Accepted name: 15-hydroxyprostaglandin dehydrogenase (NAD+). Reaction: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11α-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+. Other name(s): NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD). Systematic name: (5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase. Comments: Acts on prostaglandin E2, F2α and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9030-87-9. References:. 1. Änggård, E. and Samuelsson, ...
BACKGROUND: 15-Hydroxyprostaglandin dehydrogenase (15-PGDH, EC 1.1.1.141) is the key enzyme for the inactivation of prostaglandins, regulating processes such as inflammation or proliferation. The anabolic pathways of prostaglandins, especially with respect to regulation of the cyclooxygenase (COX) enzymes have been studied in detail; however, little is known about downstream events including functional interaction of prostaglandin-processing and -metabolizing enzymes. High-affinity probes for 15-PGDH will, therefore, represent important tools for further studies. PRINCIPAL FINDINGS: To identify novel high-affinity inhibitors of 15-PGDH we performed a quantitative high-throughput screen (qHTS) by testing |160 thousand compounds in a concentration-response format and identified compounds that act as noncompetitive inhibitors as well as a competitive inhibitor, with nanomolar affinity. Both types of inhibitors caused strong thermal stabilization of the enzyme, with cofactor dependencies correlating with
Colitis-associated colon cancer (CAC) develops as a result of inflammation-induced epithelial transformation, which occurs in response to inflammatory cytokine-dependent downregulation of 15-hydroxyprostaglandin dehydrogenase (15-PGDH) and subsequent suppression of prostaglandin metabolism. Agents that both enhance 15-PGDH expression and suppress cyclooxygenase-2 (COX-2) production may more effectively prevent CAC. Synthetic triterpenoids are a class of small molecules that suppress COX-2 as well as inflammatory cytokine signaling. Here, we found that administration of the synthetic triterpenoid 2-cyano-3,12-dioxooleana-1,9(11)-dien-C28-methyl ester (CDDO-Me) suppresses CAC in mice. In a spontaneous, inflammation-driven intestinal neoplasia model, deletion of ...
Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4 (By similarity).
Jung, A., Schlegel, W., Jackisch, R., Friedrich, E.J., Wendel, A., Rückrich, M.F.: Hoppe-Seylers Z. Physiol. Chem., 356, 787-798 (1975)PubMedCrossRefGoogle Scholar ...
Helicobacter pylori (H. pylori) infection induces a chronic inflammatory response, which promotes gastric carcinogenesis. 15-Hydroxyprostaglandin dehydrogenase (15-PGDH) plays a key role as a tumor suppressor in gastrointestinal cancers. The aim of this study was to elucidate the role of 15-PGDH in gastric carcinogenesis associated with H. pylori. 15-PGDH expression in gastric biopsies from H. pylori-infected (n = 25) and noninfected (n = 15) subjects was analyzed by quantitative real-time PCR, Western blot analysis, and immunohistochemistry. 15-PGDH DNA methylation was evaluated by methylation-specific PCR and pyrosequencing. The expression of 15-PGDH, Snail, extracellular signal-regulated kinase (ERK)1/2, TLR4, and MyD88 in response to H. pylori infection was assessed by immunoblot analysis. Compared with negative specimens, H. pylori-positive specimens had 2-fold lower 15-PGDH mRNA levels and significantly less 15-PGDH protein. In four H. pylori-infected subjects with longitudinal follow-up, ...
HPGD - HPGD (Myc-DDK-tagged)-Human hydroxyprostaglandin dehydrogenase 15-(NAD) (HPGD), transcript variant 1 available for purchase from OriGene - Your Gene Company.
PRIMARY OBJECTIVES:. I. To compare the expression of 15-hydroxyprostaglandin dehydrogenase (PGDH) messenger ribonucleic acid (mRNA) and protein levels in tumor tissue at baseline and after treatment with 25-hydroxy (OH)-vitamin D3 (cholecalciferol).. II. To compare the expression of 15-PGDH mRNA and protein levels in normal colorectal mucosa at baseline and following treatment with 25-OH-vitamin D3.. SECONDARY OBJECTIVES:. I. To compare the expression of cyclooxygenase (COX)-1 and COX-2 mRNA in tumor tissues at baseline and after treatment with 25-OH-vitamin D3.. II. To compare levels of prostaglandin E2 (PGE2) in tumor tissue at baseline and after treatment with 25-OH-vitamin D3.. III. To compare the expression of COX-1 and COX-2 mRNA in normal colorectal mucosa at baseline and after treatment with 25-OH-vitamin D3.. IV. To compare levels of PGE2 in normal colorectal mucosa at baseline and after treatment with 25-OH-vitamin D3.. V. To evaluate the tolerability of a single 100,000 international ...
To explore the proteins regulated by cyclooxygenase-2 (COX-2) in gastric cancer, the expression plasmid of COX-2siRNA was constructed and transfected into gastric cancer cell line SGC7901. Then, two-dimensional electrophoresis and the PDQuest software analysis were applied to discover the differentially expressed proteins. The differential protein spots were analyzed by matrix-assisted laser desorption/ionization time of flight mass spectrometry. Fourteen differentially expressed proteins between the two cell lines were identified. 15-Hydroxyprostaglandin dehydrogenase [NAD+] (15-PGDH), a key enzyme in prostaglandin degradation, was identified as an upregulated protein in SGC7901 cells transfected with the COX-2siRNA plasmid. To further explore whether the 15-PGDH is regulated by COX-2, western blotting and immunocytochemical assay were performed to detect the expression of 15-PGDH in different cell lines with different expression level of COX-2. The results showed that the expression of 15-PGDH ...
CBR1_HUMAN RecName: Full=Carbonyl reductase [NADPH] 1; AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)]; AltName: Full=NADPH-dependent carbonyl reductase 1; AltName: Full=Prostaglandin 9-ketoreductase; AltName: Full=Prostaglandin-E(2) 9-reductase ...
28-day run-in phase during which subjects are treated with a proton pump inhibitor (omeprazole 20 mg po q day or an equivalent dose of another proton pump inhibitor). The purpose of the run-in phase is to minimize esophagitis, which can cause histologic changes that can be confused with dysplasia. After the run-in phase, subjects will undergo an upper endoscopy for Barretts surveillance or Barretts mapping as part of routine clinical care. At the time of endoscopy, research biopsies will be obtained for the study. Subjects eligible and continuing in the study will take vitamin D3 (Cholecalciferol) 50,000 IU capsules once weekly with or without daily metformin for a total of two or twelve weeks depending on the severity of Barretts esophagus. After completion of vitamin D3 subjects will return for an EGD (endoscopy) and biopsies for the research study ...
Colorectal cancer (CRC) is the third most common malignant tumor and the fourth leading cause of cancer death worldwide. The crucial role of fatty acids for a number of important biological processes suggests a more in-depth analysis of inter-individual differences in fatty acid metabolizing genes as contributing factor to colon carcinogenesis. We examined the association between genetic variability in 43 fatty acid metabolism-related genes and colorectal risk in 1225 CRC cases and 2032 controls participating in the European Prospective Investigation into Cancer and Nutrition study. Three hundred and ninety two single-nucleotide polymorphisms were selected using pairwise tagging with an r2 cutoff of 0.8 and a minor allele frequency of ,5%. Conditional logistic regression models were used to estimate odds ratios and corresponding 95% confidence intervals. Haplotype analysis was performed using a generalized linear model framework. On the genotype level, hydroxyprostaglandin dehydrogenase 15-(NAD) ...
Elevated levels of prostaglandins (PGs) have been detected in skin following ultraviolet radiation (UVR). Prostaglandins play an important role in mediating both the acute and chronic consequences of UVR exposure. UVR-mediated induction of cyclooxygenase-2 (COX-2) contributes to increased PG synthesis. In theory, reduced catabolism might also contribute to increased PG levels. 15-hydroxyprostaglandin deyhdrogenase (15-PGDH), a tumor suppressor gene, plays a major role in PG catabolism. In this study, we investigated whether UVR exposure suppressed 15-PGDH while inducing COX-2 in keratinocytes and in human skin. UVR exposure caused dose-dependent induction of COX-2, suppression of 15-PGDH and increased PGE2 production in HaCaT cells. Exposure to UVR suppressed the transcription of 15-PGDH resulting in reduced amounts of 15-PGDH mRNA, protein and enzyme activity. UVR exposure induced Slug, a repressive transcription factor that bound to the 15-PGDH promoter. Silencing Slug blocked UVR-mediated ...
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Seo KS, Naidansuren P, Kim SH, Yun SJ, Park JJ, Sim BW, Park CW, Nanjidsuren T, Kang MH, Seo H, Ka H, Kim NH, Hwang SY, Yoon JT, Yamanouchi K, Min KS; Expression of aldo-keto reductase family 1 member C1 (AKR1C1) gene in porcine ovary and uterine endometrium during the estrous cycle and pregnancy.; Reprod Biol Endocrinol, 2011 PubMed Europe PMC Scholia ...
Complete information for AKR1C4 gene (Protein Coding), Aldo-Keto Reductase Family 1 Member C4, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for AKR7A2 gene (Protein Coding), Aldo-Keto Reductase Family 7 Member A2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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PTGES2 - PTGES2 (untagged)-Human prostaglandin E synthase 2 (PTGES2), transcript variant 1 available for purchase from OriGene - Your Gene Company.
Recombinant full length protein, corresponding to amino acids 1-323 of Human AKR1C1 with an N terminal His tag. Predicted mwt: 39 kDa;
Recombinant fragment corresponding to amino acids 224-323 of Human AKR1C2, with N terminal proprietary tag; predicted MW: 36.63 kDa inclusive of tag. AAH63574.
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Aldo-keto reductase family 1, member B10 (AKR1B10), a cancer-related oxidoreductase, is expressed in well-differentiated hepatocellular carcinomas (HCCs). However, AKR1B10 levels are minimal in normal liver tissues (NLs), similar to the 70-kilodalton heat shock protein (HSP70) and glypican-3. Moreover, the role of AKR1B10 in chronic hepatitis or cirrhosis, which are considered preneoplastic conditions for HCC, has not been fully elucidated. The aim of this study was to evaluate the expression of AKR1B10, HSP70, and glypican-3 in 61 HCC tissue samples compared to corresponding non-tumorous liver tissues (NTs), comprising 42 chronic hepatitis and 19 cirrhosis cases to clarify the significance of molecular changes at the preneoplastic stages of HCC. Immunohistochemical analysis demonstrated that the median expression levels of AKR1B10 were higher in HCCs than in NTs (p < 0.001) and higher in NTs than NLs (p < 0.001) with 54.8%, 2.1%, and 0.3% expression in HCCs, NTs, and NLs, respectively. HSP70
The thiosemicarbazone derivative of 9,10-phenanthrenequinone, 1, and its metal complexes were synthesized. The X-ray crystal structure for 1 confirms the presence of the E tautomeric arrangement in this compound. Its copper complex shows 1:1 stoichiometry while nickel and cobalt compounds show 1:2 stoichiometry. The X-ray crystal structure of the nickel complex indicates two tridentate ligands coordinating in the thiolato form yielding an octahedral geometry for the mer isomer. The copper complex exhibits maximum antiproliferative activity against human breast cancer cell-line, T47D probably due to inhibition of steroid binding to the cognative receptor or by preventing dimerization of the estrogen receptor.
The activities of catalase and of glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH), the two key enzymes in the pentose phosphate pathway (ppp), were measured in the seeds of Prunus persica (L.) Batsch var. nectarina Maxim `Nectarine 7. The seeds were subjected to three imbibition treatments: 1) continuous 24C; 2) continuous 4C; and 3) application of thiourea (TU)/gibberellic acid (GA) at various concentrations to seed held at 24C then subsequently chilled at 4C. Treatments of continuous 24 or 4C indicated that catalase, G6PDH, and 6PGDH exhibited significant activity increases only when the seeds obtained germination potential, which occurred in the seeds chilled for 7 weeks at 4C. Seeds held at 24C did not germinate and showed little change with time in G6PDH and 6PGDH activity. There was only a slight increase in catalase activity beginning 3 weeks following treatment initiation and a decrease in activity following 13 weeks of treatment. Thiourea ...
In the present study, we determined the expression and localization of porcine AKR1C1 in the ovary and uterine endometrium through RT-PCR, real-time PCR, northern blotting, and immunohistochemistry during the estrous cycle and pregnancy. Analysis of the nucleotide sequence by using the GenBank database revealed that porcine AKR1C1 cDNA belongs to the AKR family. Both nucleotide and amino acid sequences of the porcine AKR1C1 cloned in this study showed high homology with those of bovine (86/82%), goat (80/78%), rat (76/66), mouse (76/68%), and human (81/76%) 20α-HSD. Based on the results of 3-RACE, we detected a stop codon in a different site from that of porcine AKR1C1 reported previously [7]. Several conserved sequence patterns were found in the porcine AKR1C1 cloned in the present study. A catalytic tetrad, such as that consisting of Asp 50, Tyr 55, Lys 84, and His 117, is a common feature of the AKR family [1]. Other amino acids such as Gly 22, Gly 45, Asp 112, Pro 119, Gly 164, Asn 167, ...
Both COX1 and COX2 (also termed prostaglandin-endoperoxide synthase-1 (PTGS1) and PTGS2, respectively) metabolize arachidonic acid by adding molecular O2 between carbons 9 and 11 to form an endoperoxide bridge between these two carbons, adding molecular O2 to carbon 15 to yield a 15-hydroperoxy product, creating a carbon-carbon bond between carbons 8 and 12 to create a cyclopentane ring in the middle of the fatty acid, and in the process making PGG2, a product that has two fewer double bonds than arachidonic acid. The 15-hydroperoxy residue of PGG2 is then reduced to a 15-hydroxyl residue thereby forming PGH2. PGH2 is the parent prostanoid to all other prostanoids. It is metabolized by (see diagram in Prostanoids: a) the Prostaglandin E synthase pathway in which any one of three isozymes, PTGES, PTGES2, or PTGES3, convert PGH2 to PGE2 (subsequent products of this pathway include PGA2 and PGB2 (see Prostanoid#Biosynthesis); b) PGF synthase which converts PGH2 to PGF2α; c) Prostaglandin D2 ...
PubMed journal article Increases in urinary 9alpha,11beta-prostaglandin f2 indicate mast cell activation in wine-induced asthm were found in PRIME PubMed. Download Prime PubMed App to iPhone or iPad.
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Prostaglandin D2 (PGD2) was recently found to be stereospecifically converted to the compound (5Z,13E)-(15S)-9 alpha,11 beta,15-trihydroxyprosta-5,13-dien-1-oic acid (9 alpha,11 beta-PGF2) by a human liver cytosolic NADPH-dependent 11-ketoreductase enzyme. Because PGD2 is a potent bronchoconstrictor …
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This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3-alpha-hydroxysteroid dehydrogenase activity. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Dec 2011 ...
Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. May play a role in myelin formation. Can oxidize both 20-alpha- and 3-alpha-hydroxysteroids.
aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III ...
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Glutathione is at present one of many most analyzed antioxidants. This is likely because of it being endogenously synthesized all all through the body and it is basically located in all cells, at times in fairly high concentrations. Investigations have highlighted several roles in which it is used which includes antioxidant protection, detoxification of electrophilic xenobiotics, modulation of redox controlled sign transduction, storage and transportation of cysteine, regulation of mobile proliferation, synthesis of deoxyribonucleotide synthesis, regulation of immune responses, and regulation of leukotriene and prostaglandin metabolism[thirteen ...
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Other lines of investigation have demonstrated that aldose reductase exhibits broad substrate specificity for both hydrophilic and hydrophobic aldehydes. Aldose reductase and the structurally related enzyme in the aldo-keto reductase family, aldehyde reductase, both catalyze the reduction of biogenic aldehydes derived from the catabolism of the catecholamines and serotonin by the action of monoamine oxidase (Turner and Tipton, 1972; Tabakoff et al., 1973;Wermuth et al., 1982). These two enzymes also catalyze the reduction of isocorticosteroids, intermediates in the catabolism of the corticosteroid hormones (Wermuth and Monder, 1983). Recently, aldose reductase in the adrenal gland was reported to be a major reductase for isocaproaldehyde, a product of sidechain cleavage of cholesterol (Matsuura et al., 1996).. Apart from these findings, molecular cloning of bovine testicular 20α-hydroxysteroid dehydrogenase cDNA incidentally revealed that the deduced amino acid sequence of the enzyme is ...
The impact of quercetin on the mRNA expression of hepatic enzymes involved in drug metabolism was evaluated with a DNA microarray and real-time PCR. Male Sprague-Dawley rats were fed an experimental d
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TY - JOUR. T1 - Levels of retinoic acid and retinaldehyde dehydrogenase expression in eyes of the Mitf-vit mouse model of retinal degeneration.. AU - Duncan, T.. AU - Swint, C.. AU - Smith, S. B.. AU - Wiggert, B. N.. PY - 1999/6/28. Y1 - 1999/6/28. N2 - PURPOSE: Several reports have characterized the retinal degeneration observed in the Mitf(vit) mutant mouse. Despite these reports, the factor(s) that may cause or modulate the degeneration still are not well defined; however, it is known that the photoreceptors of Mitf(vit) mice die through an apoptotic mechanism. We reported previously that retinoid metabolism in the RPE of Mitf(vit)++ mice is perturbed. Retinoids regulate genes via the RAR and RXR nuclear receptor pathway that are involved in numerous cellular responses including apoptosis. It is possible that retinoic acid (RA) modulates the retinal degeneration observed in the Mitf(vit) mice. The purpose of this study was to evaluate the levels of RA in whole eyes, as well as its ...
Expression of AKR1C3 (DDX, HAKRB, HSD17B5, KIAA0119, PGFS) in nasopharynx tissue. Antibody staining with CAB010874 in immunohistochemistry.
Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.[1][2] This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.[2] ...
Aldo-keto reductases (AKRs) are a class of NADPH-dependent oxidoreductases that have been linked to metabolism of the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). Although widely used, cardiotoxicity continues to be a serious side effect that may be linked to metabolites or reactive intermediates generated in their metabolism. In this study we examine the little known effects of nonsynonymous single nucleotide polymorphisms of human AKR1A1 on the metabolism of these drugs to their alcohol metabolites. Expressed and purified from bacteria using affinity chromatography, the AKR1A1 protein with a single histidine (6x-His) tag exhibited the greatest activity using two test substrates: p-nitrobenzaldehyde (5.09 ± 0.16 μmol/min/mg of purified protein) and dl-glyceraldehyde (1.24 ± 0.17 μmol/min/mg). These activities are in agreement with published literature values of nontagged human AKR1A1. The 6x-His-tagged AKR1A1 wild type and allelic variants, E55D and N52S, were subsequently ...
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