions in label incorporation into SRIF-14, SRIF-28, and OXT 1 and 4 h after drug injection. Cysteamine 0-10 oxytocin/neurophysin I prepropeptide Rattus norvegicus 90-93 2874017-8 1986 The results suggest that cysteamine inhibits the syntheses of SRIF-14, SRIF-28, and OXT and stimulates that of AVP. Cysteamine 25-35 oxytocin/neurophysin I prepropeptide Rattus norvegicus 84-87 3744935-4 1986 However, a number of agents potentiated the cytotoxicity of HN2 to LCFU, the most active being disulfiram and AET followed by cysteamine, DMSO, WR-638, and WR-3689. Cysteamine 126-136 MT-RNR2 like 2 (pseudogene) Homo sapiens 60-63 3827485-0 1986 [Effect of secretin and vasoactive intestinal polypeptide on mucosal defensive factors in cysteamine-induced duodenal ulcer]. Cysteamine 90-100 secretin Homo sapiens 11-19 2874568-1 1986 The effects of prior treatment with cysteamine, a drug which appears to deplete selectively the neuropeptide somatostatin, on apomorphine-induced stereotypy and amphetamine-induced locomotor activity and conditioned place preferences were investigated. Cysteamine 36-46 somatostatin Homo sapiens 109-121 2874568-2 1986 Twelve hours following systemic cysteamine injections apomorphine-induced stereotypy was attenuated and striatal somatostatin levels were reduced by half. Cysteamine 32-42 somatostatin Homo sapiens 113-125 2874527-0 1986 Huntington"s disease: effect of cysteamine, a somatostatin-depleting agent. Cysteamine 32-42 somatostatin Homo sapiens 46-58 2874527-2 1986 A controlled therapeutic trial of the somatostatin-depleting agent, cysteamine, was therefore conducted in five patients, including one with the rigid-akinetic form. Cysteamine 68-78 somatostatin Homo sapiens 38-50 3721502-9 1986 However, isoelectric focusing of cysteamine-treated sera followed by immunoblotting, using anti-apo E antiserum as first antiserum, demonstrates the presence of low amounts of normal apo E3 in addition to apo E3-Leiden in serum of the affected family members. Cysteamine 33-43 apolipoprotein E Homo sapiens 205-211 2874568-4 1986 Direct injections of cysteamine into the nucleus accumbens also decreased the locomotor response to amphetamine, and produced a local reduction in somatostatin levels in the accumbens. Cysteamine 21-31 somatostatin Homo sapiens 147-159 2874568-7 1986 Furthermore, it is evident from these results that cysteamine is an important tool with which to study the central actions of somatostatin. Cysteamine 51-61 somatostatin Homo sapiens 126-138 3721502-9 1986 However, isoelectric focusing of cysteamine-treated sera followed by immunoblotting, using anti-apo E antiserum as first antiserum, demonstrates the presence of low amounts of normal apo E3 in addition to apo E3-Leiden in serum of the affected family members. Cysteamine 33-43 apolipoprotein E Homo sapiens 183-189 3698895-3 1986 Tissue PRL was depleted-transformed by the use of three different conditions: 1) 30 min of suckling after 8 h of nonsuckling; 2) in vitro incubation of APs for 2 h; or 3) in vivo cysteamine (CSH) treatment. Cysteamine 179-189 prolactin Rattus norvegicus 7-10 3723843-0 1986 [The effect of secretin on the cysteamine induced inhibition of alkaline secretion by the duodenal mucosa]. Cysteamine 31-41 secretin Homo sapiens 15-23 3485062-1 1986 The effect of oral administration of synthetic human epidermal growth factor/urogastrone (EGF/URO) on healing of chronic duodenal ulcers induced by cysteamine in rats was investigated and compared with that of cimetidine, a H2-receptor antagonist. Cysteamine 148-158 epidermal growth factor Homo sapiens 53-97 2423200-0 1986 Cysteamine effects on somatostatin, catecholamines, pineal NAT and melatonin in rats. Cysteamine 0-10 N-acetyltransferase 1 Rattus norvegicus 59-62 2423200-5 1986 Pineal N-acetyltransferase (NAT) activity was significantly higher (p less than 0.05) after cysteamine than after saline, but no statistically significant effect was observed on pineal melatonin content. Cysteamine 92-102 N-acetyltransferase 1 Rattus norvegicus 28-31 2423200-7 1986 It is suggested that cysteamine may act at an intracellular level, inhibiting NAT degradation, an effect demonstrated in vitro and thought to be related to a thiol:disulfide exchange mechanism. Cysteamine 21-31 N-acetyltransferase 1 Rattus norvegicus 78-81 3708389-5 1986 Chronic cysteamine (CYS) treatment decreased body weight gain, acutely decreased cataleptic behavior to HAL, decreased serum rPRL levels, and prevented the increase in serum rPRL levels due to HAL administration. Cysteamine 8-18 prolactin Rattus norvegicus 125-129 3708389-5 1986 Chronic cysteamine (CYS) treatment decreased body weight gain, acutely decreased cataleptic behavior to HAL, decreased serum rPRL levels, and prevented the increase in serum rPRL levels due to HAL administration. Cysteamine 8-18 prolactin Rattus norvegicus 174-178 3708389-5 1986 Chronic cysteamine (CYS) treatment decreased body weight gain, acutely decreased cataleptic behavior to HAL, decreased serum rPRL levels, and prevented the increase in serum rPRL levels due to HAL administration. Cysteamine 20-23 prolactin Rattus norvegicus 125-129 3708389-5 1986 Chronic cysteamine (CYS) treatment decreased body weight gain, acutely decreased cataleptic behavior to HAL, decreased serum rPRL levels, and prevented the increase in serum rPRL levels due to HAL administration. Cysteamine 20-23 prolactin Rattus norvegicus 174-178 3708389-7 1986 Since CYS decreased rPRL levels, these results lend further support to the hypothesis that rPRL (and prolactin in general) is a pituitary hormone with modulatory action on the increase in striatal DA receptor density. Cysteamine 6-9 prolactin Rattus norvegicus 20-24 3708389-7 1986 Since CYS decreased rPRL levels, these results lend further support to the hypothesis that rPRL (and prolactin in general) is a pituitary hormone with modulatory action on the increase in striatal DA receptor density. Cysteamine 6-9 prolactin Rattus norvegicus 91-95 2868720-0 1986 Somatostatin, insulin and glucagon secretion by the perfused pancreas from the cysteamine-treated rat. Cysteamine 79-89 somatostatin Rattus norvegicus 0-12 3524849-8 1986 Cysteamine treatment reduced the staining for somatostatin and for thioredoxin reductase in the D cells without any obvious effect on the other pancreatic cells. Cysteamine 0-10 peroxiredoxin 2 Mus musculus 67-88 3081777-0 1986 Cysteamine, zinc, and thiols modify detectability of rat pituitary prolactin: a comparison with effects on bovine prolactin suggests differences in hormone storage. Cysteamine 0-10 prolactin Rattus norvegicus 67-76 3081777-5 1986 Cysteamine and zinc inhibited tissue PRL immunoassayability in male rat pituitary homogenates and also in partially purified secretory granules as they had inhibited bovine (b) PRL; however, zinc inhibited the rodent hormone less potently than the bovine. Cysteamine 0-10 prolactin Rattus norvegicus 37-40 3081777-5 1986 Cysteamine and zinc inhibited tissue PRL immunoassayability in male rat pituitary homogenates and also in partially purified secretory granules as they had inhibited bovine (b) PRL; however, zinc inhibited the rodent hormone less potently than the bovine. Cysteamine 0-10 prolactin Bos taurus 177-180 3079953-0 1986 Cysteamine decreases prolactin responsiveness to thyrotropin-releasing hormone in normal men. Cysteamine 0-10 prolactin Homo sapiens 21-30 3079953-0 1986 Cysteamine decreases prolactin responsiveness to thyrotropin-releasing hormone in normal men. Cysteamine 0-10 thyrotropin releasing hormone Homo sapiens 49-78 3079953-1 1986 Cysteamine depletes pituitary and plasma prolactin in rats. Cysteamine 0-10 prolactin Rattus norvegicus 41-50 3079953-3 1986 The effect of cysteamine on prolactin secretion is reported in normal men. Cysteamine 14-24 prolactin Homo sapiens 28-37 3079953-8 1986 Peak serum prolactin levels following TRH, prolactin levels at the 10-min time point, and total area from 0 to 30 min under the prolactin secretory curve were significantly decreased by cysteamine administration. Cysteamine 186-196 prolactin Homo sapiens 11-20 3079953-8 1986 Peak serum prolactin levels following TRH, prolactin levels at the 10-min time point, and total area from 0 to 30 min under the prolactin secretory curve were significantly decreased by cysteamine administration. Cysteamine 186-196 thyrotropin releasing hormone Homo sapiens 38-41 3079953-8 1986 Peak serum prolactin levels following TRH, prolactin levels at the 10-min time point, and total area from 0 to 30 min under the prolactin secretory curve were significantly decreased by cysteamine administration. Cysteamine 186-196 prolactin Homo sapiens 43-52 3079953-8 1986 Peak serum prolactin levels following TRH, prolactin levels at the 10-min time point, and total area from 0 to 30 min under the prolactin secretory curve were significantly decreased by cysteamine administration. Cysteamine 186-196 prolactin Homo sapiens 43-52 3079953-11 1986 It was concluded that cysteamine reduced TRH-stimulated prolactin secretion. Cysteamine 22-32 thyrotropin releasing hormone Homo sapiens 41-44 3079953-11 1986 It was concluded that cysteamine reduced TRH-stimulated prolactin secretion. Cysteamine 22-32 prolactin Homo sapiens 56-65 4080089-0 1985 Cysteamine effects on monoamines, dopamine-beta-hydroxylase and the hypothalamic-pituitary axis. Cysteamine 0-10 dopamine beta-hydroxylase Rattus norvegicus 34-59 3709997-6 1986 The mouse can be protected against the cysteamine-induced duodenal ulcer by either the dopamine agonist lergotrile or histamine H2 receptor antagonist cimetidine. Cysteamine 39-49 histamine receptor H2 Mus musculus 118-139 3028901-0 1986 Modulation of somatostatin binding sites in cytosol of rabbit gastric fundic mucosa by cysteamine administration. Cysteamine 87-97 somatostatin Oryctolagus cuniculus 14-26 3028901-1 1986 Cysteamine, when given in vivo to rabbits, depleted immunoreactive somatostatin in rabbit gastric fundic mucosa. Cysteamine 0-10 somatostatin Oryctolagus cuniculus 67-79 3484471-0 1986 Radioprotective effect of cysteamine in glutathione synthetase-deficient cells. Cysteamine 26-36 glutathione synthetase Homo sapiens 40-62 2882057-1 1986 The purpose of our investigation was to study the effect of two somatostatin analogs (SMS 201-995 and 008) on duodenal ulcer disease induced by cysteamine in rats. Cysteamine 144-154 spermine synthase Rattus norvegicus 86-89 2882057-6 1986 Our results showed a dose-dependent effect of SMS 201-995 on the mortality, incidence, and intensity of cysteamine-induced duodenal lesions in rats. Cysteamine 104-114 spermine synthase Rattus norvegicus 46-49 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 0-10 dopamine beta-hydroxylase Rattus norvegicus 257-282 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 0-10 dopamine beta-hydroxylase Rattus norvegicus 284-287 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 12-35 dopamine beta-hydroxylase Rattus norvegicus 257-282 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 12-35 dopamine beta-hydroxylase Rattus norvegicus 284-287 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 37-40 dopamine beta-hydroxylase Rattus norvegicus 257-282 4080089-1 1985 Cysteamine (beta-mercaptoethylamine, MEA) is a naturally occurring sulfhydryl compound that depletes pituitary PRL, causes a reduction in brain and gut somatostatin (SRIF), and suppresses norepinephrine (NE) and epinephrine (EPI) synthesis by inhibition of dopamine-beta-hydroxylase (DBH). Cysteamine 37-40 dopamine beta-hydroxylase Rattus norvegicus 284-287 4053057-5 1985 Cysteamine inhibited the spontaneous degradation of N-OH-Trp-P-2 and enhanced the covalent binding of [3H]N-OH-Trp-P-2 to DNA. Cysteamine 0-10 polycystin 2, transient receptor potential cation channel Mus musculus 57-64 2864986-8 1985 Treatment with cysteamine, which caused a somatostatin depletion in the brain, was required to observe labeling in the hypothalamus. Cysteamine 15-25 somatostatin Rattus norvegicus 42-54 4053057-5 1985 Cysteamine inhibited the spontaneous degradation of N-OH-Trp-P-2 and enhanced the covalent binding of [3H]N-OH-Trp-P-2 to DNA. Cysteamine 0-10 polycystin 2, transient receptor potential cation channel Mus musculus 111-118 4053057-6 1985 This finding offered an explanation for the previously observed enhancement of Trp-P-2 mutagenicity by cysteamine. Cysteamine 103-113 polycystin 2, transient receptor potential cation channel Mus musculus 79-86 4053057-7 1985 In contrast cysteamine inhibited the N-OH-Trp-P-2-mediated inactivation of B. subtilis DNA as well as the strand cleavage in phi X174RFI DNA. Cysteamine 12-22 polycystin 2, transient receptor potential cation channel Mus musculus 42-49 2865862-0 1985 Rapid depletion of somatostatin in isolated mouse pancreatic islets after treatment with cysteamine. Cysteamine 89-99 somatostatin Mus musculus 19-31 2993777-2 1985 This hypothesis was tested in the rat following the acute administration of the DBH inhibitors diethyldithiocarbamate (DDC) and cysteamine (CSH). Cysteamine 128-138 dopamine beta-hydroxylase Rattus norvegicus 80-83 2860016-0 1985 Cysteamine-induced depletion of somatostatin and prolactin. Cysteamine 0-10 prolactin Rattus norvegicus 49-58 4004271-1 1985 L-Leucinthiol, a synthetic derivative of mercaptoethylamine with a hydrophobic side chain, was recently reported to be a potent inhibitor of microsomal aminopeptidase. Cysteamine 41-59 carboxypeptidase Q Homo sapiens 152-166 3996317-0 1985 Cysteamine causes reduction of prolactin monomers followed by aggregation in the rat pituitary gland. Cysteamine 0-10 prolactin Rattus norvegicus 31-40 3996317-1 1985 Storage forms of PRL were studied in control and cysteamine-treated cultures of estradiol-induced tumors in Fischer 344 rats and in secretory granules isolated from these tumors to further investigate the mechanism of action of cysteamine on PRL. Cysteamine 228-238 prolactin Rattus norvegicus 242-245 3996317-5 1985 Immunoreactivity of PRL in cell lysates or isolated granules is not affected by incubation with reducing agents beta-mercaptoethanol or glutathione at concentrations up to 5 mM, but cysteamine decreases PRL immunoreactivity in isolated granules at concentrations of 3 mM and higher. Cysteamine 182-192 prolactin Rattus norvegicus 20-23 3996317-5 1985 Immunoreactivity of PRL in cell lysates or isolated granules is not affected by incubation with reducing agents beta-mercaptoethanol or glutathione at concentrations up to 5 mM, but cysteamine decreases PRL immunoreactivity in isolated granules at concentrations of 3 mM and higher. Cysteamine 182-192 prolactin Rattus norvegicus 203-206 3996317-6 1985 Electrophoresis of isolated granules after incubation with 25 mM cysteamine for 1 h demonstrates that cysteamine converts PRL to the reduced form. Cysteamine 65-75 prolactin Rattus norvegicus 122-125 3996317-6 1985 Electrophoresis of isolated granules after incubation with 25 mM cysteamine for 1 h demonstrates that cysteamine converts PRL to the reduced form. Cysteamine 102-112 prolactin Rattus norvegicus 122-125 2994676-11 1985 This study could bring further information about the interactions between cysteamine and polyelectrolytic structures (ADN for example) and about the radioprotective properties of this drug. Cysteamine 74-84 complement factor D Homo sapiens 118-121 3996317-10 1985 These data indicate that: PRL exists predominantly in monomeric form in the rat pituitary gland, and cysteamine reduces PRL, and formation of disulfide-linked aggregates of PRL occurs subsequently under some conditions. Cysteamine 101-111 prolactin Rattus norvegicus 120-123 2860016-1 1985 Cysteamine (2-aminoethanethiol [CSH], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive somatostatin (irSS) in the central nervous system and gut as well as biological and immunological prolactin (PRL) activity in both the anterior pituitary and blood of the rat. Cysteamine 0-10 prolactin Rattus norvegicus 210-219 3996317-10 1985 These data indicate that: PRL exists predominantly in monomeric form in the rat pituitary gland, and cysteamine reduces PRL, and formation of disulfide-linked aggregates of PRL occurs subsequently under some conditions. Cysteamine 101-111 prolactin Rattus norvegicus 120-123 2860016-1 1985 Cysteamine (2-aminoethanethiol [CSH], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive somatostatin (irSS) in the central nervous system and gut as well as biological and immunological prolactin (PRL) activity in both the anterior pituitary and blood of the rat. Cysteamine 0-10 prolactin Rattus norvegicus 221-224 2860016-1 1985 Cysteamine (2-aminoethanethiol [CSH], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive somatostatin (irSS) in the central nervous system and gut as well as biological and immunological prolactin (PRL) activity in both the anterior pituitary and blood of the rat. Cysteamine 12-30 prolactin Rattus norvegicus 210-219 2860016-1 1985 Cysteamine (2-aminoethanethiol [CSH], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive somatostatin (irSS) in the central nervous system and gut as well as biological and immunological prolactin (PRL) activity in both the anterior pituitary and blood of the rat. Cysteamine 12-30 prolactin Rattus norvegicus 221-224 2863933-2 1985 Cysteamine-induced depletion of brain somatostatin-related peptides or central administration of a somatostatin receptor antagonist alters adrenomedullary epinephrine secretion and thermoregulation in a predictable manner. Cysteamine 0-10 somatostatin Homo sapiens 38-50 2858802-0 1985 Effect of dopamine, bombesin and cysteamine hydrochloride on plasma growth hormone response to synthetic growth hormone-releasing factor in rats. Cysteamine 33-57 gonadotropin releasing hormone receptor Rattus norvegicus 68-82 2858802-0 1985 Effect of dopamine, bombesin and cysteamine hydrochloride on plasma growth hormone response to synthetic growth hormone-releasing factor in rats. Cysteamine 33-57 growth hormone releasing hormone Rattus norvegicus 105-136 3919054-0 1985 Blunted prolactin response to thyrotropin-releasing hormone stimulation in cystinotic children receiving cysteamine. Cysteamine 105-115 thyrotropin releasing hormone Homo sapiens 30-59 3919054-1 1985 We investigated whether long term cysteamine therapy in cystinotic children altered their basal and stimulated serum PRL levels. Cysteamine 34-44 prolactin Homo sapiens 117-120 3976729-3 1985 The plasma of a type III hyperlipoproteinemic patient, when made at least 50 microM with respect to cysteamine in vitro, demonstrated a charge shift of the apolipoprotein E isoelectric focusing pattern from the E2 to the normal E3 and E4 positions. Cysteamine 100-110 apolipoprotein E Homo sapiens 156-172 3976729-4 1985 Two children treated for cystinosis with cysteamine each exhibited some charge alteration of their apoE3 to a form migrating in the apoE4 position. Cysteamine 41-51 apolipoprotein E Homo sapiens 99-104 3976729-4 1985 Two children treated for cystinosis with cysteamine each exhibited some charge alteration of their apoE3 to a form migrating in the apoE4 position. Cysteamine 41-51 apolipoprotein E Homo sapiens 132-137 3919054-2 1985 Five subjects who had normal plasma PRL responses to TRH stimulation before cysteamine treatment each had a lower basal PRL level and a blunted PRL response during long term (19-59 months) cysteamine therapy. Cysteamine 76-86 prolactin Homo sapiens 120-123 3919054-2 1985 Five subjects who had normal plasma PRL responses to TRH stimulation before cysteamine treatment each had a lower basal PRL level and a blunted PRL response during long term (19-59 months) cysteamine therapy. Cysteamine 76-86 prolactin Homo sapiens 120-123 3919054-7 1985 These findings suggest that cysteamine alters PRL secretion in humans. Cysteamine 28-38 prolactin Homo sapiens 46-49 3919971-3 1985 Incubating cells with 0.5 or 1.0 mmol/l cysteamine, a substance used in the clinical treatment of cystinosis because it depletes cells of excess cystine, greatly decreased beta-galactosidase activity in both cystinotic and normal cells. Cysteamine 40-50 galactosidase beta 1 Homo sapiens 172-190 3919971-5 1985 Thus, cysteamine, although effective in depleting cystinotic cells of excess cystine, may have the undesired side-effect of severely decreasing lysosomal beta-galactosidase. Cysteamine 6-16 galactosidase beta 1 Homo sapiens 154-172 2863933-2 1985 Cysteamine-induced depletion of brain somatostatin-related peptides or central administration of a somatostatin receptor antagonist alters adrenomedullary epinephrine secretion and thermoregulation in a predictable manner. Cysteamine 0-10 somatostatin Homo sapiens 99-111 2863933-3 1985 The actions of cysteamine and the somatostatin receptor antagonist are reversed by administration of somatostatins into the central nervous system, supporting the hypothesis that endogenous brain somatostatin-related peptides are involved in the regulation of adrenomedullary epinephrine secretion and thermoregulation. Cysteamine 15-25 somatostatin Homo sapiens 101-113 6241933-2 1984 The destruction of ATPase activity of myofibrils and myosin by lactoperoxidase and chloramine-T iodination could be prevented by the attachment of cysteamine to the sulphydryl groups prior to the iodination reaction and subsequent regeneration with thioglycolate or dithiothreitol. Cysteamine 147-157 myosin heavy chain 14 Homo sapiens 53-59 3917569-2 1985 Pretreatment with cysteamine (30 mg/100 g body wt, sc), a depletor of hypothalamic somatostatin, increased the plasma GH response to FK33-824 (10 micrograms/100 g body wt, iv). Cysteamine 18-28 gonadotropin releasing hormone receptor Rattus norvegicus 118-120 3917569-3 1985 Antiserum specific for rat GH-releasing factor (GRF) (0.5 ml/rat, iv) blunted GH release induced by FK33-824 (10 micrograms/100 g body wt, iv) in rats with or without cysteamine pretreatment. Cysteamine 167-177 growth hormone releasing hormone Rattus norvegicus 27-46 3917569-3 1985 Antiserum specific for rat GH-releasing factor (GRF) (0.5 ml/rat, iv) blunted GH release induced by FK33-824 (10 micrograms/100 g body wt, iv) in rats with or without cysteamine pretreatment. Cysteamine 167-177 growth hormone releasing hormone Rattus norvegicus 48-51 3917569-3 1985 Antiserum specific for rat GH-releasing factor (GRF) (0.5 ml/rat, iv) blunted GH release induced by FK33-824 (10 micrograms/100 g body wt, iv) in rats with or without cysteamine pretreatment. Cysteamine 167-177 gonadotropin releasing hormone receptor Rattus norvegicus 27-29 6498088-2 1984 We aimed to establish a time relationship between changes in gastric mucosal histamine, histamine formation capacity (HFC) and plasma gastrin after cysteamine administration. Cysteamine 148-158 gastrin Rattus norvegicus 134-141 6498088-4 1984 Plasma gastrin rose after cysteamine and was higher than in controls 2h after injection. Cysteamine 26-36 gastrin Rattus norvegicus 7-14 6498088-6 1984 A direct correlation was found between plasma gastrin and HFC in both controls and after cysteamine. Cysteamine 89-99 gastrin Rattus norvegicus 46-53 6498088-7 1984 It is suggested that the changes indicate that cysteamine releases gastrin, which increases HFC and thus histamine. Cysteamine 47-57 gastrin Rattus norvegicus 67-74 6093188-12 1984 Superoxide dismutase (SOD) was found to stimulate the oxygen uptake in the case of MEA and cysteine, but had little or no effect with DTT and glutathione. Cysteamine 83-86 superoxide dismutase 1 Homo sapiens 0-20 6151665-1 1984 In the present study the effects of somatostatin and cysteamine (a selective decreaser of the somatostatin level in the body) were compared in different behavioral tests on rats. Cysteamine 53-63 somatostatin Rattus norvegicus 94-106 6093188-12 1984 Superoxide dismutase (SOD) was found to stimulate the oxygen uptake in the case of MEA and cysteine, but had little or no effect with DTT and glutathione. Cysteamine 83-86 superoxide dismutase 1 Homo sapiens 22-25 6479100-1 1984 Cysteamine [2-aminoethanethiol (CySH)] reduces measurable PRL concentrations in vivo and in vitro. Cysteamine 0-10 prolactin Bos taurus 58-61 6479100-1 1984 Cysteamine [2-aminoethanethiol (CySH)] reduces measurable PRL concentrations in vivo and in vitro. Cysteamine 12-30 prolactin Bos taurus 58-61 6479100-4 1984 We undertook the present study to identify the sites involved in the loss of measurable PRL (depletion) induced by cysteamine. Cysteamine 115-125 prolactin Bos taurus 88-91 6479101-0 1984 Cysteamine depletes prolactin (PRL) but does not alter the structure of PRL-containing granules in the anterior pituitary. Cysteamine 0-10 prolactin Rattus norvegicus 20-29 6479101-0 1984 Cysteamine depletes prolactin (PRL) but does not alter the structure of PRL-containing granules in the anterior pituitary. Cysteamine 0-10 prolactin Rattus norvegicus 31-34 6479101-1 1984 Cysteamine causes a profound depletion of PRL in the anterior pituitary and in the systemic circulation, as measured by RIA and bioassay. Cysteamine 0-10 prolactin Rattus norvegicus 42-45 6479101-3 1984 In contrast to the results obtained by RIA, PRL-like immunoreactivity as detected by immunocyto-chemistry is present and similar to that of control preparations after cysteamine administration. Cysteamine 167-177 prolactin Rattus norvegicus 44-47 6479101-4 1984 We suggest that cysteamine alters PRL structure in secretory granules, probably by interacting with the disulfide bonds of PRL, thereby altering bioactivity and immunoreactivity. Cysteamine 16-26 prolactin Rattus norvegicus 34-37 6479101-4 1984 We suggest that cysteamine alters PRL structure in secretory granules, probably by interacting with the disulfide bonds of PRL, thereby altering bioactivity and immunoreactivity. Cysteamine 16-26 prolactin Rattus norvegicus 123-126 6479101-5 1984 The presence of cysteamine-altered PRL in secretory granules does not seem to trigger degradation of granules by the lysosomal system. Cysteamine 16-26 prolactin Rattus norvegicus 35-38 6209149-1 1984 Immunohistochemical studies on rats showed cysteamine to deplete immunoreactive somatostatin, but not substance P, in the substantia gelatinosa of the spinal trigeminal nucleus and spinal cord. Cysteamine 43-53 somatostatin Rattus norvegicus 80-92 6744307-0 1984 Enhancement of cysteamine cytotoxicity by hyperthermia and its modification by catalase and superoxide dismutase in Chinese hamster ovary cells. Cysteamine 15-25 catalase Cricetulus griseus 79-87 6744307-5 1984 Cysteamine toxicity was not modified by the addition of superoxide dismutase (10 micrograms/ml) but was completely blocked by the addition of catalase (50 micrograms/ml) over the drug concentration range of 0.2 to 2.0 mM. Cysteamine 0-10 catalase Cricetulus griseus 142-150 6744307-6 1984 Cysteamine autoxidation as measured by O2 uptake at 0.4 mM proceeds through hydrogen peroxide (H2O2) production as evidenced by the regeneration of O2 upon the addition of catalase. Cysteamine 0-10 catalase Cricetulus griseus 172-180 6484310-2 1984 As based on polyacrylamide disc electrophoresis, inactivation of the testicular isozyme, LDH-X, was almost complete with penicillamine and its disulfide, somewhat less with GSH and GSSG, least with thioglycolate and its disulfide and inconsistent with cysteine, 2-mercaptoethanol and 2-mercaptoethylamine. Cysteamine 284-304 lactate dehydrogenase C Homo sapiens 89-94 6745176-1 1984 Cysteamine [2-mercaptoethylamine (CySH)] displays a variety of neuroendocrine effects, the most potent being the depletion of immunoassayable tissue PRL. Cysteamine 0-10 prolactin Bos taurus 149-152 6745176-1 1984 Cysteamine [2-mercaptoethylamine (CySH)] displays a variety of neuroendocrine effects, the most potent being the depletion of immunoassayable tissue PRL. Cysteamine 12-32 prolactin Bos taurus 149-152 6146511-4 1984 However, in the rats treated with cysteamine or anti-SRIF rabbit serum, the inhibitory effect of GRP on hpGRF-induced GH release was significantly attenuated. Cysteamine 34-44 gastrin releasing peptide Rattus norvegicus 97-100 6726088-3 1984 Chemical modification of apoE2 ( Arg158 ----Cys) with sulfhydryl reagents (2-bromoethyl)-trimethylammonium bromide or cysteamine, which convert cysteine to arginyl or lysyl analogues, respectively, abolishes the difference in apparent molecular weight and results in the co-electrophoresis of E2( Arg158 ----Cys) with other apoE forms. Cysteamine 118-128 apolipoprotein E Homo sapiens 25-30 6609862-2 1984 Removal of the submandibular glands and thereby submandibular epidermal growth factor (EGF) caused rats to develop gastric lesions (ulcerations and ulcers) after administration of the duodenal ulcerogen cysteamine. Cysteamine 203-213 epidermal growth factor like 1 Rattus norvegicus 62-85 6609862-2 1984 Removal of the submandibular glands and thereby submandibular epidermal growth factor (EGF) caused rats to develop gastric lesions (ulcerations and ulcers) after administration of the duodenal ulcerogen cysteamine. Cysteamine 203-213 epidermal growth factor like 1 Rattus norvegicus 87-90 6609862-3 1984 The median output of EGF in gastric juice was reduced from 45.6 pmol/12 h (total range 17.5-65.0) in unoperated controls to less than 0.06 pmol/12 h (total range less than 0.06-1.82) in rats given cysteamine after extirpation of the submandibular glands. Cysteamine 197-207 epidermal growth factor like 1 Rattus norvegicus 21-24 6233628-6 1984 The increased killing of preincubated cells by cysteamine was shown to be similar to that of H2O2, and the dramatic reduction of cysteamine toxicity by catalase indicated H2O2 was the major reaction associated with this effect. Cysteamine 129-139 catalase Cricetulus griseus 152-160 6714167-1 1984 Cysteamine (CSH), a sulfhydryl compound, reduces both serum and anterior pituitary (AP) PRL measured by RIA. Cysteamine 0-10 prolactin Rattus norvegicus 88-91 6327714-4 1984 Modification of apo-E2 with cysteamine, which converts the cysteine at position 158 to a positively charged lysine analogue, activates receptor binding approximately 13-fold. Cysteamine 28-38 apolipoprotein E Homo sapiens 16-22 6327714-7 1984 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Cysteamine 48-58 apolipoprotein E Homo sapiens 164-170 6327714-7 1984 When the Mr = 22,000 fragment was modified with cysteamine and combined with DMPC, receptor binding was further enhanced, attaining the level of activity of normal apo-E3 X DMPC, a 100-fold increase over apo-E2 X DMPC binding. Cysteamine 48-58 apolipoprotein E Homo sapiens 204-210 6327714-10 1984 The receptor binding of apo-E2-containing beta-very low density lipoproteins could also be activated by cysteamine treatment, with the same retention of enhanced binding activity occurring after the reversal of the modification. Cysteamine 104-114 apolipoprotein E Homo sapiens 24-30 6142843-0 1984 Effect of cysteamine on secretion of gastrin and somatostatin from the rat stomach. Cysteamine 10-20 gastrin Rattus norvegicus 37-44 6142843-0 1984 Effect of cysteamine on secretion of gastrin and somatostatin from the rat stomach. Cysteamine 10-20 somatostatin Rattus norvegicus 49-61 6142843-1 1984 Cysteamine (beta-mercaptoethylamine HCl) administration to rats induces a hypergastrinemia and a reduction in gastric tissue somatostatin content. Cysteamine 0-10 somatostatin Rattus norvegicus 125-137 6142843-3 1984 Cysteamine (1 mM) rapidly increased immunoreactive gastrin release to levels ranging between 41% and 125% above basal. Cysteamine 0-10 gastrin Rattus norvegicus 51-58 6142843-7 1984 Addition of 10 mM cysteamine during gastric inhibitory polypeptide perfusion caused a 300% increase in immunoreactive gastrin. Cysteamine 18-28 gastrin Rattus norvegicus 118-125 6142843-9 1984 The results demonstrate that cysteamine can stimulate immunoreactive gastrin secretion without any change in somatostatinlike immunoreactivity release. Cysteamine 29-39 gastrin Rattus norvegicus 69-76 6142843-10 1984 When somatostatinlike immunoreactivity secretion is stimulated by an agent such as gastric inhibitory polypeptide, the cysteamine-induced release of immunoreactive gastrin is attenuated, suggesting the presence of a functional linkage between somatostatin and gastrin under these conditions. Cysteamine 119-129 gastrin Rattus norvegicus 164-171 6142843-10 1984 When somatostatinlike immunoreactivity secretion is stimulated by an agent such as gastric inhibitory polypeptide, the cysteamine-induced release of immunoreactive gastrin is attenuated, suggesting the presence of a functional linkage between somatostatin and gastrin under these conditions. Cysteamine 119-129 somatostatin Rattus norvegicus 5-17 6142843-10 1984 When somatostatinlike immunoreactivity secretion is stimulated by an agent such as gastric inhibitory polypeptide, the cysteamine-induced release of immunoreactive gastrin is attenuated, suggesting the presence of a functional linkage between somatostatin and gastrin under these conditions. Cysteamine 119-129 gastrin Rattus norvegicus 260-267 6726088-3 1984 Chemical modification of apoE2 ( Arg158 ----Cys) with sulfhydryl reagents (2-bromoethyl)-trimethylammonium bromide or cysteamine, which convert cysteine to arginyl or lysyl analogues, respectively, abolishes the difference in apparent molecular weight and results in the co-electrophoresis of E2( Arg158 ----Cys) with other apoE forms. Cysteamine 118-128 apolipoprotein E Homo sapiens 25-29 6641630-1 1983 Previous studies have shown that cysteamine [2-aminoethanethiol (CSH)], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive PRL from the anterior pituitary (AP) through a mechanism which, in vitro, does not appear to involve the dopamine (DA) receptor. Cysteamine 33-43 prolactin Rattus norvegicus 146-149 6142098-1 1984 Cysteamine administration to rats results in a marked depletion of hypothalamic somatostatin-14 (SS14) and a decrease of the potassium-evoked in vitro release of SS14 without a significant change in the content or release of somatostatin-28(1-12)-like immunoreactivity (SS28(1-12)-L1). Cysteamine 0-10 somatostatin Rattus norvegicus 97-101 6142098-1 1984 Cysteamine administration to rats results in a marked depletion of hypothalamic somatostatin-14 (SS14) and a decrease of the potassium-evoked in vitro release of SS14 without a significant change in the content or release of somatostatin-28(1-12)-like immunoreactivity (SS28(1-12)-L1). Cysteamine 0-10 somatostatin Rattus norvegicus 162-166 6142098-1 1984 Cysteamine administration to rats results in a marked depletion of hypothalamic somatostatin-14 (SS14) and a decrease of the potassium-evoked in vitro release of SS14 without a significant change in the content or release of somatostatin-28(1-12)-like immunoreactivity (SS28(1-12)-L1). Cysteamine 0-10 somatostatin Rattus norvegicus 270-274 6142098-2 1984 Furthermore, cysteamine enhances the spontaneous release and markedly potentiates the potassium-evoked release of SS14 in the in vitro slice preparation. Cysteamine 13-23 somatostatin Rattus norvegicus 114-118 6142098-4 1984 Immunohistochemical visualization of hypothalamic neuronal cell bodies and fibers following cysteamine administration shows a disappearance of the SS14 immunoreactive fibers and cell bodies with no apparent change in the SS28(1-12) immunoreactive fibers and cell bodies. Cysteamine 92-102 somatostatin Rattus norvegicus 147-151 6319389-5 1984 Furthermore, cysteamine treatment of the apo-E2 in beta-VLDL enhanced binding of the beta-VLDL to both apo-E and apo-B,E receptors. Cysteamine 13-23 apolipoprotein E Homo sapiens 41-47 6319389-5 1984 Furthermore, cysteamine treatment of the apo-E2 in beta-VLDL enhanced binding of the beta-VLDL to both apo-E and apo-B,E receptors. Cysteamine 13-23 apolipoprotein E Homo sapiens 41-46 6319389-5 1984 Furthermore, cysteamine treatment of the apo-E2 in beta-VLDL enhanced binding of the beta-VLDL to both apo-E and apo-B,E receptors. Cysteamine 13-23 apolipoprotein B Canis lupus familiaris 113-118 6140981-2 1983 We report here that acute intraperitoneal administration of cysteamine, an agent reported to deplete brain and gastrointestinal immunoreactive somatostatin content in kindled rats, led to profound suppression of kindled seizures. Cysteamine 60-70 somatostatin Rattus norvegicus 143-155 6605273-0 1983 Epidermal growth factor inhibits cysteamine-induced duodenal ulcers. Cysteamine 33-43 epidermal growth factor like 1 Rattus norvegicus 0-23 6605273-1 1983 The effect of the duodenal ulcerogen cysteamine on secretion of epidermal growth factor from Brunner"s gland pouches was studied in the rat. Cysteamine 37-47 epidermal growth factor like 1 Rattus norvegicus 64-87 6605273-2 1983 Total output of immunoreactive epidermal growth factor was reduced to approximately 55%, compared with controls, 5 h after administration of cysteamine (300 mg/kg, s.c.). Cysteamine 141-151 epidermal growth factor like 1 Rattus norvegicus 31-54 6605273-3 1983 Furthermore, measurements on tissue extracts of the pouches revealed that 5 h after cysteamine treatment, Brunner"s glands were depleted of epidermal growth factor. Cysteamine 84-94 epidermal growth factor like 1 Rattus norvegicus 140-163 6605273-6 1983 Luminal epidermal growth factor significantly inhibited the formation of cysteamine-induced duodenal ulcer, compared with controls receiving saline. Cysteamine 73-83 epidermal growth factor like 1 Rattus norvegicus 8-31 6605273-8 1983 These results demonstrate that epidermal growth factor has a cytoprotective effect on the duodenal mucosa, and it is suggested that inhibition of synthesis and secretion of endogenous epidermal growth factor may be a pathogenetic factor in cysteamine-induced duodenal ulcer. Cysteamine 240-250 epidermal growth factor like 1 Rattus norvegicus 31-54 6605273-8 1983 These results demonstrate that epidermal growth factor has a cytoprotective effect on the duodenal mucosa, and it is suggested that inhibition of synthesis and secretion of endogenous epidermal growth factor may be a pathogenetic factor in cysteamine-induced duodenal ulcer. Cysteamine 240-250 epidermal growth factor like 1 Rattus norvegicus 184-207 6641630-1 1983 Previous studies have shown that cysteamine [2-aminoethanethiol (CSH)], given in vivo or in vitro, rapidly but reversibly depletes immunoreactive PRL from the anterior pituitary (AP) through a mechanism which, in vitro, does not appear to involve the dopamine (DA) receptor. Cysteamine 45-63 prolactin Rattus norvegicus 146-149 6137403-1 1983 Previous studies showed a rapid decrease of somatostatin concentration in the gut and an increase in serum gastrin levels after a single dose of the duodenal ulcerogen cysteamine. Cysteamine 168-178 gastrin Rattus norvegicus 107-114 6137403-0 1983 The effect of the duodenal ulcerogen cysteamine on somatostatin and gastrin cells in the rat. Cysteamine 37-47 somatostatin Rattus norvegicus 51-63 6137403-0 1983 The effect of the duodenal ulcerogen cysteamine on somatostatin and gastrin cells in the rat. Cysteamine 37-47 gastrin Rattus norvegicus 68-75 6137403-6 1983 The alterations observed in the G cells after cysteamine administration are consistent with release of gastrin from mature granules and increased synthesis of the hormone. Cysteamine 46-56 gastrin Rattus norvegicus 103-110 6137403-7 1983 The lack of major morphologic changes in the D cells suggests that cysteamine affects somatostatin without causing cell necrosis or alteration in lysosome formation. Cysteamine 67-77 somatostatin Rattus norvegicus 86-98 6832077-0 1983 Cysteamine depletes prolactin in young and old hyperprolactinemic rats. Cysteamine 0-10 prolactin Rattus norvegicus 20-29 6631234-1 1983 Two-dimensional gel electrophoresis or isoelectric focusing before and after treatment with cysteamine are currently used to determine the six apolipoprotein E isomorphic phenotypes from isolated very low density lipoproteins. Cysteamine 92-102 apolipoprotein E Homo sapiens 143-159 6192467-4 1983 In vitro cysteamine significantly increased the basal release of SS14-LI and markedly potentiated the evoked release of SS14-LI from hypothalamic slices. Cysteamine 9-19 somatostatin Rattus norvegicus 65-69 6192467-4 1983 In vitro cysteamine significantly increased the basal release of SS14-LI and markedly potentiated the evoked release of SS14-LI from hypothalamic slices. Cysteamine 9-19 somatostatin Rattus norvegicus 120-124 6832077-1 1983 Studies were undertaken to evaluate the effects of cysteamine on serum and anterior pituitary concentrations of prolactin in hyperprolactinemic female rats. Cysteamine 51-61 prolactin Rattus norvegicus 112-121 6832077-3 1983 At 4 h after treatment with cysteamine (90 mg/kg body wt) serum and anterior pituitary prolactin concentrations were reduced in young animals by 98 and 85%, respectively. Cysteamine 28-38 prolactin Rattus norvegicus 87-96 6832077-4 1983 In old constant-estrous rats, cysteamine reduced serum prolactin by 92% and anterior pituitary prolactin by 82%. Cysteamine 30-40 prolactin Rattus norvegicus 55-64 6832077-6 1983 These studies indicate that cysteamine is an effective depletor of serum and pituitary prolactin in hyperprolactinemic rats. Cysteamine 28-38 prolactin Rattus norvegicus 87-96 6135242-0 1983 Somatostatin depletion of the gut and pancreas induced by cysteamine is not prevented by vagotomy or by dopamine agonists. Cysteamine 58-68 somatostatin Rattus norvegicus 0-12 6192467-5 1983 At 10 mM cysteamine, enhanced release of SS14-LI from hypothalamic slices was still observed despite a marked depletion of tissue content of SS14-LI. Cysteamine 9-19 somatostatin Rattus norvegicus 41-45 6300187-8 1983 In all cases, the binding activity of the apo-E2 was increased 10- to 20-fold by treating the apoproteins with cysteamine, a reagent that converts cysteine residues to positively charged lysine analogues. Cysteamine 111-121 apolipoprotein E Homo sapiens 42-48 6300187-9 1983 The cysteine content of each apo-E was determined by monitoring the change in the isoelectric focusing position of the cysteamine-treated apo-E2. Cysteamine 119-129 apolipoprotein E Homo sapiens 29-34 6300187-9 1983 The cysteine content of each apo-E was determined by monitoring the change in the isoelectric focusing position of the cysteamine-treated apo-E2. Cysteamine 119-129 apolipoprotein E Homo sapiens 138-144 6135242-1 1983 The role of endogenous somatostatin in the pathogenesis of duodenal was investigated in the present study by using the cysteamine animal model of the disease. Cysteamine 119-129 somatostatin Rattus norvegicus 23-35 6135242-2 1983 Our previous studies showed a rapid and multiorgan depletion of somatostatin immunoreactivity (SIR) in rats given a single dose of duodenal ulcerogen cysteamine. Cysteamine 150-160 somatostatin Rattus norvegicus 64-76 6135242-7 1983 Thus cysteamine depletes endogenous somatostatin in peripheral organs (e.g., stomach, duodenum, pancreas) by mechanisms independent of both vagus nerve and dopamine agonists. Cysteamine 5-15 somatostatin Rattus norvegicus 36-48 6184259-0 1983 Cysteamine and prostaglandin F2 beta stimulate rat gastric mucin release. Cysteamine 0-10 solute carrier family 13 member 2 Rattus norvegicus 59-64 6679320-3 1983 Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax. Cysteamine 245-255 OCA2 melanosomal transmembrane protein Gallus gallus 59-68 6679320-3 1983 Further studies on the glycine-14CO2 exchange catalyzed by p-protein and H-protein purified from chicken liver indicated that tiglyl CoA inhibited the activity of P-protein in an apparently competitive manner with respect to H-protein, and that cysteamine inhibited the activity of P-protein in two ways, by increasing the Km value for glycine and changing Vmax. Cysteamine 245-255 OCA2 melanosomal transmembrane protein Gallus gallus 163-172 6129131-0 1983 Cysteamine effects on growth hormone secretion in the male rat. Cysteamine 0-10 gonadotropin releasing hormone receptor Rattus norvegicus 22-36 6184259-2 1983 The purpose of this study was to measure the release of mucin glycoproteins from rat stomach after treatment with cysteamine and prostaglandin F2 beta, two structurally unrelated drugs that have been shown to protect the stomach against the noxious effects of alcohol and other damaging agents. Cysteamine 114-124 solute carrier family 13 member 2 Rattus norvegicus 56-61 6184259-4 1983 Cysteamine produced a dose-dependent increase in release of soluble and gel mucin. Cysteamine 0-10 solute carrier family 13 member 2 Rattus norvegicus 76-81 6184259-8 1983 Similarly, indomethacin inhibited mucin secretion by cysteamine but did not significantly influence cytoprotection. Cysteamine 53-63 solute carrier family 13 member 2 Rattus norvegicus 34-39 7089575-0 1982 Cysteamine: a potent and specific depletor of pituitary prolactin. Cysteamine 0-10 prolactin Homo sapiens 56-65 6186951-0 1982 The effect of cysteamine on immunoreactive somatostatin in the rabbit retina. Cysteamine 14-24 somatostatin Oryctolagus cuniculus 43-55 6186951-5 1982 Cysteamine injected locally into the retina is a relatively specific drug for depletion of somatostatin. Cysteamine 0-10 somatostatin Oryctolagus cuniculus 91-103 7089575-1 1982 Cysteamine rapidly reduces the concentration of prolactin in pituitary tissue in vivo and in vitro. Cysteamine 0-10 prolactin Homo sapiens 48-57 7115528-1 1982 A study was made of the effect of a synthetic enkephalin analog and cimetidinee on experimental duodenal ulcer in rats induced by cysteamine administration. Cysteamine 130-140 proenkephalin Rattus norvegicus 46-56 7178823-0 1982 The mechanism of gastrin release in cysteamine-induced duodenal ulcer. Cysteamine 36-46 gastrin Rattus norvegicus 17-24 7178823-3 1982 This study was performed to elucidate the mechanisms of gastrin release after an ulcerogenic dose of cysteamine. Cysteamine 101-111 gastrin Rattus norvegicus 56-63 7178823-4 1982 Cysteamine induced a rise in serum gastrin from 29 +/- 5 pg/ml to a maximum of 203 +/- 62 pg/ml after 3 h in unoperated rats, whereas no rise was seen in vagotomized or antrectomized rats. Cysteamine 0-10 gastrin Rattus norvegicus 35-42 7178823-5 1982 The beta-adrenergic blocking agent propranolol strongly inhibited cysteamine-induced gastrin release, whereas atropine dependent on an intact vagus and may be mediated by beta-adrenergic receptors. Cysteamine 66-76 gastrin Rattus norvegicus 85-92 6120164-0 1982 Thiazolidine-2-carboxylic acid, an adduct of cysteamine and glyoxylate, as a substrate for D-amino acid oxidase. Cysteamine 45-55 D-amino acid oxidase Homo sapiens 91-111 5031432-0 1972 [Properties of lysozyme and ribonuclease A, irradiated in the dry state, following treatment with beta-mercaptoethylamine]. Cysteamine 98-121 lysozyme Homo sapiens 15-23 6118261-0 1981 Somatostatin in rat tissues is depleted by cysteamine administration. Cysteamine 43-53 somatostatin Rattus norvegicus 0-12 6118261-2 1981 Because the ulcerogenic properties of cysteamine are markedly reduced by treatment with somatostatin, we considered the possibility that cysteamine-induced duodenal ulcer might be mediated by depletion of tissue somatostatin, and thereby of its paracrine influences on gastrin and gastric acid secretion. Cysteamine 137-147 somatostatin Rattus norvegicus 88-100 6118261-2 1981 Because the ulcerogenic properties of cysteamine are markedly reduced by treatment with somatostatin, we considered the possibility that cysteamine-induced duodenal ulcer might be mediated by depletion of tissue somatostatin, and thereby of its paracrine influences on gastrin and gastric acid secretion. Cysteamine 137-147 somatostatin Rattus norvegicus 212-224 6118261-2 1981 Because the ulcerogenic properties of cysteamine are markedly reduced by treatment with somatostatin, we considered the possibility that cysteamine-induced duodenal ulcer might be mediated by depletion of tissue somatostatin, and thereby of its paracrine influences on gastrin and gastric acid secretion. Cysteamine 137-147 gastrin Rattus norvegicus 269-276 6118261-5 1981 IR-somatostatin in hypothalamus and pancreas decreased gradually to a minimum at 7 h. Another duodenal ulcerogen, propionitrile (10 mg/100 g bw, s.c.) which is more toxic than cysteamine, and several stressful procedures including ether anesthesia, restraint and s.c. formalin did not lower stomach or duodenal IR-somatostatin. Cysteamine 176-186 somatostatin Rattus norvegicus 3-15 6118261-7 1981 These findings suggest that cysteamine is a relatively specific depletor of tissue somatostatin. Cysteamine 28-38 somatostatin Rattus norvegicus 83-95 37058-3 1979 The formation of duodenal ulcers induced by the administration of propionitrile or cysteamine was abolished by vagotomy, decreased by sympathectomy, histamine depletion, histamine H-2 receptor antagonists, hypophysectomy, thyroidectomy, or adrenalectomy. Cysteamine 83-93 histamine receptor H 2 Rattus norvegicus 170-192 1027239-1 1976 A glutathione reductase activity was unaltered in thymus and liver tissue and slightly increased in spleen of rats within 15-30 min after administration of a radioprotector mercaptoethylamine. Cysteamine 173-191 glutathione-disulfide reductase Rattus norvegicus 2-23 824715-3 1976 Both the "J-negative" proteins contained bound albumin and alpha-1 antitrypsin (alpha1AT),and reduction with mercaptoethylamine caused a release of albumin and alpha1AT concomitant with depolymerization of the higher polymers of IgA. Cysteamine 109-127 serpin family A member 1 Homo sapiens 160-168 1175606-6 1975 Cholesterol 7alpha-hydroxylase activity is enhanced in vitro by thiol-containing substances like mercaptoethanol, dithiothreitol, or cysteamine. Cysteamine 133-143 cytochrome P450 family 7 subfamily A member 1 Homo sapiens 0-30 1126937-4 1975 Polymers of IgA were reduced with mercaptoethylamine and subsequently alkylated with [14C]-iodoacetamide and the dimer and monomer isolated. Cysteamine 34-52 CD79a molecule Homo sapiens 12-15 6803092-2 1982 A single subcutaneous injection of cysteamine (300 mg/kg) reduces significantly (p less than or equal to 0.05 serum concentrations of LH, FSH and T. Cysteamine blocked LH secretion induced by castration and administration of naloxone and LHRH. Cysteamine 35-45 gonadotropin releasing hormone 1 Rattus norvegicus 238-242 6803092-2 1982 A single subcutaneous injection of cysteamine (300 mg/kg) reduces significantly (p less than or equal to 0.05 serum concentrations of LH, FSH and T. Cysteamine blocked LH secretion induced by castration and administration of naloxone and LHRH. Cysteamine 149-159 gonadotropin releasing hormone 1 Rattus norvegicus 238-242 6803092-4 1982 These results suggest that cysteamine acts to reduce pituitary responsiveness to LHRH, resulting in lower mean serum gonadotropin and testosterone concentrations. Cysteamine 27-37 gonadotropin releasing hormone 1 Rattus norvegicus 81-85 6803092-5 1982 It is possible, however, that cysteamine acts also at the hypothalamus to reduce LHRH secretion and/or at the testes to reduce testosterone release. Cysteamine 30-40 gonadotropin releasing hormone 1 Rattus norvegicus 81-85 7233083-1 1981 Cysteamine in a single subcutaneous administration induces release of gastrin, acid hypersecretion, and duodenal ulcer in rats. Cysteamine 0-10 gastrin Rattus norvegicus 70-77 6252011-5 1980 Cysteamine, when injected in vivo, kept up the glucose-6-phosphatase of whole liver. Cysteamine 0-10 glucose-6-phosphatase catalytic subunit 1 Rattus norvegicus 47-68 490537-1 1979 One-step treatment of daunomycinone with excess 2-aminoethanethiol and 2-aminoethanol in trifluoroacetic acid afforded at C-7 the thioether (77% yield) and ether (30% after recycling), respectively. Cysteamine 48-66 complement C7 Homo sapiens 122-125 309452-2 1978 The injection of ascrobate together with cysteamine (beta-mercaptoethylamin or MEA) was shown to cause a partial reversion of the radioprotective action of MEA in mice, and simultaneously of the suppressive action of MEA on RNA synthesis in bone marrow cells. Cysteamine 41-51 meander tail Mus musculus 53-82 309452-2 1978 The injection of ascrobate together with cysteamine (beta-mercaptoethylamin or MEA) was shown to cause a partial reversion of the radioprotective action of MEA in mice, and simultaneously of the suppressive action of MEA on RNA synthesis in bone marrow cells. Cysteamine 41-51 meander tail Mus musculus 156-159 913972-0 1977 Duodenal ulcerogens, cysteamine and propionitrile, stimulate serum gastrin levels in the rat. Cysteamine 21-31 gastrin Rattus norvegicus 67-74 913972-4 1977 Intragastric administration of cysteamine caused a 3- to 4-fold increase in fasting serum gastrin levels over the values of controls. Cysteamine 31-41 gastrin Rattus norvegicus 90-97 913972-6 1977 The food-stimulated rise in serum gastrin levels after either a chow meal or intragastric instillation of a peptone solution was markedly enhanced by cysteamine pretreatment. Cysteamine 150-160 gastrin Rattus norvegicus 34-41 913972-7 1977 Three hours after feeding the serum gastrin levels of cysteamine pretreated rats were 6 times higher than those of fed controls. Cysteamine 54-64 gastrin Rattus norvegicus 36-43 913972-8 1977 The high serum gastrin levels of cysteamine-pretreated fed rats could not be explained solely by the additive effects of cysteamine and food, indicating that a potentiating interaction may exist between the two stimulants of gastrin release. Cysteamine 33-43 gastrin Rattus norvegicus 15-22 913972-8 1977 The high serum gastrin levels of cysteamine-pretreated fed rats could not be explained solely by the additive effects of cysteamine and food, indicating that a potentiating interaction may exist between the two stimulants of gastrin release. Cysteamine 33-43 gastrin Rattus norvegicus 225-232 1126937-1 1975 Employing mercaptoethylamine as a reducing agent, it was demonstrated by analytical ultracentrifugation and polyacrylamide gel electrophoresis that polymeric immunoglobulin A (IgA) was reduced to a 10 S dimer and 7 S monomer, and that dimer IgA was more resistant to reductive cleavage than the higher polymers. Cysteamine 10-28 immunoglobulin heavy variable 4-38-2-like Homo sapiens 158-180 1126937-1 1975 Employing mercaptoethylamine as a reducing agent, it was demonstrated by analytical ultracentrifugation and polyacrylamide gel electrophoresis that polymeric immunoglobulin A (IgA) was reduced to a 10 S dimer and 7 S monomer, and that dimer IgA was more resistant to reductive cleavage than the higher polymers. Cysteamine 10-28 CD79a molecule Homo sapiens 176-179 4431456-0 1974 Interaction of dGMP radical with cysteamine and promethazine as possible model of DNA repair. Cysteamine 33-43 fliF Drosophila melanogaster 15-19 5983963-0 1966 [The activity of deoxyribonuclease I in the urine of irradiated rats under conditions of protection with cysteamine]. Cysteamine 105-115 deoxyribonuclease 1 Rattus norvegicus 17-36 33429019-5 2021 The decrease in analytical responses of cysteamine was monitored to evaluate the reactivity of three electrophilic activators of the Nrf2 pathway, which mediates the cellular stress response. Cysteamine 40-50 nuclear factor, erythroid derived 2, like 2 Mus musculus 133-137 13884364-0 1962 Temporary suppression of diamine oxidase (histaminase) activity by cysteamine. Cysteamine 67-77 amine oxidase copper containing 1 Homo sapiens 25-40 13884364-0 1962 Temporary suppression of diamine oxidase (histaminase) activity by cysteamine. Cysteamine 67-77 amine oxidase copper containing 1 Homo sapiens 42-53 13499717-0 1957 [Effect in vivo and in vitro of mercaptoethylamine or cysteamine on the formation and reduction of methemoglobin]. Cysteamine 32-50 hemoglobin subunit gamma 2 Homo sapiens 99-112 13499717-0 1957 [Effect in vivo and in vitro of mercaptoethylamine or cysteamine on the formation and reduction of methemoglobin]. Cysteamine 54-64 hemoglobin subunit gamma 2 Homo sapiens 99-112 34054147-2 2021 This article describes an electrochemical immunoassay platform developed to determine the severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) spike antibody by using gold-clusters capped with cysteamine, glutaraldehyde, the spike protein of the SARS-CoV-2 antigen and bovine serum albumin on a glassy carbon electrode. Cysteamine 201-211 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 151-156 33283949-4 2021 The current molecular docking study suggested that the selected new compounds such as ninhydrin, naphthoquinone, cysteamine and disulfide cysteamine could be suitable molecules as a G9a and GLP inhibitors. Cysteamine 113-123 euchromatic histone lysine methyltransferase 2 Homo sapiens 182-185 33283949-4 2021 The current molecular docking study suggested that the selected new compounds such as ninhydrin, naphthoquinone, cysteamine and disulfide cysteamine could be suitable molecules as a G9a and GLP inhibitors. Cysteamine 113-123 euchromatic histone lysine methyltransferase 1 Homo sapiens 190-193 33330868-4 2021 We found that thiol-based drugs, cysteamine and WR-1065 (the active metabolite of amifostine) in particular, decrease binding of SARS-CoV-2 spike protein to its receptor, decrease the entry efficiency of SARS-CoV-2 spike pseudotyped virus, and inhibit SARS-CoV-2 live virus infection. Cysteamine 33-43 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 140-145 32299163-1 2021 Objective: Vanin1 (VNN1) is a pantetheinase that can catalyze the hydrolysis of pantetheine to produce pantothenic acid and cysteamine. Cysteamine 124-134 VNN1 Gallus gallus 11-17 32299163-1 2021 Objective: Vanin1 (VNN1) is a pantetheinase that can catalyze the hydrolysis of pantetheine to produce pantothenic acid and cysteamine. Cysteamine 124-134 VNN1 Gallus gallus 19-23 33370348-9 2020 The most consistent findings were for cysteamine 450mg twice daily that had effects additional to that observed with placebo, with improved symptoms, CRISS additional 9.85 points (95% CI 0.02, 19.7) p = 0.05, reduced blood leukocyte count by 2.46x109 /l (95% CI 0.11, 4.80), p = 0.041 and reduced CRP by geometric mean 2.57 nmol/l (95% CI 0.15, 0.99), p = 0.049. Cysteamine 38-48 C-reactive protein Homo sapiens 297-300 33438698-3 2021 The immunosensor consists of rabbit anti-leptin antibody immobilized on a gold chip via cysteamine linker, using the EDC/NHS protocol. Cysteamine 88-98 leptin Homo sapiens 41-47 33139125-5 2021 Herein, we report the therapeutic effects of dietary therapy, cysteamine, and NAC in two siblings with ECHS1D, including their clinical, neuroradiological, and chemical aspects. Cysteamine 62-72 enoyl-CoA hydratase, short chain 1 Homo sapiens 103-109 33530504-0 2021 Activation of NRF2 and ATF4 Signaling by the Pro-Glutathione Molecule I-152, a Co-Drug of N-Acetyl-Cysteine and Cysteamine. Cysteamine 112-122 NFE2 like bZIP transcription factor 2 Homo sapiens 14-18 33530504-0 2021 Activation of NRF2 and ATF4 Signaling by the Pro-Glutathione Molecule I-152, a Co-Drug of N-Acetyl-Cysteine and Cysteamine. Cysteamine 112-122 activating transcription factor 4 Homo sapiens 23-27 33330868-4 2021 We found that thiol-based drugs, cysteamine and WR-1065 (the active metabolite of amifostine) in particular, decrease binding of SARS-CoV-2 spike protein to its receptor, decrease the entry efficiency of SARS-CoV-2 spike pseudotyped virus, and inhibit SARS-CoV-2 live virus infection. Cysteamine 33-43 surface glycoprotein Severe acute respiratory syndrome coronavirus 2 215-220 32864760-2 2020 Topical 5% cysteamine is an antioxidant and tyrosinase inhibitor that has been shown to be effective in the treatment of melasma. Cysteamine 11-21 tyrosinase Homo sapiens 44-54 33289461-1 2022 Vanin-1 (VNN1) is a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme which hydrolyzes pantetheine to pantothenic acid and cysteamine. Cysteamine 128-138 vanin 1 Homo sapiens 0-7 33289461-1 2022 Vanin-1 (VNN1) is a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme which hydrolyzes pantetheine to pantothenic acid and cysteamine. Cysteamine 128-138 vanin 1 Homo sapiens 9-13 33247224-7 2020 The histological features observed increased tubal metaplasia (TM) including negative expression of the estrogen receptor (ER) and progesterone receptor (PR) in the endometrium subsequent MEA treatment. Cysteamine 188-191 progesterone receptor Homo sapiens 154-156 33247224-9 2020 Further study is required to clarify the molecular mechanisms of tubal metaplasia and the expression loss of hormone receptor in the endometrium as a result of MEA treatment. Cysteamine 160-163 nuclear receptor subfamily 4 group A member 1 Homo sapiens 109-125 32303119-3 2020 In this work, we reported a novel sandwich-type electrochemical immunosensor based on gold nanoparticles functionalized cysteamine-glutaraldehyde (AuNPs-CysA-GA) and it successfully designed to detection of the CEA biomarker in a human plasma sample. Cysteamine 120-130 CEA cell adhesion molecule 3 Homo sapiens 211-214 33615064-8 2021 Male sex and delayed cysteamine initiation were independently associated with impaired grip strength. Cysteamine 21-31 glutamate receptor interacting protein 1 Homo sapiens 87-91 32798729-0 2020 Beneficial effects of cysteamine in Thy1-alpha-Syn mice and induced pluripotent stem cells with a SNCA gene triplication. Cysteamine 22-32 synuclein, alpha Mus musculus 41-50 32798729-8 2020 SNCA neurons treated with cysteamine exhibited significantly more intact/healthy neurites than cells treated with 6-OHDA alone. Cysteamine 26-36 synuclein alpha Homo sapiens 0-4 32798729-9 2020 Additionally, SNCA neurons treated with cysteamine in the absence of 6-OHDA showed a trend towards lower total alpha-Syn levels. Cysteamine 40-50 synuclein alpha Homo sapiens 14-18 32798729-9 2020 Additionally, SNCA neurons treated with cysteamine in the absence of 6-OHDA showed a trend towards lower total alpha-Syn levels. Cysteamine 40-50 synuclein alpha Homo sapiens 111-120 32798729-10 2020 Overall, our in vivo and in vitro findings suggest that cysteamine can act as a disease-modifying molecule by enhancing dopaminergic neuronal survival and reducing pathological forms of alpha-Syn. Cysteamine 56-66 synuclein alpha Homo sapiens 186-195 33095336-3 2020 The immunosensor was fabricated with core-shell nanoparticles and cysteamine employing covalent chemistry (amide bond formation) strategy for ensuring proper orientation of anti-hepcidin antibody on to the amine-functionalized nanomaterial decorated electrodes. Cysteamine 66-76 hepcidin antimicrobial peptide Homo sapiens 178-186 32497402-10 2020 We also found that a diagnosis of DHL rather than of MYC-DLBCL was significantly associated with CD10% > 60, Ki-67% > 50, and SS (B/T) <1.5. Cysteamine 34-37 membrane metalloendopeptidase Homo sapiens 97-101 32432367-1 2020 The design of biomimetic model complexes for the cysteine dioxygenase (CDO) and cysteamine dioxygenase (ADO) is reported, where the 3-His coordination of the iron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand (Tp) and protected cysteine and cysteamine represent substrate ligands. Cysteamine 80-90 2-aminoethanethiol dioxygenase Homo sapiens 104-107 32601061-2 2020 It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as regulator of G protein signaling 5 (RGS5). Cysteamine 31-41 regulator of G protein signaling 5 Homo sapiens 128-162 32843697-4 2020 The results suggested that AID is of important value in predicting DHL, stronger CSR of AID was observed in DHL patients, which exhibited AID overexpression and c-Myc gene translocation of DHL after CSR induction. Cysteamine 67-70 activation induced cytidine deaminase Homo sapiens 27-30 32843697-4 2020 The results suggested that AID is of important value in predicting DHL, stronger CSR of AID was observed in DHL patients, which exhibited AID overexpression and c-Myc gene translocation of DHL after CSR induction. Cysteamine 67-70 activation induced cytidine deaminase Homo sapiens 88-91 32843697-4 2020 The results suggested that AID is of important value in predicting DHL, stronger CSR of AID was observed in DHL patients, which exhibited AID overexpression and c-Myc gene translocation of DHL after CSR induction. Cysteamine 67-70 activation induced cytidine deaminase Homo sapiens 88-91 32843697-4 2020 The results suggested that AID is of important value in predicting DHL, stronger CSR of AID was observed in DHL patients, which exhibited AID overexpression and c-Myc gene translocation of DHL after CSR induction. Cysteamine 67-70 MYC proto-oncogene, bHLH transcription factor Homo sapiens 161-166 32843697-5 2020 It is concluded that AID directly induces CSR in DHL and may result in c-Myc gene translocation. Cysteamine 49-52 activation induced cytidine deaminase Homo sapiens 21-24 32843697-6 2020 Targeting AID may be a good treatment regimen for DHL. Cysteamine 50-53 activation induced cytidine deaminase Homo sapiens 10-13 32667185-4 2020 Whereas hSlo1 channels are activated by CO and even more strongly by Fe2+, Fe3+ and cysteamine possess only marginal activating potency. Cysteamine 84-94 potassium calcium-activated channel subfamily M alpha 1 Homo sapiens 8-13 32823962-5 2020 The miniature Au-E biosensor was designed and constructed through the immobilization of tyrosinase on an electroactive layer of cysteamine and carbon nanoparticles covering the gold electrode. Cysteamine 128-138 tyrosinase Homo sapiens 88-98 32601061-2 2020 It catalyzes oxidation of both cysteamine in sulfur metabolism and N-terminal cysteine-containing proteins or peptides, such as regulator of G protein signaling 5 (RGS5). Cysteamine 31-41 regulator of G protein signaling 5 Homo sapiens 164-168 31869680-0 2020 Blue luminescent graphene quantum dot conjugated cysteamine functionalized-gold nanoparticles (GQD-AuNPs) for sensing hazardous dye Erythrosine B. Cysteamine 49-59 estrogen receptor 2 Homo sapiens 132-145 32591583-6 2020 Gold electrodes were used to fabricate the immunosensors by immobilizing IKZF1 and IKZF3 specific antibodies using cysteamine and PDITC crosslinkers. Cysteamine 115-125 IKAROS family zinc finger 1 Homo sapiens 73-78 32591583-6 2020 Gold electrodes were used to fabricate the immunosensors by immobilizing IKZF1 and IKZF3 specific antibodies using cysteamine and PDITC crosslinkers. Cysteamine 115-125 IKAROS family zinc finger 3 Homo sapiens 83-88 32528489-3 2020 The findings that AtAMT1;3 transports methylammonium (MeA+, a chemical analog of NH4 +) with extremely low affinity (K m in the range of 2.9-6.1 mM) led to investigate the mechanisms underlying substrate binding. Cysteamine 54-58 ammonium transporter 1;3 Arabidopsis thaliana 18-26 32528489-4 2020 Homologous modeling and substrate docking analyses predicted that the deduced substrate binding motif of AtAMT1;3 facilitates the binding of NH4 + ions but loosely accommodates the binding of MeA+ to a more superficial location of the permeation pathway. Cysteamine 192-196 ammonium transporter 1;3 Arabidopsis thaliana 105-113 32623404-0 2020 Cysteamine Protects Neurons from Mutant Huntingtin Toxicity. Cysteamine 0-10 huntingtin Homo sapiens 40-50 31854983-4 2020 Cysteamine (Cys) and N-acetyl-l-cysteine (NAC) costabilized gold nanoclusters (Cys/NAC-AuNCs) were synthesized and adopted as an electron acceptor, and pyridoxal phosphate (PLP) was selected as an electron donor. Cysteamine 0-10 X-linked Kx blood group Homo sapiens 83-86 31854983-4 2020 Cysteamine (Cys) and N-acetyl-l-cysteine (NAC) costabilized gold nanoclusters (Cys/NAC-AuNCs) were synthesized and adopted as an electron acceptor, and pyridoxal phosphate (PLP) was selected as an electron donor. Cysteamine 0-3 X-linked Kx blood group Homo sapiens 42-45 31854983-4 2020 Cysteamine (Cys) and N-acetyl-l-cysteine (NAC) costabilized gold nanoclusters (Cys/NAC-AuNCs) were synthesized and adopted as an electron acceptor, and pyridoxal phosphate (PLP) was selected as an electron donor. Cysteamine 0-3 X-linked Kx blood group Homo sapiens 83-86 31854983-4 2020 Cysteamine (Cys) and N-acetyl-l-cysteine (NAC) costabilized gold nanoclusters (Cys/NAC-AuNCs) were synthesized and adopted as an electron acceptor, and pyridoxal phosphate (PLP) was selected as an electron donor. Cysteamine 12-15 X-linked Kx blood group Homo sapiens 83-86 31854983-5 2020 PLP can form a Schiff base (an aldimine) with the primary amino group of Cys/NAC-AuNC through its aldehyde group and thereby suppresses the fluorescence of Cys/NAC-AuNC. Cysteamine 73-76 X-linked Kx blood group Homo sapiens 77-80 31854983-5 2020 PLP can form a Schiff base (an aldimine) with the primary amino group of Cys/NAC-AuNC through its aldehyde group and thereby suppresses the fluorescence of Cys/NAC-AuNC. Cysteamine 73-76 X-linked Kx blood group Homo sapiens 160-163 31854983-5 2020 PLP can form a Schiff base (an aldimine) with the primary amino group of Cys/NAC-AuNC through its aldehyde group and thereby suppresses the fluorescence of Cys/NAC-AuNC. Cysteamine 156-159 X-linked Kx blood group Homo sapiens 77-80 31854983-5 2020 PLP can form a Schiff base (an aldimine) with the primary amino group of Cys/NAC-AuNC through its aldehyde group and thereby suppresses the fluorescence of Cys/NAC-AuNC. Cysteamine 156-159 X-linked Kx blood group Homo sapiens 160-163 31854983-7 2020 Since the pyridoxal (PL) produced by the acid phosphatase (ACP)-catalyzed cleavage of PLP has a weak interaction with Cys/NAC-AuNC, a novel turn-on fluorescent method for selective detection of ACP was successfully realized. Cysteamine 118-121 X-linked Kx blood group Homo sapiens 122-125 31820638-4 2020 On the other hand, a composite nanoparticle is fabricated as SERS probe for reading out the fingerprint spectral data, which consists of MOF materials (Zeolitic Imidazolate framework-8 (ZIF-8)) and Au@Ag nanocubes, as well as cysteamine (CA) that serves as the gas capturing agent. Cysteamine 226-236 seryl-tRNA synthetase 2, mitochondrial Homo sapiens 61-65 31514860-4 2020 The anti-MUC16 antibody was attached to a gold chip via a cysteamine linker. Cysteamine 58-68 mucin 16, cell surface associated Homo sapiens 9-14 31629988-5 2019 LDL receptor-deficient mice were fed a Western diet (19-22 per group) and some given cysteamine in their drinking water at a dose equivalent to that used in cystinosis patients. Cysteamine 85-95 low density lipoprotein receptor Mus musculus 0-12 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 21-31 brain derived neurotrophic factor Homo sapiens 246-279 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 21-31 brain derived neurotrophic factor Homo sapiens 281-285 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 21-31 NFE2 like bZIP transcription factor 2 Homo sapiens 291-334 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 21-31 NFE2 like bZIP transcription factor 2 Homo sapiens 336-340 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 127-137 brain derived neurotrophic factor Homo sapiens 246-279 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 127-137 brain derived neurotrophic factor Homo sapiens 281-285 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 127-137 NFE2 like bZIP transcription factor 2 Homo sapiens 291-334 31920936-7 2019 The small molecules, cysteamine, the decarboxylated derivative of the amino acid cysteine, and cystamine, the oxidized form of cysteamine, respectively, mitigate oxidative stress and inflammation and upregulate neuroprotective pathways involving brain-derived neurotrophic factor (BDNF) and Nuclear factor erythroid 2-related factor 2 (Nrf2) signaling. Cysteamine 127-137 NFE2 like bZIP transcription factor 2 Homo sapiens 336-340 31888107-6 2019 Cysteamine treatment restored the fission 1 ubiquitination, the mitochondrial size, number and lumen of cristae, but had no effect on cristae junction width, making CTNS-/- tubular cells more susceptible to apoptotic stimuli. Cysteamine 0-10 cystinosin, lysosomal cystine transporter Homo sapiens 165-169 31752970-11 2019 Notably, in a mouse model of DHL bearing primary tumor cells derived from lymphoma patients, combined treatment with XPO1 and BCL2 inhibitors blocks tumor progression, prevents brain metastasis, and extends host survival. Cysteamine 29-32 exportin 1 Homo sapiens 117-121 31752970-11 2019 Notably, in a mouse model of DHL bearing primary tumor cells derived from lymphoma patients, combined treatment with XPO1 and BCL2 inhibitors blocks tumor progression, prevents brain metastasis, and extends host survival. Cysteamine 29-32 BCL2 apoptosis regulator Homo sapiens 126-130 31404995-2 2019 Its major function is related to its pantetheinase activity; vanin 1 breaks down pantetheine in cysteamine and pantothenic acid, a precursor of coenzyme A. Cysteamine 96-106 vanin 1 Homo sapiens 61-68 31357466-3 2019 The gp120 antibody is then immobilized on this flexible electrode through cysteamine (Cys) modified on the surface of the Au/MoS2/Au nanolayer. Cysteamine 74-84 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 4-9 31357466-3 2019 The gp120 antibody is then immobilized on this flexible electrode through cysteamine (Cys) modified on the surface of the Au/MoS2/Au nanolayer. Cysteamine 86-89 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 4-9 31117849-10 2019 Targeted approaches, especially chimeric antigen receptor T-cell therapies and small-molecule inhibitors targeting myc or bcl-2, exhibit the potential of improving outcomes for patients with DHL. Cysteamine 191-194 MYC proto-oncogene, bHLH transcription factor Homo sapiens 115-118 31117849-10 2019 Targeted approaches, especially chimeric antigen receptor T-cell therapies and small-molecule inhibitors targeting myc or bcl-2, exhibit the potential of improving outcomes for patients with DHL. Cysteamine 191-194 BCL2 apoptosis regulator Homo sapiens 122-127 31391983-1 2019 The title binuclear CoIII complex, [Co2(C9H8BrNOS)2(C18H16Br2N2O2S2)] C3H7NO, with a Schiff base ligand formed in situ from cyste-amine (2-amino-ethane-thiol) and 5-bromo-salicyl-aldehyde crystallizes in the space group P21. Cysteamine 124-135 mitochondrially encoded cytochrome c oxidase III Homo sapiens 20-25 31656521-0 2019 Pre-IVM treatment with C-type natriuretic peptide in the presence of cysteamine enhances bovine oocytes antioxidant defense ability and developmental competence in vitro. Cysteamine 69-79 natriuretic peptide C Bos taurus 23-49 31656521-10 2019 Notably, the presence of cysteamine during pre-IVM culture with CNP significantly improved the rate of embryos developed to the blastocyst stage after in vitro maturation and fertilization, moreover, it increased the levels of GSH and reduced the levels of ROS in bovine oocytes. Cysteamine 25-35 natriuretic peptide C Bos taurus 64-67 30668749-5 2019 Micromolar range cysteamine bitartrate treatment in Caenorhabditis elegans gas-1(fc21) RC complex I (NDUFS2-/-) disease invertebrate worms significantly improved mitochondrial membrane potential and oxidative stress, with corresponding modest improvement in fecundity but not lifespan. Cysteamine 17-38 putative NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial Caenorhabditis elegans 75-80 30668749-6 2019 At 10 to 100 mum concentrations, cysteamine bitartrate improved multiple RC complex disease FBXL4 human fibroblast survival, and protected both complex I (rotenone) and complex IV (azide) Danio rerio vertebrate zebrafish disease models from brain death. Cysteamine 33-54 F-box and leucine rich repeat protein 4 Homo sapiens 92-97 31391983-1 2019 The title binuclear CoIII complex, [Co2(C9H8BrNOS)2(C18H16Br2N2O2S2)] C3H7NO, with a Schiff base ligand formed in situ from cyste-amine (2-amino-ethane-thiol) and 5-bromo-salicyl-aldehyde crystallizes in the space group P21. Cysteamine 137-157 mitochondrially encoded cytochrome c oxidase III Homo sapiens 20-25 30500419-7 2019 Next, we validated experimentally that autophagy/lipophagy-induction using an anti-oxidant, cysteamine, significantly (p < 0.05) reduces CS-extract (CSE)-mediated intracellular-ceramide-accumulation in p62 + aggresome-bodies. Cysteamine 92-102 nucleoporin 62 Homo sapiens 202-205 29931583-2 2019 This study examined triple targeting of c-MYC, BCL2 and the B-cell receptor (BCR) signaling pathway for DHL and DEL. Cysteamine 104-107 MYC proto-oncogene, bHLH transcription factor Homo sapiens 40-45 29931583-9 2019 These results provide a rationale for dual targeting of BRD4 and BCL2 using AZD5153 and AZD4320 as a therapeutic strategy against DHL and DEL. Cysteamine 130-133 bromodomain containing 4 Homo sapiens 56-60 29931583-9 2019 These results provide a rationale for dual targeting of BRD4 and BCL2 using AZD5153 and AZD4320 as a therapeutic strategy against DHL and DEL. Cysteamine 130-133 BCL2 apoptosis regulator Homo sapiens 65-69 30874346-7 2019 Here, we review our current knowledge about the role of MYC in germinal center B-cells and lymphomas, discuss MYC-induced dependencies that can sensitize cancer cells to select pharmacological inhibitors, and illustrate their therapeutic potential in aggressive lymphomas-and in particular in DHL, in combination with BCL2 inhibitors. Cysteamine 293-296 MYC proto-oncogene, bHLH transcription factor Homo sapiens 110-113 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 transglutaminase 2, C polypeptide Mus musculus 52-70 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 transglutaminase 2, C polypeptide Mus musculus 72-76 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 beclin 1, autophagy related Mus musculus 116-124 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 beclin 1, autophagy related Mus musculus 126-131 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 cystic fibrosis transmembrane conductance regulator Mus musculus 193-197 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 88-98 cystic fibrosis transmembrane conductance regulator Mus musculus 298-302 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 164-174 transglutaminase 2, C polypeptide Mus musculus 52-70 30874543-5 2019 Here we demonstrate that the proteostasis regulator/transglutaminase 2 (TGM2) inhibitor cysteamine restores reduced Beclin 1 (BECN1) protein levels in mice bearing cysteamine-rescuable F508del-CFTR mutant, either in homozygosis or in compound heterozygosis with a null allele, but not in knock-out CFTR mice. Cysteamine 164-174 transglutaminase 2, C polypeptide Mus musculus 72-76 30874543-6 2019 When cysteamine restored BECN1 expression, autophagy was increased and gliadin-induced inflammation was reduced. Cysteamine 5-15 beclin 1, autophagy related Mus musculus 25-30 30874543-7 2019 The beneficial effects of cysteamine on F508del-CFTR mice were lost when these mice were backcrossed into a Becn1 haploinsufficient/autophagy-deficient background. Cysteamine 26-36 cystic fibrosis transmembrane conductance regulator Mus musculus 48-52 30874543-7 2019 The beneficial effects of cysteamine on F508del-CFTR mice were lost when these mice were backcrossed into a Becn1 haploinsufficient/autophagy-deficient background. Cysteamine 26-36 beclin 1, autophagy related Mus musculus 108-113 30500419-8 2019 In addition to intracellular-accumulation, we found that CSE also induces membrane-ceramide-accumulation by ROS-dependent acid-sphingomyelinase (ASM) activation and plasma-membrane translocation, which was significantly controlled (p < 0.05) by cysteamine (an anti-oxidant) and amitriptyline (AMT, an inhibitor of ASM). Cysteamine 245-255 sphingomyelin phosphodiesterase 1 Homo sapiens 122-143 30500419-9 2019 Cysteamine-mediated and CSE-induced membrane-ceramide regulation was nullified by CFTR-inhibitor-172, demonstrating that CFTR controls redox impaired-autophagy dependent membrane-ceramide accumulation. Cysteamine 0-10 CF transmembrane conductance regulator Homo sapiens 82-86 30500419-9 2019 Cysteamine-mediated and CSE-induced membrane-ceramide regulation was nullified by CFTR-inhibitor-172, demonstrating that CFTR controls redox impaired-autophagy dependent membrane-ceramide accumulation. Cysteamine 0-10 CF transmembrane conductance regulator Homo sapiens 121-125 30500419-11 2019 Thus, CS-exposure alters the sphingolipid-rheostat leading to the increased membrane- and intracellular- ceramide-accumulation inducing COPD-emphysema pathogenesis that is alleviated by treatment with cysteamine, a potent anti-oxidant with CFTR/autophagy-augmenting properties. Cysteamine 201-211 CF transmembrane conductance regulator Homo sapiens 240-244 31068510-3 2019 However, several retrospective studies conducted recently have demonstrated a relatively favorable outcome with intensive chemotherapy, such as dose-adjusted EPOCH-R, than those receiving R-CHOP in patients with DHL. Cysteamine 212-215 DNA damage inducible transcript 3 Homo sapiens 190-194 30856117-0 2019 Cysteamine Protects Neurons from Mutant Huntingtin Toxicity. Cysteamine 0-10 huntingtin Homo sapiens 40-50 30856117-5 2019 OBJECTIVE: The objective of this study is to assess the capacity of cysteamine for neuroprotection against mutant Huntingtin in vitro using cellular models of HD, and to provide initial data regarding mechanism of action. Cysteamine 68-78 huntingtin Homo sapiens 114-124 30856117-7 2019 RESULTS: Cysteamine showed a strong neuroprotective effect (EC50 = 7.1 nM) against mutant Htt-(aa-1-586 82Q) toxicity, in a nuclear condensation cell toxicity assay. Cysteamine 9-19 huntingtin Homo sapiens 90-93 30856117-8 2019 Cysteamine also rescued mitochondrial changes induced by mutant Htt. Cysteamine 0-10 huntingtin Homo sapiens 64-67 30856117-10 2019 Taurine and Hypotaurine, which are metabolites of cysteamine can protect neurons against Htt toxicity, but the inhibition of the enzyme converting cysteamine to hypotaurine does not block either protective activity, suggesting independent protective pathways. Cysteamine 50-60 huntingtin Homo sapiens 89-92 30856117-11 2019 Cysteamine has been suggested to activate BDNF secretion; however, cysteamine protection was not blocked by BDNF pathway antagonists. Cysteamine 0-10 brain derived neurotrophic factor Homo sapiens 42-46 30260324-3 2018 Notably, PLK1 was expressed at high levels in DHL, correlated with MYC expression, and connoted poor outcome. Cysteamine 46-49 polo like kinase 1 Homo sapiens 9-13 30647729-7 2018 In addition, systemic administration of cysteamine, a TG2 inhibitor, attenuated social behavior deficits. Cysteamine 40-50 transglutaminase 2, C polypeptide Mus musculus 54-57 30260324-4 2018 Further, PLK1 signaling augmented MYC protein stability, and in turn, MYC directly induced PLK1 transcription, establishing a feed-forward MYC-PLK1 circuit in DHL. Cysteamine 159-162 polo like kinase 1 Homo sapiens 9-13 30395539-7 2018 PLK1 inhibition with volasertib, alone and in combination with the BCL-2 inhibitor venetoclax, was efficacious in multiple DHL models, including mice harboring DHL patient-derived xenografts. Cysteamine 123-126 polo like kinase 1 Mus musculus 0-4 30395539-7 2018 PLK1 inhibition with volasertib, alone and in combination with the BCL-2 inhibitor venetoclax, was efficacious in multiple DHL models, including mice harboring DHL patient-derived xenografts. Cysteamine 160-163 polo like kinase 1 Mus musculus 0-4 30260324-4 2018 Further, PLK1 signaling augmented MYC protein stability, and in turn, MYC directly induced PLK1 transcription, establishing a feed-forward MYC-PLK1 circuit in DHL. Cysteamine 159-162 MYC proto-oncogene, bHLH transcription factor Homo sapiens 34-37 30395539-8 2018 Together, these data support PLK1 as a promising prognostic marker and therapeutic target for DHL. Cysteamine 94-97 polo like kinase 1 Homo sapiens 29-33 30260324-4 2018 Further, PLK1 signaling augmented MYC protein stability, and in turn, MYC directly induced PLK1 transcription, establishing a feed-forward MYC-PLK1 circuit in DHL. Cysteamine 159-162 MYC proto-oncogene, bHLH transcription factor Homo sapiens 70-73 30260324-4 2018 Further, PLK1 signaling augmented MYC protein stability, and in turn, MYC directly induced PLK1 transcription, establishing a feed-forward MYC-PLK1 circuit in DHL. Cysteamine 159-162 polo like kinase 1 Homo sapiens 91-95 30260324-4 2018 Further, PLK1 signaling augmented MYC protein stability, and in turn, MYC directly induced PLK1 transcription, establishing a feed-forward MYC-PLK1 circuit in DHL. Cysteamine 159-162 MYC proto-oncogene, bHLH transcription factor Homo sapiens 139-147 28428344-7 2018 Of a number of natural VAP-1 substrates tested, cysteamine-which can be secreted by inflamed colonic epithelium and gut bacteria-was the most efficient (yielded the highest enzymatic rate) and efficacious in its ability to induce expression of functional mucosal addressin cell adhesion molecule-1 on hepatic endothelium. Cysteamine 48-58 amine oxidase copper containing 3 Homo sapiens 23-28 29365190-10 2018 In vitro low doses of cysteamine have beneficial antiresorptive effects on healthy human-derived OCs and may partly correct the CTNS-induced osteoclastic dysfunction in patients with NC. Cysteamine 22-32 cystinosin, lysosomal cystine transporter Homo sapiens 128-132 29935061-7 2018 Inhibition of transglutaminases (including TGM2) with cysteamine appreciably reduced transglutaminase activity in vivo, as assessed by Nepsilon -(gamma-l-glutamyl)-l-lysine abundance and TGM catalytic activity, and restored normal dihydroxylysinonorleucine and hydroxylysylpiridinoline collagen cross-link abundance under pathological conditions. Cysteamine 54-64 transglutaminase 2, C polypeptide Mus musculus 43-47 30004544-4 2018 To improve the detection sensitivity, the aptamer-antibody sandwich assay for the detection of tau-381 was developed by using a tau antibody (anti-tau) and an aptamer specific to tau-381 as the recognition element and cysteamine-stabilized gold nanoparticles (AuNPs) for signal amplification. Cysteamine 218-228 microtubule associated protein tau Homo sapiens 95-98 29936082-3 2018 In this work, the antibody (horseradish peroxidase (HRP)-Labeled anti CA 15-3) was immobilized onto a green and biocompatible nanocomposite containing gold nano-shrub (Au NSs) electrochemically assembled onto thiolated graphene quantum dots (GQDs/CysA (Cysteamine)). Cysteamine 253-263 mucin 1, cell surface associated Homo sapiens 70-77 29776542-0 2018 Aggregation of cysteamine-capped gold nanoparticles in presence of ATP as an analytical tool for rapid detection of creatine kinase (CK-MM). Cysteamine 15-25 creatine kinase, M-type Homo sapiens 133-138 29776542-2 2018 We have developed a method based on the aggregation of cysteamine (Cys) functionalized GNPs in presence of ATP for effective detection of creatine kinase (CK-MM). Cysteamine 55-65 creatine kinase, M-type Homo sapiens 155-160 29776542-2 2018 We have developed a method based on the aggregation of cysteamine (Cys) functionalized GNPs in presence of ATP for effective detection of creatine kinase (CK-MM). Cysteamine 67-70 creatine kinase, M-type Homo sapiens 155-160 29776542-3 2018 Positively charged Cys-GNPs (brick red color) aggregate in presence of negatively charged ATP (blue color) but the process is prevented when CK-MM is added to the solution. Cysteamine 19-22 creatine kinase, M-type Homo sapiens 141-146 29807255-17 2018 SOD2, HADC1 and HADC2 expression was higher for Cys 0.1 ICSI than for IVF embryos (p <= 0.05). Cysteamine 48-51 superoxide dismutase 2, mitochondrial Bos taurus 0-4 29353886-9 2018 Together, these findings highlight the relevance of BFL-1 in DH lymphoma-associated drug resistance and support the combined use of a BCL-2 antagonist and a BET inhibitor as a promising therapeutic strategy for patients with aggressive DHL. Cysteamine 236-239 BCL2 apoptosis regulator Homo sapiens 134-139 29415993-1 2018 Cystic Fibrosis (CF) due to the DeltaF508 mutation of cystic fibrosis transmembrane conductance regulator (CFTR) can be treated with a combination of cysteamine and Epigallocatechin gallate (EGCG). Cysteamine 150-160 CF transmembrane conductance regulator Homo sapiens 54-105 29415993-1 2018 Cystic Fibrosis (CF) due to the DeltaF508 mutation of cystic fibrosis transmembrane conductance regulator (CFTR) can be treated with a combination of cysteamine and Epigallocatechin gallate (EGCG). Cysteamine 150-160 CF transmembrane conductance regulator Homo sapiens 107-111 29415993-2 2018 Since ECGC is not a clinically approved drug, we attempted to identify other compounds that might favourably interact with cysteamine to induce autophagy and thus rescuing the function of DeltaF508 CFTR as a chloride channel in the plasma membrane. Cysteamine 123-133 CF transmembrane conductance regulator Homo sapiens 198-202 27413169-5 2018 Moreover, treatment with the autophagy-inducing antioxidant drug cysteamine significantly ( P < 0.001) decreased CSE/CS-induced aggresome bodies. Cysteamine 65-75 cystathionase (cystathionine gamma-lyase) Mus musculus 116-122 27413169-9 2018 Additionally, Beas2b cells and murine lungs exposed to CSE/CS showed cellular apoptosis and senescence, which were both controlled by cysteamine treatment. Cysteamine 134-144 cystathionase (cystathionine gamma-lyase) Mus musculus 55-61 29285589-1 2018 An efficient and highly selective pyrene-thiophene conjugate has been reported as a dual sensor for Hg2+ and cysteamine (an important drug for genetic disorder). Cysteamine 109-119 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 100-103 29285589-4 2018 Moreover, the [probe-Hg2+] adduct functions as an efficient sensor for cysteamine. Cysteamine 71-81 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 21-24