PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29153608-7 2017 There were increased levels of iNOS, TNF-alpha, HO1, Nrf2, Wfs-1, XBP-1 and spliced XBP-1 observed in response to hemin treatment and the signaling was found to be partly mediated by cofilin. Hemin 114-119 heme oxygenase 1 Homo sapiens 48-51 25998388-5 2015 Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards. Hemin 28-33 heme oxygenase 1 Homo sapiens 97-113 29089150-0 2017 Hemin Reduces HMGB1 Release by UVB in an AMPK/HO-1-dependent Pathway in Human Keratinocytes HaCaT Cells. Hemin 0-5 heme oxygenase 1 Homo sapiens 46-50 29089150-2 2017 We hypothesized that hemin might reduce HMGB1 release through the induction of HO-1 in UVB-induced HaCaTs. Hemin 21-26 heme oxygenase 1 Homo sapiens 79-83 29668174-5 2016 The E47 cells were treated with hemin chloride to induce HO-1 expression during INH-RMP treatment. Hemin 32-46 heme oxygenase 1 Homo sapiens 57-61 29668174-10 2016 Addition of Hemin chloride during treatment of INH-RMP induced HO-1 in E47 cells and reversed the drug induced liver injury. Hemin 12-26 heme oxygenase 1 Homo sapiens 63-67 26507166-11 2015 IL-13 significantly increased goblet cells, MUC5AC protein secretion (p b 0.01) and MUC5AC mRNA (p b 0.001), and these were decreased by hemin by way of HO-1. Hemin 137-142 heme oxygenase 1 Homo sapiens 153-157 28627599-6 2017 Hemin inhibited TGF-beta-induced EMT in the MCF-7 cells, whereas HMOX-1 siRNA attenuated the suppressive effect of hemin as determined by the expression and cellular distribution of selected EMT markers. Hemin 115-120 heme oxygenase 1 Homo sapiens 65-71 28627599-7 2017 In summary, our results revealed that hemin treatment increased HMOX-1 expression and inhibited TGF-beta-induced EMT in MCF-7 cells. Hemin 38-43 heme oxygenase 1 Homo sapiens 64-70 28298633-8 2017 Prior administration of hemin to renal IRI was associated with significant increase of the renal HO-1+ CD11b+ F4/80lo myeloid cells in comparison to control mice. Hemin 24-29 heme oxygenase 1 Homo sapiens 97-101 28270832-0 2017 Actin Family Proteins in the Human INO80 Chromatin Remodeling Complex Exhibit Functional Roles in the Induction of Heme Oxygenase-1 with Hemin. Hemin 137-142 heme oxygenase 1 Homo sapiens 115-131 27641735-10 2017 Restoration of HO-1 expression by hemin (20 mumol/L) abolished the inhibition of miR-1304 on cell growth and rescued miR-1304-induced apoptosis in A549 cells. Hemin 34-39 heme oxygenase 1 Homo sapiens 15-19 27283929-4 2016 AIMS: To compare effects of hemin and placebo infusions on HO1 activity and protein, GE, autonomic function, and gastrointestinal symptoms in diabetic gastroparesis. Hemin 28-33 heme oxygenase 1 Homo sapiens 59-62 27283929-12 2016 Further studies are necessary to ascertain whether more frequent hemin infusions or other drugs would have a more sustained effect on HO1 and improve GE. Hemin 65-70 heme oxygenase 1 Homo sapiens 134-137 27251503-3 2016 Although hemin treatment caused the increased expression of heme oxygenase (HO)-1, the inhibition of HO activity resulted in the aggravation of hemin-induced barrier dysfunction. Hemin 9-14 heme oxygenase 1 Homo sapiens 60-81 25998388-5 2015 Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards. Hemin 28-33 heme oxygenase 1 Homo sapiens 115-119 25998388-5 2015 Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards. Hemin 354-359 heme oxygenase 1 Homo sapiens 97-113 25998388-5 2015 Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards. Hemin 354-359 heme oxygenase 1 Homo sapiens 115-119 25633656-6 2015 The results of the present study demonstrated that the mRNA expression levels of HO-1 increased in a dose-dependent manner in the HepG2.2.15 cells, following exposure to 5-50 microM hemin. Hemin 182-187 heme oxygenase 1 Homo sapiens 81-85 25185584-8 2015 Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death. Hemin 48-53 heme oxygenase 1 Homo sapiens 13-29 25185584-8 2015 Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death. Hemin 48-53 heme oxygenase 1 Homo sapiens 31-36 25185584-8 2015 Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death. Hemin 48-53 heme oxygenase 1 Homo sapiens 37-41 23893806-5 2013 Peripheral blood mononuclear cells isolated from asthmatic patients and healthy controls were co-cultured with human bone marrow mesenchymal stem cells which were pretreated with Hemin (the revulsive of Heme Oxygenase-1), Protoporphyrin IX zinc (the inhibitor of Heme Oxygenase-1) and saline. Hemin 179-184 heme oxygenase 1 Homo sapiens 203-219 24830678-7 2014 We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5). Hemin 26-31 heme oxygenase 1 Homo sapiens 47-63 24830678-7 2014 We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5). Hemin 26-31 heme oxygenase 1 Homo sapiens 65-69 25136403-5 2014 HO-1 isoform has been extensively studied mainly by its ability to respond to cellular stresses such as hemin, nitric oxide donors, oxidative damage, hypoxia, hyperthermia, and heavy metals, between others. Hemin 104-109 heme oxygenase 1 Homo sapiens 0-4 25093998-3 2014 However, the only drugs (i.e., hemin and heme arginate) which pharmacologically upregulate HO-1 in humans are expensive and can only be administered intravenously. Hemin 31-36 heme oxygenase 1 Homo sapiens 91-95 24879794-6 2014 Exogenous hemin induced Treg polarization in purified T cell/monocyte cocultures from healthy volunteers through the monocyte anti-inflammatory heme-degrading enzyme heme oxygenase-1. Hemin 10-15 heme oxygenase 1 Homo sapiens 166-182 24792517-4 2014 Although hemin was able to induce HO-1 in a dose dependent manner, a specific HO-1 inhibitor, Sn-PPIX, was unable to interfere with the effect of hemin on Caco-2 cells. Hemin 9-14 heme oxygenase 1 Homo sapiens 34-38 24583029-3 2014 Hemin, a commercial preparation of heme, is used as an iron donor or heme oxygenase 1 (HO-1) inducer, and has been shown to provide antiviral activity in many studies. Hemin 0-5 heme oxygenase 1 Homo sapiens 69-85 24583029-3 2014 Hemin, a commercial preparation of heme, is used as an iron donor or heme oxygenase 1 (HO-1) inducer, and has been shown to provide antiviral activity in many studies. Hemin 0-5 heme oxygenase 1 Homo sapiens 87-91 23893806-5 2013 Peripheral blood mononuclear cells isolated from asthmatic patients and healthy controls were co-cultured with human bone marrow mesenchymal stem cells which were pretreated with Hemin (the revulsive of Heme Oxygenase-1), Protoporphyrin IX zinc (the inhibitor of Heme Oxygenase-1) and saline. Hemin 179-184 heme oxygenase 1 Homo sapiens 263-279 23893806-6 2013 The expression of Heme Oxygenase-1 in MSCs was enhanced by Hemin and inhibited by Protoporphyrin zinc in vitro. Hemin 59-64 heme oxygenase 1 Homo sapiens 18-34 20966033-1 2011 Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis. Hemin 37-42 heme oxygenase 1 Homo sapiens 0-16 23419834-10 2013 Treatment with hemin, a HO-1 inducer, and with [Ru(CO)3Cl2]2, a CO donor, decreased LPS-stimulated iNOS induction and NO production. Hemin 15-20 heme oxygenase 1 Homo sapiens 24-28 22120038-7 2012 Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, or supplementing heme, using hemin, caused a partial restoration of Pb(2+)-mediated inhibition of CYP1A1 induction by TCDD. Hemin 97-102 heme oxygenase 1 Homo sapiens 31-35 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 79-84 heme oxygenase 1 Homo sapiens 0-16 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 79-84 heme oxygenase 1 Homo sapiens 18-22 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 201-206 heme oxygenase 1 Homo sapiens 0-16 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 201-206 heme oxygenase 1 Homo sapiens 18-22 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 201-206 heme oxygenase 1 Homo sapiens 0-16 21681819-3 2011 Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact. Hemin 201-206 heme oxygenase 1 Homo sapiens 18-22 21549697-6 2011 In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression. Hemin 90-95 heme oxygenase 1 Homo sapiens 28-32 21549697-6 2011 In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression. Hemin 90-95 heme oxygenase 1 Homo sapiens 111-115 21549697-6 2011 In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression. Hemin 90-95 heme oxygenase 1 Homo sapiens 111-115 21781496-3 2011 Different concentrations of hemin were used to induce HO-1 expression of K562/A02-IM, HO-1 expression at different time was detected by RT-PCR and Western blot analysis. Hemin 28-33 heme oxygenase 1 Homo sapiens 54-58 21781496-3 2011 Different concentrations of hemin were used to induce HO-1 expression of K562/A02-IM, HO-1 expression at different time was detected by RT-PCR and Western blot analysis. Hemin 28-33 heme oxygenase 1 Homo sapiens 86-90 23068042-5 2013 Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1. Hemin 39-44 heme oxygenase 1 Homo sapiens 202-206 23068042-5 2013 Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1. Hemin 85-90 heme oxygenase 1 Homo sapiens 202-206 23092325-6 2013 Cells were incubated for 24h with Imatinib (1 muM) alone or in combination with Hemin (10muM), an inducer of HO-1. Hemin 80-85 heme oxygenase 1 Homo sapiens 109-113 20966033-1 2011 Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis. Hemin 37-42 heme oxygenase 1 Homo sapiens 18-22 20966033-1 2011 Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis. Hemin 46-56 heme oxygenase 1 Homo sapiens 0-16 20966033-1 2011 Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis. Hemin 46-56 heme oxygenase 1 Homo sapiens 18-22 20966033-2 2011 As a preclinical first step toward determining whether HO-1 upregulation is a viable target in acute pancreatitis (AP) patients, we tested the hypothesis that HO-1 expression in peripheral blood mononuclear cell (PBMC) subsets of hospitalized patients with mild AP is upregulated then normalizes upon recovery and that cells from AP patients have the potential to upregulate their HO-1 ex vivo if exposed to Panhematin. Hemin 408-418 heme oxygenase 1 Homo sapiens 159-163 20966033-2 2011 As a preclinical first step toward determining whether HO-1 upregulation is a viable target in acute pancreatitis (AP) patients, we tested the hypothesis that HO-1 expression in peripheral blood mononuclear cell (PBMC) subsets of hospitalized patients with mild AP is upregulated then normalizes upon recovery and that cells from AP patients have the potential to upregulate their HO-1 ex vivo if exposed to Panhematin. Hemin 408-418 heme oxygenase 1 Homo sapiens 159-163 20966033-6 2011 Panhematin induced HO-1 in ex vivo cultured AP PBMCs more readily than in HC or VC PBMCs. Hemin 0-10 heme oxygenase 1 Homo sapiens 19-23 20822529-10 2010 Pretreatment with hemin alone substantially induced both HO-1 mRNA and protein expression, and HO-1 mRNA expression was further enhanced when hemin was combined with IL-1beta treatment. Hemin 18-23 heme oxygenase 1 Homo sapiens 57-61 21297920-4 2011 Under these circumstances, the cells exhibited global protein arginine methylation: this event was also reproduced by the cell treatment with hemin, a heme oxygenase-1 inducer. Hemin 142-147 heme oxygenase 1 Homo sapiens 151-167 19956091-2 2010 In this randomized study of 10 healthy volunteers, hemin (3 mg/kg intravenously in 25% albumin) was shown to increase plasma HO-1 protein concentration four- to fivefold and HO-1 activity ~15-fold relative to baseline at 24 and 48 h (placebo -56.41 +/- 6.31 (baseline), 69.79 +/- 13.00 (24 h), 77.44 +/- 10.62 (48 h) vs. hemin -71.70 +/- 9.20 (baseline), 1,126.20 +/- 293.30 (24 h), 1,192.20 +/- 333.30 (48 h)) in four of five subjects as compared with albumin alone (P </= 0.03). Hemin 51-56 heme oxygenase 1 Homo sapiens 125-129 20378668-7 2010 The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin. Hemin 169-177 heme oxygenase 1 Homo sapiens 37-40 19956091-2 2010 In this randomized study of 10 healthy volunteers, hemin (3 mg/kg intravenously in 25% albumin) was shown to increase plasma HO-1 protein concentration four- to fivefold and HO-1 activity ~15-fold relative to baseline at 24 and 48 h (placebo -56.41 +/- 6.31 (baseline), 69.79 +/- 13.00 (24 h), 77.44 +/- 10.62 (48 h) vs. hemin -71.70 +/- 9.20 (baseline), 1,126.20 +/- 293.30 (24 h), 1,192.20 +/- 333.30 (48 h)) in four of five subjects as compared with albumin alone (P </= 0.03). Hemin 51-56 heme oxygenase 1 Homo sapiens 174-178 18381758-2 2008 Here we report that both HO-1 expression and activity can be highly increased in undifferentiated human mesenchymal stem cells (MSCs) treated with hemin, a known HO-1 inducer. Hemin 147-152 heme oxygenase 1 Homo sapiens 25-29 18824663-5 2008 The cardioprotection by hemin was accompanied by increased HO-1, HO activity, cGMP, superoxide dismutase, catalase, the total antioxidant capacity alongside the reduction of 8-isoprostane, AP-1, AP-2, nuclear factor-kappaB, and c-Jun-NH(2)-terminal kinase, whereas chromium mesoporphyrin abolished the hemin effects. Hemin 24-29 heme oxygenase 1 Homo sapiens 59-63 18701634-5 2008 HO-1 was induced in cultured mTALH cells by treatment with cobalt protoporphyrin (CoPP, 10 microM) or hemin (50 microM) or by transfection with a plasmid containing the human HO-1 isoform. Hemin 102-107 heme oxygenase 1 Homo sapiens 0-4 18412543-3 2008 Fluorescence correlation spectroscopy was used to investigate the mobility of hBVR in living cells and its function in the nuclear transport of haematin for induction of HO-1. Hemin 144-152 heme oxygenase 1 Homo sapiens 170-174 18412543-9 2008 Experiments with nuclear localization, export signal mutants and si-hBVR [siRNA (small interfering RNA) specific to hBVR] indicate that nuclear localization of hBVR is required for induction of HO-1 by haematin. Hemin 202-210 heme oxygenase 1 Homo sapiens 194-198 19903769-7 2009 Hemin treatment increased HO-1 at both protein and mRNA levels in all cell lines and decreased cell proliferation and invasion. Hemin 0-5 heme oxygenase 1 Homo sapiens 26-30 18485456-4 2009 RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin. Hemin 26-31 heme oxygenase 1 Homo sapiens 13-17 18485456-4 2009 RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin. Hemin 26-31 heme oxygenase 1 Homo sapiens 54-58 18485456-4 2009 RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin. Hemin 26-31 heme oxygenase 1 Homo sapiens 54-58 18485456-4 2009 RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin. Hemin 172-177 heme oxygenase 1 Homo sapiens 13-17 18381758-2 2008 Here we report that both HO-1 expression and activity can be highly increased in undifferentiated human mesenchymal stem cells (MSCs) treated with hemin, a known HO-1 inducer. Hemin 147-152 heme oxygenase 1 Homo sapiens 162-166 18172853-6 2008 Protein levels of gamma-GCS and heme oxygenase-1 (HO-1), two MARE-containing genes, were also increased after hemin treatment. Hemin 110-115 heme oxygenase 1 Homo sapiens 32-48 18026199-10 2007 Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments. Hemin 15-20 heme oxygenase 1 Homo sapiens 55-59 18215737-6 2008 Furthermore, hemin induced HO-1 expression, and HO-1 knockdown, HO-1 inhibition, or CO scavengers all reversed the prosurvival effects of hemin. Hemin 13-18 heme oxygenase 1 Homo sapiens 27-31 18026199-10 2007 Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments. Hemin 15-20 heme oxygenase 1 Homo sapiens 98-102 18026199-10 2007 Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments. Hemin 15-20 heme oxygenase 1 Homo sapiens 98-102 17973866-2 2007 Heme compounds, like hemin, a heme oxygenase-1 inducer, are used in the treatment of acute porphyria treatment. Hemin 21-26 heme oxygenase 1 Homo sapiens 30-46 17219054-6 2007 Conversely, increasing HO-1 protein level by hemin prior to irradiation is cytoprotective. Hemin 45-50 heme oxygenase 1 Homo sapiens 23-27 17729116-0 2007 Hemin-induced Erk1/2 activation and heme oxygenase-1 expression in human umbilical vein endothelial cells. Hemin 0-5 heme oxygenase 1 Homo sapiens 36-52 17079780-4 2007 Heme oxygenase-1 expression increased dramatically in cytosolic and mitochondrial fractions of human alveolar (A549), or bronchial epithelial cells (Beas-2b) exposed to either hemin, lipopolysaccharide, or CSE. Hemin 176-181 heme oxygenase 1 Homo sapiens 0-16 16858012-11 2006 The inflammation was suppressed by treatment with hemin, an inducer of HO-1, and enhanced by zinc protoporphyrin, an inhibitor of HO-1. Hemin 50-55 heme oxygenase 1 Homo sapiens 71-75 17204476-5 2007 Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction. Hemin 89-94 heme oxygenase 1 Homo sapiens 115-131 17204476-5 2007 Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction. Hemin 89-94 heme oxygenase 1 Homo sapiens 210-226 16474202-4 2006 Increased HO-1 induction by hemin resulted in a significant decrease in the Lyso-PC-mediated induction of MCP-1 mRNA expression. Hemin 28-33 heme oxygenase 1 Homo sapiens 10-14 16959797-6 2006 511, 21-27], and then examined the effect of DCFH-DA on the induction of HO-1 expression by arsenite, cadmium and hemin, which induce oxidative stress and cytotoxicity. Hemin 114-119 heme oxygenase 1 Homo sapiens 73-77 16495208-2 2006 We have reported recently that nitric oxide (NO) augments the incorporation of free hemin in endothelial cells, resulting in amplified HO-1 expression and production of bilirubin. Hemin 84-89 heme oxygenase 1 Homo sapiens 135-139 16545694-3 2006 RESULTS: Treatment of HaCaT keratinocytes with hemin (heme chloride) induced HO-1 expression and activity. Hemin 47-52 heme oxygenase 1 Homo sapiens 77-81 16545694-7 2006 Moreover, HO-1 expression was also induced in keratinocytes cultured in hypoxia, with concomitant augmentation of VEGF production, which was further potentiated by hemin stimulation. Hemin 164-169 heme oxygenase 1 Homo sapiens 10-14 16545694-9 2006 CONCLUSIONS: HO-1 is involved in hemin-induced VEGF expression in HaCaT and may play a role in hypoxic regulation of this protein. Hemin 33-38 heme oxygenase 1 Homo sapiens 13-17 16474202-5 2006 SnPP (IX), the specific inhibitor of HO-1 enzymatic activity, prevented the hemin-mediated attenuation of MCP-1 mRNA expression. Hemin 76-81 heme oxygenase 1 Homo sapiens 37-41 16234431-6 2005 When HO-1 was induced by hemin in vitro, a significant dose-dependent inhibition of osteoclastogenesis was observed. Hemin 25-30 heme oxygenase 1 Homo sapiens 5-9 16329999-11 2006 However, endogenous overproduction of CO by super-induction of HO-1 (obtained by pretreatment of macrophages with either buthionine sulfoximine or hemin) decreased the LPS-derived iNOS expression without affecting cell survival. Hemin 147-152 heme oxygenase 1 Homo sapiens 63-67 16181113-3 2005 In a prior study, we reported that increasing HO-1 expression by adenoviral gene transfer prior to hemin exposure attenuated oxidative stress and cell death in astrocytes. Hemin 99-104 heme oxygenase 1 Homo sapiens 46-50 16308001-4 2005 The aim of our study was to induce heme oxygenase 1 by using hemin in human internal thoracic and radial arteries and to evaluate the effect of this induction on the contractility of these arterial grafts. Hemin 61-66 heme oxygenase 1 Homo sapiens 35-51 16308001-11 2005 Immunohistochemical staining revealed a large expression of heme oxygenase 1 in all vascular layers of hemin-treated internal thoracic artery and radial artery rings. Hemin 103-108 heme oxygenase 1 Homo sapiens 60-76 16308001-12 2005 Enzyme-linked immunosorbent assay studies showed a significant increase in heme oxygenase 1 levels in hemin-treated internal thoracic artery and radial artery rings. Hemin 102-107 heme oxygenase 1 Homo sapiens 75-91 16308001-13 2005 CONCLUSION: Hemin caused in vitro induction of heme oxygenase 1 in human internal thoracic artery and radial artery grafts. Hemin 12-17 heme oxygenase 1 Homo sapiens 47-63 12709592-8 2003 HO-1 activity was determined by the ability of the enzyme to generate bilirubin from hemin. Hemin 85-90 heme oxygenase 1 Homo sapiens 0-4 15258907-3 2004 The results show that HO-1 is significantly induced by hemin and cadmium. Hemin 55-60 heme oxygenase 1 Homo sapiens 22-26 15258907-4 2004 In addition to inducing HO-1, hemin and cadmium also cause a rise in the levels of p21, a cyclin-dependent kinase inhibitor. Hemin 30-35 heme oxygenase 1 Homo sapiens 24-28 14647439-4 2004 The cells were treated with hemin and cadmium to induce HO-1. Hemin 28-33 heme oxygenase 1 Homo sapiens 56-60 14647439-5 2004 The result showed that HO-1 protein was significantly induced by hemin and cadmium in both cells tested. Hemin 65-70 heme oxygenase 1 Homo sapiens 23-27 12969148-6 2003 RESULTS: In HRPTECs, both HO-1 mRNA expression and protein production peaked at around 12 h and persisted until 24 h after hemin stimulation. Hemin 123-128 heme oxygenase 1 Homo sapiens 26-30 12622689-5 2003 A role for haem metabolites in modulating HO-1 expression by NO was assessed by exposing cells to SNAP, SNP or DETA/NO in medium derived from cells treated with haemin, which contained increased bilirubin levels. Hemin 161-167 heme oxygenase 1 Homo sapiens 42-46 15611319-2 2005 We studied the effects of heme oxygenase-1 (HO-1) induced by its substrate hemin on apoptosis, caspase-3 expression and the differentiation of freshly isolated human monocytes. Hemin 75-80 heme oxygenase 1 Homo sapiens 26-42 15611319-2 2005 We studied the effects of heme oxygenase-1 (HO-1) induced by its substrate hemin on apoptosis, caspase-3 expression and the differentiation of freshly isolated human monocytes. Hemin 75-80 heme oxygenase 1 Homo sapiens 44-48 15611319-3 2005 Hemin induced HO-1 in a dose- and time-dependent fashion as measured by semi-quantitative RT-PCR and flow cytometry. Hemin 0-5 heme oxygenase 1 Homo sapiens 14-18 15589375-8 2005 Results indicate that the HO-1 and HO-2 cells are more resistant than controls to hemin and to the organic tert-butyl hydroperoxide, t-BuOOH. Hemin 82-87 heme oxygenase 1 Homo sapiens 26-39 15339982-11 2004 In conclusion, VT augments hemin-induced toxicity in renal tubular epithelial cells that can be reversed by prior induction of HO-1. Hemin 27-32 heme oxygenase 1 Homo sapiens 127-131 12947311-5 2003 METHODS: Human umbilical vein endothelial cells were pretreated with hemin (100 micromol/L) for 5 hours, and the induction of HO-1 was confirmed by Western blot. Hemin 69-74 heme oxygenase 1 Homo sapiens 126-130 12947311-8 2003 RESULTS: HO-1 protein was increased 3-fold by exposure to hemin under all conditions. Hemin 58-63 heme oxygenase 1 Homo sapiens 9-13 11571246-3 2001 METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells. Hemin 204-209 heme oxygenase 1 Homo sapiens 100-104 12646399-6 2003 Pretreatment of monolayers with hemin for 2 h followed by 18 h in complete medium resulted in HO-1 induction and the attenuation of H(2)O(2)-mediated increases in endothelial permeability, and significantly improved the restoration of endothelial barrier function 48 h later. Hemin 32-37 heme oxygenase 1 Homo sapiens 94-98 12699247-3 2002 In this study, we report that exposure of cardiac cells to hemin (5-20 microM) in combination with compounds that liberate nitroxyl (HNO/NO-) or release NO significantly potentiates HO-1 mRNA and protein expression leading to a remarkable increase in heme oxygenase activity under both normoxic and hypoxic conditions. Hemin 59-64 heme oxygenase 1 Homo sapiens 182-186 12699247-4 2002 The amplification of the heme oxygenase pathway appears to involve a direct interaction between heme and the NO groups, as the ability of both NO(-)- and NO-releasing agents to induce HO-1 is totally lost by their pre-incubation for 1 hr in complete medium prior to cell treatment but is highly preserved by addition of hemin during the preincubation step. Hemin 320-325 heme oxygenase 1 Homo sapiens 184-188 11571246-3 2001 METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells. Hemin 204-209 heme oxygenase 1 Homo sapiens 115-119 10807584-6 2000 In vitro studies in human renal proximal tubule cells demonstrate that hemin, an inducer of HO-1, significantly attenuated cisplatin-induced apoptosis and necrosis, whereas inhibition of HO-1 enzyme activity reversed the cytoprotective effect. Hemin 71-76 heme oxygenase 1 Homo sapiens 92-96 11435909-5 2001 In this study, we showed high expression of HO-1 in lesions of EAE, and demonstrated that hemin, an inducer of HO-1, inhibited EAE effectively. Hemin 90-95 heme oxygenase 1 Homo sapiens 44-48 11435909-5 2001 In this study, we showed high expression of HO-1 in lesions of EAE, and demonstrated that hemin, an inducer of HO-1, inhibited EAE effectively. Hemin 90-95 heme oxygenase 1 Homo sapiens 111-115 10589693-6 1999 Glomerular HO-1 expression in nephritic animals was upregulated by treatment with hemin (30 micromol/kg body wt). Hemin 82-87 heme oxygenase 1 Homo sapiens 11-15 10589693-12 1999 Hemin treatment of nephritic animals resulted in upregulation of glomerular HO-1 levels and a two- to threefold reduction in glomerular iNOS mRNA levels. Hemin 0-5 heme oxygenase 1 Homo sapiens 76-80 10589693-15 1999 These studies demonstrate that in glomerular immune injury, hemin treatment upregulates glomerular HO-1 with an attendant downregulation of iNOS expression, and thus points to regulatory interaction between the two systems. Hemin 60-65 heme oxygenase 1 Homo sapiens 99-103 9722676-0 1998 Involvement of the tyrosine phosphorylation pathway in induction of human heme oxygenase-1 by hemin, sodium arsenite, and cadmium chloride. Hemin 94-99 heme oxygenase 1 Homo sapiens 74-90 10581397-6 1999 When the time-course of HO-1 expression was compared between dopamine and hemin, the latter induced the gene immediately while the former did so with a lag. Hemin 74-79 heme oxygenase 1 Homo sapiens 24-28 10349844-8 1999 Moreover, pretreatment with interferon-gamma partially suppressed the induction of heme oxygenase-1 mRNA expression caused by either sodium nitroprusside, cadmium, or hemin. Hemin 167-172 heme oxygenase 1 Homo sapiens 83-99 9722676-4 1998 Genistein (50 microM), another tyrosine kinase inhibitor, also inhibited the induction of HO-1 mRNA by hemin, arsenite, and cadmium. Hemin 103-108 heme oxygenase 1 Homo sapiens 90-94 9722676-5 1998 Nuclear runoff assays revealed that herbimycin blocked the hemin-induced transcription of the HO-1 gene. Hemin 59-64 heme oxygenase 1 Homo sapiens 94-98 9722676-8 1998 When HeLa cells were treated with a specific inhibitor of the mitogen-activated protein kinase (MAPK)/extracellular-signal regulated kinase cascade, PD58059 (100 microM), suppression of the cadmium-dependent HO-1 induction was not observed, but the hemin- or arsenite-dependent induction was slightly inhibited. Hemin 249-254 heme oxygenase 1 Homo sapiens 208-212 9722676-1 1998 The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined. Hemin 137-142 heme oxygenase 1 Homo sapiens 77-93 9722676-1 1998 The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined. Hemin 137-142 heme oxygenase 1 Homo sapiens 95-99 9722676-2 1998 The induction of HO-1 mRNA by hemin was inhibited when the cells were pretreated with herbimycin A. Hemin 30-35 heme oxygenase 1 Homo sapiens 17-21 9337616-8 1997 Because either hemin alone or UVA radiation are able to lead to a refractoriness of the heme oxygenase-1 gene to reinduction by a second exposure to one or the other agent in human fibroblasts, we conclude that heme, or an as yet unidentified heme derivative, is involved in the refractoriness response. Hemin 15-20 heme oxygenase 1 Homo sapiens 88-104 34728736-0 2021 Hemin as a novel candidate for treating COVID-19 via heme oxygenase-1 induction. Hemin 0-5 heme oxygenase 1 Homo sapiens 53-69 9276739-5 1997 Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment. Hemin 139-144 heme oxygenase 1 Homo sapiens 0-16 9276739-5 1997 Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment. Hemin 139-144 heme oxygenase 1 Homo sapiens 18-22 8783636-8 1996 In conclusion, two interrelated stressors, H2O2 and hemin, produced a stimulation of HO-1, and this was associated with a reduction in the viability of BSC-1 cells. Hemin 52-57 heme oxygenase 1 Homo sapiens 85-89 8652820-7 1996 Interestingly, heat shock abolished the remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1-0-A cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably induced. Hemin 130-135 heme oxygenase 1 Homo sapiens 77-93 33761605-0 2021 Heme oxygenase-1 inducer hemin does not inhibit SARS-CoV-2 virus infection. Hemin 25-30 heme oxygenase 1 Homo sapiens 0-16 33761605-3 2021 Given that hemin is a natural inducer of the HO-1 gene, the aim of this study was to develop an in vitro assay to analyze the antiviral potency of hemin against SARS-CoV-2 infection. Hemin 11-16 heme oxygenase 1 Homo sapiens 45-49 33761605-3 2021 Given that hemin is a natural inducer of the HO-1 gene, the aim of this study was to develop an in vitro assay to analyze the antiviral potency of hemin against SARS-CoV-2 infection. Hemin 147-152 heme oxygenase 1 Homo sapiens 45-49 33761605-7 2021 Hemin administration to the culture medium induced a high induction in the expression of the HO-1 gene that was stronger in Vero-E6 macaque-derived cells than in the human Calu-3 cell line. Hemin 0-5 heme oxygenase 1 Homo sapiens 93-97 33761605-9 2021 In conclusion, although exposure to hemin induced strong HO-1 up-regulation, this effect was unable to inhibit or delay the progression of SARS-CoV-2 infection in two epithelial cell lines susceptible to infection. Hemin 36-41 heme oxygenase 1 Homo sapiens 57-61 19161347-7 2009 IBTP had no effect on basal HO-1 levels, but effectively blocked HO-1 induction by a variety of reagents including haemin, iodoacetamide and 15d-PGJ2. Hemin 115-121 heme oxygenase 1 Homo sapiens 65-69 34953799-10 2022 However, the increased cell sensitivity induced by MSK1 downregulation was reversed by the induction of HO-1 inducer Hemin. Hemin 117-122 heme oxygenase 1 Homo sapiens 104-108 34728736-5 2021 To confirm whether HO-1 suppresses SARS-CoV-2 infection, we assessed the antiviral activity of hemin, an effective and safe HO-1 inducer, in SARS-CoV-2 infection. Hemin 95-100 heme oxygenase 1 Homo sapiens 124-128 34728736-10 2021 Overall, the findings suggested that HO-1, induced by hemin, effectively suppressed SARS-CoV-2 in vitro. Hemin 54-59 heme oxygenase 1 Homo sapiens 37-41 34452191-5 2021 Hemin (HO-1 inducer) induced HO-1 mRNA and protein expression, as expected, and below 50 mM, dose-dependently reduced the viral RNA and proteins in the HAV-infected cells without cytotoxicity. Hemin 0-5 heme oxygenase 1 Homo sapiens 7-11 34448349-4 2021 After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively. Hemin 114-119 heme oxygenase 1 Homo sapiens 210-226 34448349-4 2021 After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively. Hemin 114-119 heme oxygenase 1 Homo sapiens 228-233 34452191-5 2021 Hemin (HO-1 inducer) induced HO-1 mRNA and protein expression, as expected, and below 50 mM, dose-dependently reduced the viral RNA and proteins in the HAV-infected cells without cytotoxicity. Hemin 0-5 heme oxygenase 1 Homo sapiens 29-33 35598290-9 2022 Furthermore, hemin"s induction of GPX4 involved HO-1 and nuclear factor Nrf2. Hemin 13-18 heme oxygenase 1 Homo sapiens 48-52 34208670-5 2021 After HO-1 pharmacological induction with hemin, PC3 and C4-2B cells exhibited a significantly impaired cellular metabolic rate, reflected by glucose uptake, ATP production, lactate dehydrogenase (LDH) activity and extracellular lactate levels. Hemin 42-47 heme oxygenase 1 Homo sapiens 6-10 35598290-0 2022 Hemin mitigates contrast-induced nephropathy by inhibiting ferroptosis via HO-1/Nrf2/GPX4 pathway. Hemin 0-5 heme oxygenase 1 Homo sapiens 75-79 35598290-10 2022 Either HO-1 or Nrf2 inhibitor prevented hemin"s effect on GPX4 to a comparable extent, and over-expression of Nrf2 increased GPX4 expression. Hemin 40-45 heme oxygenase 1 Homo sapiens 7-11 35598290-12 2022 Thus, we showed hemin mitigated CIN, inhibiting oxidative stress and ferroptosis, by upregulation of GPX4 via activation of HO-1/Nrf2. Hemin 16-21 heme oxygenase 1 Homo sapiens 124-128 35453452-6 2022 Interestingly, treatment of cells with either hemin, an HO-1 inducer, or supplementation with carbon monoxide (CO), a by-product of HO-1 enzymatic activity, increased TLR4 expression. Hemin 46-51 heme oxygenase 1 Homo sapiens 56-60 35428017-7 2022 HO-1 expression in SW480 was increased with all hemin concentrations and HO-2 expression was downregulated at the highest hemin concentration. Hemin 122-127 heme oxygenase 1 Homo sapiens 0-4 35428017-12 2022 CONCLUSION: HO-1 and HO-2 expression is respectively induced and repressed by exogenous hemin in normal colon and colon cancer cells. Hemin 88-93 heme oxygenase 1 Homo sapiens 12-16 35428017-3 2022 METHODS: HO-1 and HO-2 expression alterations in normal colonic epithelial (FHC) and colon cancer cells (SW480) were explored following treatment with 0 microM, 25 microM, 100 microM and 250 microM concentrations of hemin, using qPCR. Hemin 216-221 heme oxygenase 1 Homo sapiens 9-13 35428017-6 2022 RESULTS: Low concentrations of hemin caused upregulation and high concentration caused downregulation of HO-1 expression, whereas HO-2 expression was significantly downregulated with all hemin concentrations in FHC. Hemin 31-36 heme oxygenase 1 Homo sapiens 105-109 35428017-7 2022 HO-1 expression in SW480 was increased with all hemin concentrations and HO-2 expression was downregulated at the highest hemin concentration. Hemin 48-53 heme oxygenase 1 Homo sapiens 0-4 32968051-9 2020 Hemin caused stabilization and nuclear translocation of Nrf2, which induced heme oxygenase-1 (HO-1) and ferritin heavy chain (FtH). Hemin 0-5 heme oxygenase 1 Homo sapiens 76-92 35419025-8 2022 Finally, Hemin, the agonist of HO-1, was applied in rescue assays, thereby verifying the mechanism of KLF7 modulating osteoclast differentiation by HO-1. Hemin 9-14 heme oxygenase 1 Homo sapiens 31-35 35047060-4 2022 Methods: An HO-1 inducer Hemin or an HO-1 inhibitor ZnPP-IX was used to treat the activated HSC-T6, respectively. Hemin 25-30 heme oxygenase 1 Homo sapiens 12-16 33664571-6 2021 Subsequently, for oxidative stress parameter detection, the cells were pre-treated with hemin to induce HO-1 expression prior to CuNP treatment. Hemin 88-93 heme oxygenase 1 Homo sapiens 104-108 33664571-8 2021 Furthermore, hemin pretreatment induced HO-1 expression in cells, which partially reduced the accumulation of reactive oxygen species induced by CuNPs and increased the levels of antioxidant enzymes. Hemin 13-18 heme oxygenase 1 Homo sapiens 40-44 33254548-5 2020 HO-1 is induced by hemin, a well-tolerated molecule, used for decades in the treatment of acute intermittent porphyria. Hemin 19-24 heme oxygenase 1 Homo sapiens 0-4 32968051-11 2020 Chemical inhibition or genetic knockdown of HO-1 potentiated hemin-triggered ROS generation and oxidative DNA damage preferentially in HCEC. Hemin 61-66 heme oxygenase 1 Homo sapiens 44-48 32968051-12 2020 Furthermore, HO-1 abrogation strongly augmented the cytotoxic effects of hemin in HCEC, revealing its pivotal function in colonocytes and highlighting the toxicity of free intracellular heme iron. Hemin 73-78 heme oxygenase 1 Homo sapiens 13-17 32968051-14 2020 Importantly, HO-1 conferred protection against the detrimental effects of hemin. Hemin 74-79 heme oxygenase 1 Homo sapiens 13-17 32968051-9 2020 Hemin caused stabilization and nuclear translocation of Nrf2, which induced heme oxygenase-1 (HO-1) and ferritin heavy chain (FtH). Hemin 0-5 heme oxygenase 1 Homo sapiens 94-98 29797346-0 2018 Hemin provides protection against lead neurotoxicity through heme oxygenase 1/carbon monoxide activation. Hemin 0-5 heme oxygenase 1 Homo sapiens 61-77 32581238-6 2020 Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls. Hemin 21-26 heme oxygenase 1 Homo sapiens 13-17 32581238-6 2020 Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls. Hemin 21-26 heme oxygenase 1 Homo sapiens 234-238 32581238-8 2020 Our results suggest a mechanism that excess hemin of beta-thalassaemia patients is a significant cause of immune suppression via HO-1 induction and may underlie the susceptibility of these individuals to severe bacterial infection. Hemin 44-49 heme oxygenase 1 Homo sapiens 129-133 32485912-0 2020 Roles of JNK/Nrf2 Pathway on Hemin-Induced Heme Oxygenase-1 Activation in MCF-7 Human Breast Cancer Cells. Hemin 29-34 heme oxygenase 1 Homo sapiens 43-59 32485912-2 2020 In this study, we investigated that the mechanisms of hemin-induced HO-1 expression and its signaling pathways in human breast cancer cell. Hemin 54-59 heme oxygenase 1 Homo sapiens 68-72 32485912-4 2020 Hemin increased HO-1 expression in MCF-7 cells in a dose- and time-dependent manner. Hemin 0-5 heme oxygenase 1 Homo sapiens 16-20 32485912-5 2020 Hemin enhanced HO-1 expression through the activation of c-Jun N-terminal kinases (JNK) signaling pathway. Hemin 0-5 heme oxygenase 1 Homo sapiens 15-19 32485912-6 2020 Hemin also induced activation of Nrf2, a major transcription factor of HO-1 expression. Hemin 0-5 heme oxygenase 1 Homo sapiens 71-75 32485912-8 2020 These results indicated that brazilin inhibits hemin-induced HO-1 expressions through inactivation of JNK/Nrf2 in MCF-7 cells. Hemin 47-52 heme oxygenase 1 Homo sapiens 61-65 32108290-8 2020 Our results showed that hemin was able to induce both HO-1 gene and protein expression in a cell-dependent manner being A172 more responsive to pharmacological upregulation of HO-1. Hemin 24-29 heme oxygenase 1 Homo sapiens 54-58 32108290-8 2020 Our results showed that hemin was able to induce both HO-1 gene and protein expression in a cell-dependent manner being A172 more responsive to pharmacological upregulation of HO-1. Hemin 24-29 heme oxygenase 1 Homo sapiens 176-180 30876940-6 2019 Hemin or ZnPP was combined to regulate heme oxygenase-1 (HO-1), and a pathway inhibitor was added to measure changes in the JNK/AP-1 signaling pathway. Hemin 0-5 heme oxygenase 1 Homo sapiens 39-55 30876940-6 2019 Hemin or ZnPP was combined to regulate heme oxygenase-1 (HO-1), and a pathway inhibitor was added to measure changes in the JNK/AP-1 signaling pathway. Hemin 0-5 heme oxygenase 1 Homo sapiens 57-61 31356851-10 2019 Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells. Hemin 86-91 heme oxygenase 1 Homo sapiens 14-30 31356851-10 2019 Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells. Hemin 96-101 heme oxygenase 1 Homo sapiens 14-30 31356851-10 2019 Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells. Hemin 96-101 heme oxygenase 1 Homo sapiens 14-30 30851935-3 2019 The cell oxidative stress models were incubated with Hemin (an inducer of HO-1), then, the HTR8/SVneo cells were transfected by ZO-1 small interfering RNA (siRNA). Hemin 53-58 heme oxygenase 1 Homo sapiens 74-78 30851935-6 2019 In both the trophoblastic and HUVEC oxidative stress models, HO-1 ZO-1 and occludin were increased incubated with Hemin. Hemin 114-119 heme oxygenase 1 Homo sapiens 61-65 29797346-3 2018 In this study, we applied hemin, the substrate and a well-known inducer of HO-1, to investigate the possible role of HO-1 in protecting against Pb neurotoxicity. Hemin 26-31 heme oxygenase 1 Homo sapiens 75-79 29797346-6 2018 However, knocking down HO-1 could significantly abolish the cytoprotective action of hemin against Pb toxicity, confirming HO-1 contributed to the protection. Hemin 85-90 heme oxygenase 1 Homo sapiens 23-27 29797346-6 2018 However, knocking down HO-1 could significantly abolish the cytoprotective action of hemin against Pb toxicity, confirming HO-1 contributed to the protection. Hemin 85-90 heme oxygenase 1 Homo sapiens 123-127 29797346-7 2018 Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells. Hemin 150-155 heme oxygenase 1 Homo sapiens 13-17 29797346-7 2018 Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells. Hemin 150-155 heme oxygenase 1 Homo sapiens 123-127 29797346-8 2018 Overall, this study showed that hemin provided protection against Pb neurotoxicity by HO-1/carbon monoxide activation. Hemin 32-37 heme oxygenase 1 Homo sapiens 86-90 29896252-4 2018 HSCs-T6 were incubated with different concentrations of hemin (HO-1 chemical inducer) and Znpp-IX (HO-1 chemical inhibitor) for 12, 24 and 48 h. Cell viability was determined using an MTT assay. Hemin 56-61 heme oxygenase 1 Homo sapiens 63-67 29498764-8 2018 Moreover, we showed that both in animal model and in human liver, frequent hemin infusions generate a chronic inflammatory hepatic disease which induces HO1 remotely to hemin treatment and maintains a high ALAS1 level responsible for recurrence. Hemin 75-80 heme oxygenase 1 Homo sapiens 153-156 29498764-8 2018 Moreover, we showed that both in animal model and in human liver, frequent hemin infusions generate a chronic inflammatory hepatic disease which induces HO1 remotely to hemin treatment and maintains a high ALAS1 level responsible for recurrence. Hemin 169-174 heme oxygenase 1 Homo sapiens 153-156