PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16642978-1 2006 A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL). Proline 105-112 peptidase D Homo sapiens 17-26 17081196-2 2006 Prolidase is a Mn(2+)-dependent dipeptidase that cleaves imidodipeptides containing C-terminal proline or hydroxyproline. Proline 95-102 peptidase D Homo sapiens 0-9 16634881-3 2006 Prolidase, an imidodipeptide-cleaving cytosolic enzyme, plays an important role in the collagen catabolic process by recycling proline for collagen synthesis. Proline 127-134 peptidase D Homo sapiens 0-9 16642978-1 2006 A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL). Proline 105-112 peptidase D Homo sapiens 28-31 16642978-2 2006 A detection limit of 12.2 fmol (S/N = 3) for proline, corresponding to 1.22 x 10(-8) units of prolidase catalyzing for 1 min was achieved. Proline 45-52 peptidase D Homo sapiens 94-103 15804176-0 2005 Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs. Proline 61-68 peptidase D Homo sapiens 0-9 16470701-1 2006 Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline. Proline 168-175 peptidase D Homo sapiens 15-26 16470701-1 2006 Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline. Proline 168-175 peptidase D Homo sapiens 28-32 16470701-1 2006 Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline. Proline 168-175 peptidase D Homo sapiens 64-73 21783632-7 2005 Prolidase [E.C.3.4.13.9] is a cytosolic metalloproteinase, which specifically splits imidodipeptides with C-terminal proline that is recycled for collagen biosynthesis. Proline 117-124 peptidase D Homo sapiens 0-9 15804176-2 2005 The analyses indicated that prolidase might be a desirable enzyme target based on its differential expression in melanoma cancer cell lines and its high substrate specificity for dipeptides containing proline at the carboxy terminus. Proline 201-208 peptidase D Homo sapiens 28-37 15337432-1 2004 Proline analogue of melphalan (Mel-pro) is one of the pro-drugs activated by prolidase, cytoplasmic imidodipeptidase highly expressed in some neoplastic tissues. Proline 0-7 peptidase D Homo sapiens 77-86 15265726-1 2004 Proline-containing peptides of the X-proline type are cleaved by the dipeptidase prolidase. Proline 0-7 peptidase D Homo sapiens 81-90 15265726-2 2004 The classical method of prolidase assay relied on the colorimetric estimation of the liberated proline with ninhydrin using acidic media and heat. Proline 95-102 peptidase D Homo sapiens 24-33 15173663-8 2004 This suggests that a decrease in prolidase activity may contribute to a decrease in the biosynthesis of proline-containing proteins, such as collagen and SOS. Proline 104-111 peptidase D Homo sapiens 33-42 15173663-2 2004 The mechanism of their action on collagen biosynthesis involves inactivation of prolidase, the enzyme that recovers proline from collagen degradation products for collagen re-synthesis. Proline 116-123 peptidase D Homo sapiens 80-89 11733182-10 2002 Prolidase activity was almost 3-fold lower in the preeclamptic extract (240.6+/-29.3 nmol Pro x min(-1) x mg(-1) protein) in comparison to the control (608.2+/-63.7 nmol Pro x min(-1) x mg(-1)protein). Proline 90-93 peptidase D Homo sapiens 0-9 14572862-0 2003 Proline analogue of melphalan as a prodrug susceptible to the action of prolidase in breast cancer MDA-MB 231 cells. Proline 0-7 peptidase D Homo sapiens 72-81 14572862-1 2003 Proline analogue of melphalan (Mel-pro) was synthesized as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase-prolidase [E.C.3.4.13.9]. Proline 0-7 peptidase D Homo sapiens 151-160 14572862-2 2003 Conjugation of melphalan (Mel) with proline (Pro) through imido-bond resulted in formation of a good substrate for prolidase. Proline 36-43 peptidase D Homo sapiens 115-124 14572862-2 2003 Conjugation of melphalan (Mel) with proline (Pro) through imido-bond resulted in formation of a good substrate for prolidase. Proline 45-48 peptidase D Homo sapiens 115-124 14572862-3 2003 Cytosolic location of prolidase in neoplastic cell suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertible prodrug. Proline 65-72 peptidase D Homo sapiens 22-31 14572862-3 2003 Cytosolic location of prolidase in neoplastic cell suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertible prodrug. Proline 65-72 peptidase D Homo sapiens 120-129 11338665-0 2001 Decreased cytotoxicity and increased antimitotic activity of a proline analogue of chlorambucil as a prodrug susceptible to the action of fibroblast"s prolidase. Proline 63-70 peptidase D Homo sapiens 151-160 11680815-0 2001 Cytotoxicity and effect on collagen biosynthesis of proline analogue of melphalan as a prolidase-convertible prodrug in cultured human skin fibroblasts. Proline 52-59 peptidase D Homo sapiens 87-96 11680815-1 2001 Proline analogue of melphalan (MEL-PRO) was synthesised as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase--prolidase [E.C.3.4.13.9]. Proline 0-7 peptidase D Homo sapiens 152-161 11680815-2 2001 Conjugation of melphalan (MEL) with proline (PRO) through an imido-bond resulted in formation of a good substrate for prolidase. Proline 36-43 peptidase D Homo sapiens 118-127 11680815-2 2001 Conjugation of melphalan (MEL) with proline (PRO) through an imido-bond resulted in formation of a good substrate for prolidase. Proline 45-48 peptidase D Homo sapiens 118-127 11451388-1 2001 Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides. Proline 115-122 peptidase D Homo sapiens 0-9 11451388-1 2001 Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides. Proline 115-122 peptidase D Homo sapiens 54-70 11338665-1 2001 We synthesized an proline analogue of chlorambucil (CH-pro) as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidopeptidase--prolidase [E.C.3.4.13.9]. Proline 18-25 peptidase D Homo sapiens 154-163 11338665-2 2001 A conjugation of chlorambucil (CH) with proline through an imido-bond resulted in the formation of a good substrate for prolidase. Proline 40-47 peptidase D Homo sapiens 120-129 11820612-3 2001 Cytosolic location of prolidase in neoplastic cells suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertable pro-drug. Proline 66-73 peptidase D Homo sapiens 121-130 11820611-2 2001 Prolidase evokes the ability to hydrolyse the imido-bond of various low molecular weight compounds coupled to L-proline. Proline 110-119 peptidase D Homo sapiens 0-9 11820611-4 2001 Treatment of these prodrugs with prolidase generated L-proline and the free drug, demonstrating their substrate susceptibility prolidase. Proline 53-62 peptidase D Homo sapiens 33-42 11820611-4 2001 Treatment of these prodrugs with prolidase generated L-proline and the free drug, demonstrating their substrate susceptibility prolidase. Proline 53-62 peptidase D Homo sapiens 127-136 11820612-0 2001 Proline analogue of melphalan as a prolidase-convertible pro-drug in breast cancer MCF-7 cells. Proline 0-7 peptidase D Homo sapiens 35-44 11820612-1 2001 Prolidase [E.C.3.4.13.9] is ubiquitously distributed cytosolic egzopeptidase that is known to cleave imido-bond of some low molecular weight compounds coupled to L-proline. Proline 162-171 peptidase D Homo sapiens 0-9 11820612-2 2001 Previously we have found that conjugation of antineoplastic drug--melphalan (Mel) with proline (pro) through imido-bond resulted in formation of a good substrate for purified prolidase. Proline 87-94 peptidase D Homo sapiens 175-184 11820612-2 2001 Previously we have found that conjugation of antineoplastic drug--melphalan (Mel) with proline (pro) through imido-bond resulted in formation of a good substrate for purified prolidase. Proline 87-90 peptidase D Homo sapiens 175-184 11820612-3 2001 Cytosolic location of prolidase in neoplastic cells suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertable pro-drug. Proline 66-73 peptidase D Homo sapiens 22-31 11137854-4 2001 Prolidase [EC 3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen synthesis. Proline 70-77 peptidase D Homo sapiens 0-9 11137854-4 2001 Prolidase [EC 3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen synthesis. Proline 105-112 peptidase D Homo sapiens 0-9 10451808-1 1999 Prolidase [EC 3.4.13.9] plays an important role in the recycling of proline for collagen synthesis and cell growth. Proline 68-75 peptidase D Homo sapiens 0-9 11204951-0 2000 Prolidase-activated prodrug for cancer chemotherapy cytotoxic activity of proline analogue of chlorambucil in breast cancer MCF-7 cells. Proline 74-81 peptidase D Homo sapiens 0-9 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 118-127 peptidase D Homo sapiens 8-17 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 118-127 peptidase D Homo sapiens 290-299 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 118-127 peptidase D Homo sapiens 290-299 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 162-171 peptidase D Homo sapiens 8-17 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 162-171 peptidase D Homo sapiens 290-299 11204951-2 2000 Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity. Proline 162-171 peptidase D Homo sapiens 290-299 11204951-4 2000 Treatment of this prodrug with prolidase generated the L-proline and the free drug, demonstrating its substrate susceptibility to prolidase. Proline 55-64 peptidase D Homo sapiens 31-40 11204951-4 2000 Treatment of this prodrug with prolidase generated the L-proline and the free drug, demonstrating its substrate susceptibility to prolidase. Proline 55-64 peptidase D Homo sapiens 130-139 10582130-1 1999 Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins. Proline 9-16 peptidase D Homo sapiens 95-104 9879669-1 1998 Prolidase [E.C.3.4.13.9] is a cytosolic exopeptidase that catalyses the hydrolysis of C-terminal proline containing dipeptides or tripeptides. Proline 97-104 peptidase D Homo sapiens 0-9 10697434-2 1999 Synthesis of proline analogues of melphalan and theirs susceptibility to the action of prolidase. Proline 13-20 peptidase D Homo sapiens 87-96 10697434-4 1999 The synthesis of proline analogues of melphalan (well known antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed. Proline 17-24 peptidase D Homo sapiens 134-143 10697434-6 1999 It suggests that targeting of prolidase as a proline analogue of melphalan-converting enzyme may serve as a novel strategy in therapy of neoplastic diseases. Proline 45-52 peptidase D Homo sapiens 30-39 9619859-1 1998 Prolidase (EC 3.4.13.9) is an ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of dipeptides containing C-terminal proline or hydroxyproline. Proline 138-145 peptidase D Homo sapiens 0-9 9972056-2 1998 Synthesis of proline analogue of anthraquinone-2-carboxylic acid and its susceptibility to the action of prolidase. Proline 13-20 peptidase D Homo sapiens 105-114 9798267-4 1998 Prolidase [E.C.3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen resynthesis. Proline 71-78 peptidase D Homo sapiens 0-9 9798267-4 1998 Prolidase [E.C.3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen resynthesis. Proline 106-113 peptidase D Homo sapiens 0-9 9972056-4 1998 The synthesis of proline analogue of anthraquinone-2-carboxylic acid (potential antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed. Proline 17-24 peptidase D Homo sapiens 154-163 9972056-8 1998 Although insolubility of the proline analogue of anthraquinone-2-carboxylic acid in aqueous solutions limit its potential therapeutic value, the presented data suggest that prolidase may have a broader substrate specificity than thought previously. Proline 29-36 peptidase D Homo sapiens 173-182 9328822-1 1997 Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides. Proline 115-122 peptidase D Homo sapiens 0-9 9020526-4 1996 Prolidase plays an important role in the recycling of proline for collagen synthesis and cell growth and probably serves as an interface between protein nutrition and matrix breakdown. Proline 54-61 peptidase D Homo sapiens 0-9 9581474-0 1997 Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase. Proline 57-64 peptidase D Homo sapiens 0-9 9581474-0 1997 Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase. Proline 57-64 peptidase D Homo sapiens 130-139 9581474-2 1997 The synthesis of proline analogue of chlorambucil (well known antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed. Proline 17-24 peptidase D Homo sapiens 136-145 7748973-1 1995 Prolidase (EC: 3.4.13.9) catalyses the hydrolysis of the peptide bond involving the imino nitrogen of proline or hydroxyproline. Proline 102-109 peptidase D Homo sapiens 0-9 1437403-2 1992 The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline. Proline 65-72 peptidase D Homo sapiens 11-20 1437403-5 1992 Our results indicate that prolidase plays a major role in the recycling of dipeptide-bound proline. Proline 91-98 peptidase D Homo sapiens 26-35 2246246-1 1990 The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance. Proline 61-68 peptidase D Homo sapiens 42-51 1972707-1 1990 Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. Proline 94-101 peptidase D Homo sapiens 11-22 1972707-1 1990 Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. Proline 94-101 peptidase D Homo sapiens 0-9 1972707-1 1990 Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. Proline 143-150 peptidase D Homo sapiens 0-9 1972707-1 1990 Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. Proline 143-150 peptidase D Homo sapiens 11-22 34943229-8 2021 The amount of this amino acid is regulated at the level of prolidase (proline releasing enzyme), collagen biosynthesis (proline utilizing process), and glutamine, glutamate, alpha-ketoglutarate, and ornithine metabolism. Proline 70-77 peptidase D Homo sapiens 59-68 33818628-6 2021 Proline availability is regulated by prolidase (proline supporting enzyme), collagen biosynthesis (proline utilizing process) and proline synthesis from glutamine, glutamate, alpha-ketoglutarate (alpha-KG) and ornithine. Proline 0-7 peptidase D Homo sapiens 37-46 34880421-3 2021 We recently found that p53 binds via its proline-rich domain to peptidase D (PEPD) and is activated when the binding is disrupted. Proline 41-48 peptidase D Homo sapiens 64-75 34880421-3 2021 We recently found that p53 binds via its proline-rich domain to peptidase D (PEPD) and is activated when the binding is disrupted. Proline 41-48 peptidase D Homo sapiens 77-81 34943229-10 2021 It seems that in estrogen receptor-positive breast cancer cells, prolidase supports proline for collagen biosynthesis, limiting its availability for PRODH/POX-dependent apoptosis. Proline 84-91 peptidase D Homo sapiens 65-74 34577574-11 2021 In MCF-7 breast cancer cells, Cx affected proline metabolism through upregulation of proline biosynthesis, PRODH/POX and PYCRs expressions, PEPD activity, and downregulation of collagen biosynthesis. Proline 42-49 peptidase D Homo sapiens 140-144 34532344-1 2021 Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline. Proline 182-189 peptidase D Homo sapiens 0-9 34532344-1 2021 Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline. Proline 182-189 peptidase D Homo sapiens 40-44 3139928-1 1988 A 17-year-old girl was shown to have prolidase deficiency on the basis of the presence of large amounts of proline-containing dipeptides in urine and an almost complete absence of prolidase in plasma and erythrocytes. Proline 107-114 peptidase D Homo sapiens 37-46 2673209-5 1989 Products of most loci have multiple, overlapping substrate affinities (except for the products of Pep-D, which react only with a peptide containing a carboxyterminal proline). Proline 166-173 peptidase D Homo sapiens 98-103 35165443-5 2022 CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8. Proline 127-134 peptidase D Homo sapiens 39-48 35165443-5 2022 CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8. Proline 127-134 peptidase D Homo sapiens 50-54 35197125-1 2022 BACKGROUND: Prolidase deficiency (PD) is an autosomal recessive inborn multisystemic disease caused by mutations in the PEPD gene encoding the enzyme prolidase D, leading to defects in turnover of proline-containing proteins, such as collagen. Proline 197-204 peptidase D Homo sapiens 120-124 3148067-6 1988 We suggest that in prolidase-deficient fibroblasts, this rise in prolinase activity constitutes an attempt to compensate for the prolidase deficiency by increasing the greatly reduced intracellular proline pool. Proline 198-205 peptidase D Homo sapiens 19-28 7139961-0 1982 Optimal conditions for prolidase assay by proline colorimetric determination: application to iminodipeptiduria. Proline 42-49 peptidase D Homo sapiens 23-32 4084535-1 1985 In an effort to further develop the technique of isomer-specific proteolysis, a number of proline-containing substrates were subjected to hydrolysis in the presence of chymotrypsin, trypsin, or prolidase. Proline 90-97 peptidase D Homo sapiens 194-203 7139961-1 1982 Prolidase assay was reinvestigated by determining proline, using Chinard"s method. Proline 50-57 peptidase D Homo sapiens 0-9 33045291-1 2021 Prolidase is a metal-dependent peptidase specialized in the cleavage of dipeptides containing proline or hydroxyproline on their C-termini. Proline 94-101 peptidase D Homo sapiens 0-9 862347-11 1977 This correlation was not observed with unhydrolysed urine, and it appeared to reside in the diffusible fraction, part of whose proline could be liberated by prolidase digestion. Proline 127-134 peptidase D Homo sapiens 157-166 32815823-2 2021 Prolidase is a metalloprotease found in various tissues, which has been associated with the concentrations of proline, a neurotransmitter, in the brain. Proline 110-117 peptidase D Homo sapiens 0-9 32455636-1 2020 Prolidase is a ubiquitous enzyme that plays a major role in the metabolism of proline-rich proteins. Proline 78-85 peptidase D Homo sapiens 0-9 33287453-9 2020 Proline concentration and collagen biosynthesis were increased in HaCaT cells under prolidase treatment. Proline 0-7 peptidase D Homo sapiens 84-93 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). Proline 22-29 peptidase D Homo sapiens 77-86 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). Proline 95-102 peptidase D Homo sapiens 77-86 32918543-10 2020 RESULTS: Prolidase overexpression in MCF-7PL cells contributed to 10-fold increase in the enzyme activity, 3-fold increase in cytoplasmic proline level and decrease in cell viability and DNA biosynthesis compared to wild type MCF-7 cells. Proline 138-145 peptidase D Homo sapiens 9-18 32918543-16 2020 CONCLUSION: The data suggest that overexpression of prolidase in MCF-7 cells contributes to increase in intracellular proline concentration and PRODH/POX-dependent autophagic cell death. Proline 118-125 peptidase D Homo sapiens 52-61 32598484-1 2020 Prolidase catalyzes the cleavage of dipeptides containing proline on their C-terminus. Proline 58-65 peptidase D Homo sapiens 0-9 32824561-1 2020 Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline. Proline 97-104 peptidase D Homo sapiens 0-9 32824561-1 2020 Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline. Proline 97-104 peptidase D Homo sapiens 34-38 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 0-7 peptidase D Homo sapiens 148-157 29233996-4 2017 PEPD binds to the proline-rich domain in p53, which inhibits phosphorylation of nuclear p53 and MDM2-mediated mitochondrial translocation of nuclear and cytoplasmic p53. Proline 18-25 peptidase D Homo sapiens 0-4 30911252-2 2019 Prolidase has an extremely important role in proline recycling for collagen synthesis. Proline 45-52 peptidase D Homo sapiens 0-9 30066404-1 2018 Prolidase is a metallopeptidase that cleaves iminodipeptides containing a proline (Pro) or hydroxyproline (Hyp) residue at their C-terminal end. Proline 74-81 peptidase D Homo sapiens 0-9 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. Proline 23-30 peptidase D Homo sapiens 54-63 29568391-6 2018 In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells. Proline 23-30 peptidase D Homo sapiens 130-139 28382686-4 2017 In cells treated with 0.01, 0.03 and 0.05% MP a dose-dependent decrease in collagen biosynthesis was revealed, which was positively correlated with the activity of prolidase responsible for the recovery of proline. Proline 206-213 peptidase D Homo sapiens 164-173 28863383-2 2017 Previous studies suggested that this group of compounds affect prolidase activity (proline releasing enzyme from imidodipeptides) and collagen biosynthesis (proline utilizing process) providing substrate (proline) for proline oxidase (POX) dependent apoptosis. Proline 83-90 peptidase D Homo sapiens 63-72 28863383-10 2017 The data suggest that massive production of proline by proBet-dependent activation of prolidase and inhibition of proline utilization for collagen biosynthesis may represent mechanism for POX-dependent apoptosis in EA cells. Proline 44-51 peptidase D Homo sapiens 86-95 28677335-1 2017 Prolidase is a ubiquitously distributed dipeptidase and the only dipeptidase in humans capable of cleaving the peptide bond preceding the amino acids proline (Pro) or hydroxyproline (Hyp). Proline 150-157 peptidase D Homo sapiens 0-9 28942439-3 2017 We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase. Proline 26-33 peptidase D Homo sapiens 202-211 28942439-3 2017 We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase. Proline 134-141 peptidase D Homo sapiens 110-119 27040799-1 2016 Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline. Proline 99-106 peptidase D Homo sapiens 0-9 27067078-1 2017 The enzyme prolidase cleaves dipeptides where the C-terminal amino acid corresponds to proline or hydroxyproline. Proline 87-94 peptidase D Homo sapiens 11-20 27040799-1 2016 Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline. Proline 99-106 peptidase D Homo sapiens 25-41 27040799-14 2016 Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Proline 0-7 peptidase D Homo sapiens 90-99 27482243-2 2016 The prolidase enzyme is a cytosolic exopeptidase that detaches proline or hydroxyproline from the carboxyl terminal position of dipeptides. Proline 63-70 peptidase D Homo sapiens 4-13 27000973-3 2016 Prolidase plays an important role in collagen metabolism by degrading imidodipeptides, in which proline or hydroxyproline residue is located at the C-terminal end. Proline 96-103 peptidase D Homo sapiens 0-9 25691319-2 2015 Deficiency of prolidase leads to the increased excretion of proline in urine, which causes impaired collagen synthesis and delay in wound healing. Proline 60-67 peptidase D Homo sapiens 14-23 25943419-0 2016 High proline-related inhibition of serum prolidase enzyme activity in scleroderma. Proline 5-12 peptidase D Homo sapiens 41-50 27546702-1 2016 Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position. Proline 27-34 peptidase D Homo sapiens 0-9 26198764-11 2015 Among the novel potential susceptibility genes is PEPD, a gene involved in proline metabolism, which is associated with a Mendelian disorder characterized by developmental delay and cognitive deficits. Proline 75-82 peptidase D Homo sapiens 50-54 22512465-0 2012 Prolidase function in proline metabolism and its medical and biotechnological applications. Proline 22-29 peptidase D Homo sapiens 0-9 23479033-2 2013 Prolidase is known to have a crucial part in the recycling of proline for collagen synthesis. Proline 62-69 peptidase D Homo sapiens 0-9 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Proline 145-152 peptidase D Homo sapiens 0-9 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Proline 145-152 peptidase D Homo sapiens 25-44 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Proline 145-152 peptidase D Homo sapiens 48-59 23212918-1 2013 Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus. Proline 145-152 peptidase D Homo sapiens 61-65 23516557-1 2013 Prolidase is the only human enzyme responsible for the digestion of iminodipeptides containing proline or hydroxyproline at their C-terminal end, being a key player in extracellular matrix remodeling. Proline 95-102 peptidase D Homo sapiens 0-9 23553128-5 2013 Serum prolidase assay is based on a colorimetric determination of proline by Chinard"s reagent. Proline 66-73 peptidase D Homo sapiens 6-15 22512465-1 2012 Prolidase is a multifunctional enzyme that possesses the unique ability to degrade imidodipeptides in which a proline or hydroxyproline residue is located at the C-terminal end. Proline 110-117 peptidase D Homo sapiens 0-9 23430876-2 2012 Prolidase is a ubiquitous enzyme that hydrolyses dipeptides with C-terminal proline or hydroxyproline residues and indeed, lack of this enzyme activity causes massive urine excretion of undigested iminodipeptides. Proline 76-83 peptidase D Homo sapiens 0-9 22245250-6 2012 RESULTS: In addition to the expected changes in MMPs and collagen synthesis in HDEs in response to ATRA, prolidase, an important enzyme in the recycling of proline and hydroxyproline from degraded collagen molecules, was significantly decreased by UVA irradiation, and its down-regulation was antagonized by ATRA. Proline 156-163 peptidase D Homo sapiens 105-114 20383038-2 2010 Prolidase is an enzyme that catalyzes the final step of collagen breakdown by liberating free proline for collagen recycling. Proline 94-101 peptidase D Homo sapiens 0-9 20674353-2 2010 Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently. Proline 0-7 peptidase D Homo sapiens 73-82 20674353-2 2010 Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently. Proline 140-147 peptidase D Homo sapiens 73-82 21254236-2 2011 Prolidase has an important role in the recycling of proline for collagen synthesis and cell growth. Proline 52-59 peptidase D Homo sapiens 0-9 19834130-1 2010 Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays a major role in collagen turnover. Proline 89-96 peptidase D Homo sapiens 0-9 19695763-1 2009 OBJECTIVE: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with C-terminal proline and hydroxyproline and plays a major role in collagen turnover. Proline 94-101 peptidase D Homo sapiens 11-20 19288447-2 2009 The enzyme prolidase plays an important role in the breakdown of collagen and the breakdown of intracellular protein especially in the final stage when peptides and dipeptides contain a high level of proline. Proline 200-207 peptidase D Homo sapiens 11-20 18806116-5 2008 Proline as substrate is stored as collagen in extracellular matrix, connective tissue, and bone and it is rapidly released from this reservoir by the sequential action of matrix metalloproteinases, peptidases, and prolidase. Proline 0-7 peptidase D Homo sapiens 214-223 18806117-16 2008 Prolidase catalyzes hydrolysis of dipeptide or oligopeptide with a C-terminal proline or hydroxyproline and its deficiency can cause mental retardation and severe skin ulcers. Proline 78-85 peptidase D Homo sapiens 0-9 18607169-1 2008 OBJECTIVES: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays major role in collagen turnover. Proline 101-108 peptidase D Homo sapiens 12-21 18320291-1 2008 Prolidase [EC.3.4.13.9] is a cytosolic imidodipeptidase, which specifically splits imidodipeptides with C-terminal proline or hydroxyproline. Proline 115-122 peptidase D Homo sapiens 0-9 18340504-0 2008 Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations. Proline 104-111 peptidase D Homo sapiens 6-15 18340504-2 2008 Among the peptidases, prolidase is the only metalloenzyme that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end. Proline 104-111 peptidase D Homo sapiens 22-31 18157855-5 2008 Overexpression of prolidase in some neoplastic cells suggests that the proline analogue of alkylating agents may serve as a prolidase convertible prodrugs. Proline 71-78 peptidase D Homo sapiens 18-27 18157855-5 2008 Overexpression of prolidase in some neoplastic cells suggests that the proline analogue of alkylating agents may serve as a prolidase convertible prodrugs. Proline 71-78 peptidase D Homo sapiens 124-133 17377743-0 2007 Proline prodrug of melphalan targeted to prolidase, a prodrug activating enzyme overexpressed in melanoma. Proline 0-7 peptidase D Homo sapiens 41-50 17377743-1 2007 PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan. Proline 73-80 peptidase D Homo sapiens 54-63 17377743-1 2007 PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan. Proline 73-80 peptidase D Homo sapiens 142-151 17377743-1 2007 PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan. Proline 73-80 peptidase D Homo sapiens 142-151