PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8370712-1 1993 The widespread tissue distribution of prostaglandin dehydrogenase (PGDH), the main enzyme for the metabolism and deactivation of prostaglandin (PG), suggests that local effective levels of PG are controlled by catabolism. Prostaglandins 38-51 15-hydroxyprostaglandin dehydrogenase Homo sapiens 67-71 8086429-1 1994 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the first step in the catabolic pathway of the prostaglandins. Prostaglandins 122-136 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 8086429-1 1994 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the first step in the catabolic pathway of the prostaglandins. Prostaglandins 122-136 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 8370712-1 1993 The widespread tissue distribution of prostaglandin dehydrogenase (PGDH), the main enzyme for the metabolism and deactivation of prostaglandin (PG), suggests that local effective levels of PG are controlled by catabolism. Prostaglandins 67-69 15-hydroxyprostaglandin dehydrogenase Homo sapiens 38-65 8370712-1 1993 The widespread tissue distribution of prostaglandin dehydrogenase (PGDH), the main enzyme for the metabolism and deactivation of prostaglandin (PG), suggests that local effective levels of PG are controlled by catabolism. Prostaglandins 144-146 15-hydroxyprostaglandin dehydrogenase Homo sapiens 38-65 8370712-1 1993 The widespread tissue distribution of prostaglandin dehydrogenase (PGDH), the main enzyme for the metabolism and deactivation of prostaglandin (PG), suggests that local effective levels of PG are controlled by catabolism. Prostaglandins 144-146 15-hydroxyprostaglandin dehydrogenase Homo sapiens 67-71 8370712-7 1993 These findings show that PG stimulation by antiprogestin is by means of a direct effect on PGDH, and secondly, that the prominent rise in PGE in blood vessels may be a major mode of action of this steroid in causing abortion, as PGs may synergize with leukocyte chemotactic agents to stimulate neutrophil ingress and tissue destruction. Prostaglandins 25-27 15-hydroxyprostaglandin dehydrogenase Homo sapiens 91-95 1641503-1 1992 Human tissues contain two enzymes that catalyze the oxidation of the 15-hydroxy group of prostaglandins: NAD-dependent 15-hydroxyprostaglandin dehydrogenase which is fairly specific for prostaglandins and NADP-dependent 15-hydroxyprostaglandin dehydrogenase with low specificity for prostaglandins. Prostaglandins 89-103 15-hydroxyprostaglandin dehydrogenase Homo sapiens 105-156 8508808-1 1993 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase catalyzes the first step in the metabolism of prostaglandins which is usually associated with physiological inactivation. Prostaglandins 101-115 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 1508955-1 1992 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is a key enzyme involved in the catabolism of the prostaglandins. Prostaglandins 115-129 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 1641503-1 1992 Human tissues contain two enzymes that catalyze the oxidation of the 15-hydroxy group of prostaglandins: NAD-dependent 15-hydroxyprostaglandin dehydrogenase which is fairly specific for prostaglandins and NADP-dependent 15-hydroxyprostaglandin dehydrogenase with low specificity for prostaglandins. Prostaglandins 186-200 15-hydroxyprostaglandin dehydrogenase Homo sapiens 105-156 1641503-1 1992 Human tissues contain two enzymes that catalyze the oxidation of the 15-hydroxy group of prostaglandins: NAD-dependent 15-hydroxyprostaglandin dehydrogenase which is fairly specific for prostaglandins and NADP-dependent 15-hydroxyprostaglandin dehydrogenase with low specificity for prostaglandins. Prostaglandins 186-200 15-hydroxyprostaglandin dehydrogenase Homo sapiens 105-156 1953649-1 1991 Human promyelocytic leukaemia (HL-60) cells were employed to study the induction of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), the key enzyme in controlling prostaglandin inactivation. Prostaglandins 111-124 15-hydroxyprostaglandin dehydrogenase Homo sapiens 140-147 1612526-5 1992 We speculate that PGDH is ideally localized to metabolize and to maintain low concentrations of primary prostaglandins in the fetal membranes for much of gestation. Prostaglandins 104-118 15-hydroxyprostaglandin dehydrogenase Homo sapiens 18-22 34429873-6 2021 Additionally, high expression of the hydroxyprostaglandin dehydrogenase gene, HPGD encoding prostaglandin-degrading enzyme 15-hydroxyprostaglandin dehydrogenase (15-PGDH) and low expression of the proteoglycan 2 gene, PRG2 encoding constituent of the eosinophil granule in sputum cells might serve as a predictor of good response to aspirin therapy. Prostaglandins 92-105 15-hydroxyprostaglandin dehydrogenase Homo sapiens 78-82 2025296-1 1991 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is a key enzyme involved in the biological inactivation of the prostaglandins. Prostaglandins 128-142 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 2025296-1 1991 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is a key enzyme involved in the biological inactivation of the prostaglandins. Prostaglandins 128-142 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 1697582-1 1990 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase catalyzes the oxidation of many prostaglandins at C-15, resulting in a subsequent reduction in their biological activity. Prostaglandins 87-101 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 34507099-6 2021 The bicyclo(3.3.0)octane scaffold, found in natural products and in anticancer compounds, are expected to keep their activity in PG analogs; the bulky scaffold, separated by a methylene group from the C-15 carbon atom, is expected to diminish the inactivation of the PG analog by enzyme oxidation of 15alpha-OH oxidation to 15-Keto via PGDH pathway. Prostaglandins 267-269 15-hydroxyprostaglandin dehydrogenase Homo sapiens 336-340 3662534-1 1987 The oxidation of the 15-hydroxy group of prostaglandins of the A, E, and F series by the NAD+-dependent prostaglandin dehydrogenase (PGDH) has been well documented. Prostaglandins 41-55 15-hydroxyprostaglandin dehydrogenase Homo sapiens 104-131 34202639-2 2021 The bulky pentalenofurane skeleton is expected to introduce more hindrance in the prostaglandin analogues of type III, greater than that obtained with the bicyclo(3.3.0)oct(a)ene fragments of prostaglandin analogues I and II, to slow down (retard) the inactivation of the prostaglandin analogues by oxidation of 15alpha-OH to the 15-keto group via the 15-PGDH pathway. Prostaglandins 82-95 15-hydroxyprostaglandin dehydrogenase Homo sapiens 352-359 34202639-2 2021 The bulky pentalenofurane skeleton is expected to introduce more hindrance in the prostaglandin analogues of type III, greater than that obtained with the bicyclo(3.3.0)oct(a)ene fragments of prostaglandin analogues I and II, to slow down (retard) the inactivation of the prostaglandin analogues by oxidation of 15alpha-OH to the 15-keto group via the 15-PGDH pathway. Prostaglandins 192-205 15-hydroxyprostaglandin dehydrogenase Homo sapiens 352-359 34202639-2 2021 The bulky pentalenofurane skeleton is expected to introduce more hindrance in the prostaglandin analogues of type III, greater than that obtained with the bicyclo(3.3.0)oct(a)ene fragments of prostaglandin analogues I and II, to slow down (retard) the inactivation of the prostaglandin analogues by oxidation of 15alpha-OH to the 15-keto group via the 15-PGDH pathway. Prostaglandins 272-285 15-hydroxyprostaglandin dehydrogenase Homo sapiens 352-359 3662534-7 1987 These data indicate that omega 6-hydroxy fatty acids, in addition to prostaglandins, are also substrates of the lung NAD+-dependent PGDH and that the enzyme does not require the cyclopentane ring of prostaglandins. Prostaglandins 69-83 15-hydroxyprostaglandin dehydrogenase Homo sapiens 132-136 3662534-7 1987 These data indicate that omega 6-hydroxy fatty acids, in addition to prostaglandins, are also substrates of the lung NAD+-dependent PGDH and that the enzyme does not require the cyclopentane ring of prostaglandins. Prostaglandins 199-213 15-hydroxyprostaglandin dehydrogenase Homo sapiens 132-136 3662534-1 1987 The oxidation of the 15-hydroxy group of prostaglandins of the A, E, and F series by the NAD+-dependent prostaglandin dehydrogenase (PGDH) has been well documented. Prostaglandins 41-55 15-hydroxyprostaglandin dehydrogenase Homo sapiens 133-137 3662534-2 1987 In addition to prostaglandins, we have observed that the purified lung PGDH also will oxidize 15-HETE to a novel metabolite that was isolated by reverse-phase HPLC and identified by gas chromatography-mass spectrometry as the 15-keto-5,8,11-cis-13-trans-eicosatetraenoic acid (15-KETE). Prostaglandins 15-29 15-hydroxyprostaglandin dehydrogenase Homo sapiens 71-75 32884353-3 2020 The enzyme 15-PGDH, which plays a key role in prostaglandin degradation, is a critical inflammatory mediator in gastric cancer (GC) tumorigenesis. Prostaglandins 46-59 15-hydroxyprostaglandin dehydrogenase Homo sapiens 11-18 3120517-1 1987 A number of prostaglandins and mono-hydroxylated fatty acids were investigated as substrates for NAD-dependent 15-prostaglandin dehydrogenase (15-PGDH) obtained from human HL-60 cells. Prostaglandins 12-26 15-hydroxyprostaglandin dehydrogenase Homo sapiens 143-150 3479888-5 1987 Thus, HL-60 cells express two enzymes of the major prostaglandin catabolic pathway, 15-PGDH and ketoprostaglandin delta 13-reductase. Prostaglandins 51-64 15-hydroxyprostaglandin dehydrogenase Homo sapiens 84-91 3878384-1 1985 The high activity of 15-hydroxyprostaglandin dehydrogenase (PGDH) which catalyzes the first step in prostaglandin metabolism has been demonstrated in the human placenta. Prostaglandins 31-44 15-hydroxyprostaglandin dehydrogenase Homo sapiens 60-64 6499716-8 1984 Such an evaluation of the regulation of PGDH is believed to be of importance since PGDH serves to regulate the levels of and, thence, the action of the biologically active prostaglandins. Prostaglandins 172-186 15-hydroxyprostaglandin dehydrogenase Homo sapiens 40-44 6499716-8 1984 Such an evaluation of the regulation of PGDH is believed to be of importance since PGDH serves to regulate the levels of and, thence, the action of the biologically active prostaglandins. Prostaglandins 172-186 15-hydroxyprostaglandin dehydrogenase Homo sapiens 83-87 29204966-2 2017 It is well known to play a key role in the metabolic clearance of prostaglandins, which are taken up into the cell by OATP2A1 and then oxidatively inactivated by 15-ketoprostaglandin dehydrogenase (encoded by HPGD); indeed, OATP2A1-mediated uptake is the rate-limiting step of PGE2 catabolism. Prostaglandins 66-80 15-hydroxyprostaglandin dehydrogenase Homo sapiens 209-213 30248390-4 2018 RESULTS: Prostaglandin synthases and two enzymes involved in prostaglandin degradation, hydroxyprostaglandin dehydrogenase (HPGD) and CBR1, were detected by the mass spectrometer. Prostaglandins 61-74 15-hydroxyprostaglandin dehydrogenase Homo sapiens 88-122 30248390-4 2018 RESULTS: Prostaglandin synthases and two enzymes involved in prostaglandin degradation, hydroxyprostaglandin dehydrogenase (HPGD) and CBR1, were detected by the mass spectrometer. Prostaglandins 61-74 15-hydroxyprostaglandin dehydrogenase Homo sapiens 124-128 29249255-1 2018 Chorionic NAD-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH) plays a pivotal role in controlling the amount of prostaglandins in the uterus and has been implicated in the process of labor. Prostaglandins 119-133 15-hydroxyprostaglandin dehydrogenase Homo sapiens 63-67 28916395-2 2017 To date, two genes involved in prostaglandin metabolism, HPGD and SLCO2A1, have been identified. Prostaglandins 31-44 15-hydroxyprostaglandin dehydrogenase Homo sapiens 57-61 21735612-0 2010 Potent and selective inhibitors of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (HPGD) 15-hydroxyprostaglandin dehydrogenase (15-PGDH; HPGD) is the key enzyme for the inactivation of prostaglandins, and thus regulates processes such as inflammation or proliferation. Prostaglandins 193-207 15-hydroxyprostaglandin dehydrogenase Homo sapiens 91-95 26093984-1 2015 Chorionic NAD-dependent 15-hydroxy prostaglandin dehydrogenase (PGDH) plays a pivotal role in controlling the amount of prostaglandins in the uterus. Prostaglandins 120-134 15-hydroxyprostaglandin dehydrogenase Homo sapiens 35-62 26093984-1 2015 Chorionic NAD-dependent 15-hydroxy prostaglandin dehydrogenase (PGDH) plays a pivotal role in controlling the amount of prostaglandins in the uterus. Prostaglandins 120-134 15-hydroxyprostaglandin dehydrogenase Homo sapiens 64-68 22197745-4 2012 Using two dimensional gel electrophoresis and western blot analyses with monoclonal and polyclonal antibodies we identified 15-hydroxy prostaglandin dehydrogenase (PGDH), a major prostaglandin catabolizing enzyme, as a target for nitration in LAD2. Prostaglandins 135-148 15-hydroxyprostaglandin dehydrogenase Homo sapiens 164-168 28479736-1 2017 BACKGROUND: Prostaglandins (PGs) have short existence in vivo because they are rapidly metabolized by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to 15-ketoprostaglandins. Prostaglandins 12-26 15-hydroxyprostaglandin dehydrogenase Homo sapiens 102-154 28479736-1 2017 BACKGROUND: Prostaglandins (PGs) have short existence in vivo because they are rapidly metabolized by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to 15-ketoprostaglandins. Prostaglandins 12-26 15-hydroxyprostaglandin dehydrogenase Homo sapiens 156-163 28479736-1 2017 BACKGROUND: Prostaglandins (PGs) have short existence in vivo because they are rapidly metabolized by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to 15-ketoprostaglandins. Prostaglandins 28-31 15-hydroxyprostaglandin dehydrogenase Homo sapiens 102-154 28479736-1 2017 BACKGROUND: Prostaglandins (PGs) have short existence in vivo because they are rapidly metabolized by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to 15-ketoprostaglandins. Prostaglandins 28-31 15-hydroxyprostaglandin dehydrogenase Homo sapiens 156-163 25834895-1 2010 These prostaglandins are involved in a number of processes, including inflammation, differentiation, and cellular signaling, which makes HPGD an important target for pharmacological intervention. Prostaglandins 6-20 15-hydroxyprostaglandin dehydrogenase Homo sapiens 137-141 23506845-1 2013 The chorion laeve controls the levels of active prostaglandins within the uterus by NAD-dependent 15-hydroxy prostaglandin dehydrogenase (PGDH). Prostaglandins 48-62 15-hydroxyprostaglandin dehydrogenase Homo sapiens 109-136 23506845-1 2013 The chorion laeve controls the levels of active prostaglandins within the uterus by NAD-dependent 15-hydroxy prostaglandin dehydrogenase (PGDH). Prostaglandins 48-62 15-hydroxyprostaglandin dehydrogenase Homo sapiens 138-142 21735612-0 2010 Potent and selective inhibitors of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (HPGD) 15-hydroxyprostaglandin dehydrogenase (15-PGDH; HPGD) is the key enzyme for the inactivation of prostaglandins, and thus regulates processes such as inflammation or proliferation. Prostaglandins 193-207 15-hydroxyprostaglandin dehydrogenase Homo sapiens 145-149 20643784-5 2010 15-Hydroxyprostaglandin deyhdrogenase (15-PGDH), a tumor suppressor gene, plays a major role in PG catabolism. Prostaglandins 42-44 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-37 20699658-2 2010 Recently, 15-hydroxyprostaglandin dehydrogenase [NAD+] (15-PGDH), the key enzyme in prostaglandin degradation, was found to be down-regulated in human gastric cancer tissues, but little is known about its role in gastric tumorigenesis. Prostaglandins 20-33 15-hydroxyprostaglandin dehydrogenase Homo sapiens 59-63 21167905-1 2011 The ovulatory gonadotropin surge increases granulosa cell prostaglandin synthesis as well as prostaglandin dehydrogenase (PGDH), the key enzyme responsible for prostaglandin metabolism. Prostaglandins 93-106 15-hydroxyprostaglandin dehydrogenase Homo sapiens 122-126 21167905-8 2011 Increased, then decreased PGDH activity may delay accumulation of prostaglandins in the follicle until late in the periovulatory interval, contributing to timely ovulation in primates. Prostaglandins 66-80 15-hydroxyprostaglandin dehydrogenase Homo sapiens 26-30 18593902-4 2008 15-PGDH is a critical metabolic enzyme of proliferative prostaglandins, an antagonist to cyclooxygenase-2 and a tumor suppressor in colon cancer. Prostaglandins 56-70 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-7 20156557-5 2010 Calcitriol suppresses COX-2 expression and increases that of 15-PGDH thereby reducing the levels and biological activity of prostaglandins (PGs). Prostaglandins 124-138 15-hydroxyprostaglandin dehydrogenase Homo sapiens 61-68 20156557-5 2010 Calcitriol suppresses COX-2 expression and increases that of 15-PGDH thereby reducing the levels and biological activity of prostaglandins (PGs). Prostaglandins 140-143 15-hydroxyprostaglandin dehydrogenase Homo sapiens 61-68 20592360-7 2010 CONCLUSION: The inverse correlation between VDR and both COX-2 and 15-PGDH, as well as between PGE(2) and 25(OH)(2)D(3) levels, suggests a possible link between VDR-associated target genes and prostaglandin metabolism. Prostaglandins 193-206 15-hydroxyprostaglandin dehydrogenase Homo sapiens 67-74 19667156-0 2009 Expression of prostaglandin metabolising enzymes COX-2 and 15-PGDH and VDR in human granulosa cells. Prostaglandins 14-27 15-hydroxyprostaglandin dehydrogenase Homo sapiens 59-66 19667156-3 2009 First references suggest a correlation between vitamin D and prostaglandin metabolism through the impact of 1,25(OH)2D3 (calcitriol) on the expression of COX-2 and 15-PGDH. Prostaglandins 61-74 15-hydroxyprostaglandin dehydrogenase Homo sapiens 164-171 20122835-1 2010 Prostaglandins have a short life in vivo because they are metabolized rapidly by oxidation to 15-ketoprostaglandins catalyzed by a cytosolic enzyme known as NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH). Prostaglandins 0-14 15-hydroxyprostaglandin dehydrogenase Homo sapiens 157-211 20122835-1 2010 Prostaglandins have a short life in vivo because they are metabolized rapidly by oxidation to 15-ketoprostaglandins catalyzed by a cytosolic enzyme known as NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH). Prostaglandins 0-14 15-hydroxyprostaglandin dehydrogenase Homo sapiens 213-220 18639206-2 2008 Prostaglandin output is regulated by the synthetic and metabolic enzymes, prostaglandin synthase type 2 (PTGS2) and 15-hydroxyprostaglandin dehydrogenase (PGDH). Prostaglandins 0-13 15-hydroxyprostaglandin dehydrogenase Homo sapiens 155-159 18639206-11 2008 Calcium influx regulates PTGS2 and PGDH expression, thereby promoting coordinated increased prostaglandin output in circumstances such as term and preterm labor. Prostaglandins 92-105 15-hydroxyprostaglandin dehydrogenase Homo sapiens 35-39 18328086-1 2008 NAD(+) dependent 15-hydroxyprostaglandin dehydrogenate (15-PGDH) catalyses oxidation of 15(S)-hydroxyl group of prostaglandins and as a result inactivates their physiological potential. Prostaglandins 112-126 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 18328086-3 2008 In the present study, we showed that 15-PGDH was expressed in human hair follicle mainly in melanocytes and keratinocytes, which brought us to consider this enzyme as a possible target to sustain local prostaglandin production. Prostaglandins 202-215 15-hydroxyprostaglandin dehydrogenase Homo sapiens 37-44 18328086-6 2008 In the context of recent interest in prostaglandins and prostaglandin analogues as hair regrowth agents, we postulated that the use of selected 15-PGDH inhibitors could reinforce or prolong the effect of these physiological mediators on hair and skin. Prostaglandins 37-51 15-hydroxyprostaglandin dehydrogenase Homo sapiens 144-151 18328086-6 2008 In the context of recent interest in prostaglandins and prostaglandin analogues as hair regrowth agents, we postulated that the use of selected 15-PGDH inhibitors could reinforce or prolong the effect of these physiological mediators on hair and skin. Prostaglandins 37-50 15-hydroxyprostaglandin dehydrogenase Homo sapiens 144-151 16164015-5 2005 IL-10 induced the expression of prostaglandin dehydrogenase (PGDH), the major catabolic enzyme involved in prostaglandin degradation. Prostaglandins 32-45 15-hydroxyprostaglandin dehydrogenase Homo sapiens 61-65 18212353-2 2008 The enzymes responsible for PG synthesis and metabolism are prostaglandin-endoperoxide synthase 2 (PTGS2) and 15-hydroxyprostaglandin dehydrogenase (PGDH). Prostaglandins 28-30 15-hydroxyprostaglandin dehydrogenase Homo sapiens 149-153 17463062-1 2007 Throughout gestation, the chorion laeve controls the levels of biologically active prostaglandins (PGs) by its high level of nicotinamide adenine dinucleotide-dependent 15-hydroxy PG dehydrogenase (PGDH). Prostaglandins 83-97 15-hydroxyprostaglandin dehydrogenase Homo sapiens 180-196 17463062-1 2007 Throughout gestation, the chorion laeve controls the levels of biologically active prostaglandins (PGs) by its high level of nicotinamide adenine dinucleotide-dependent 15-hydroxy PG dehydrogenase (PGDH). Prostaglandins 83-97 15-hydroxyprostaglandin dehydrogenase Homo sapiens 198-202 17463062-1 2007 Throughout gestation, the chorion laeve controls the levels of biologically active prostaglandins (PGs) by its high level of nicotinamide adenine dinucleotide-dependent 15-hydroxy PG dehydrogenase (PGDH). Prostaglandins 99-102 15-hydroxyprostaglandin dehydrogenase Homo sapiens 180-196 17463062-1 2007 Throughout gestation, the chorion laeve controls the levels of biologically active prostaglandins (PGs) by its high level of nicotinamide adenine dinucleotide-dependent 15-hydroxy PG dehydrogenase (PGDH). Prostaglandins 99-102 15-hydroxyprostaglandin dehydrogenase Homo sapiens 198-202 15581601-1 2005 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a member of the short-chain dehydrogenase/reductase (SDR) family, catalyzes the first step in the catabolic pathways of prostaglandins and lipoxins, and is believed to be the key enzyme responsible for the biological inactivation of these biologically potent eicosanoids. Prostaglandins 186-200 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 18174234-5 2008 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. Prostaglandins 10-23 15-hydroxyprostaglandin dehydrogenase Homo sapiens 51-55 17636240-2 2007 15-Hydroxyprostaglandin dehydrogenase (PGDH), localized primarily to chorion trophoblasts, is the key enzyme responsible for the metabolism of prostaglandins. Prostaglandins 143-157 15-hydroxyprostaglandin dehydrogenase Homo sapiens 39-43 16828555-1 2006 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a member of the short-chain dehydrogenase/reductase (SDR) family, catalyzes the first step in the catabolic pathways of prostaglandins and lipoxins. Prostaglandins 184-198 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-52 15358636-2 2005 Using quantitative reverse transcription-polymerase chain reaction, we analyzed RNA levels of the key prostaglandin catabolic enzyme, NAD+-linked 15-hydroxyprostaglandin dehydrogenase (15-PGDH), in 19 pairs of NSCLC tumors and adjacent non-malignant tissue from the same patient. Prostaglandins 102-115 15-hydroxyprostaglandin dehydrogenase Homo sapiens 185-192 15531523-1 2004 The prostaglandin (PG)-inactivating enzyme 15-hydroxyprostaglandin dehydrogenase (PGDH) is highly expressed in the chorion leave. Prostaglandins 4-17 15-hydroxyprostaglandin dehydrogenase Homo sapiens 82-86 15531523-1 2004 The prostaglandin (PG)-inactivating enzyme 15-hydroxyprostaglandin dehydrogenase (PGDH) is highly expressed in the chorion leave. Prostaglandins 19-21 15-hydroxyprostaglandin dehydrogenase Homo sapiens 82-86 12220539-1 2002 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes NAD(+)-dependent oxidation of prostaglandins and other nonprostanoid compounds. Prostaglandins 105-119 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 12914529-1 2003 The NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH) is a catabolic enzyme that controls the biological activities of prostaglandins by converting them into inactive keto-metabolites. Prostaglandins 131-145 15-hydroxyprostaglandin dehydrogenase Homo sapiens 4-58 12914529-1 2003 The NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH) is a catabolic enzyme that controls the biological activities of prostaglandins by converting them into inactive keto-metabolites. Prostaglandins 131-145 15-hydroxyprostaglandin dehydrogenase Homo sapiens 60-64 12788907-1 2003 Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. Prostaglandins 47-61 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-27 12788907-1 2003 Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. Prostaglandins 47-61 15-hydroxyprostaglandin dehydrogenase Homo sapiens 29-33 12788907-1 2003 Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. Prostaglandins 63-66 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-27 12788907-1 2003 Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. Prostaglandins 63-66 15-hydroxyprostaglandin dehydrogenase Homo sapiens 29-33 14718596-2 2004 Ureteral obstruction is associated with increased prostanoid synthesis via cyclooxygenase induction; however, prostaglandin degradation mediated by 15-hydroxyprostaglandin dehydrogenase (PGDH) has not been evaluated in the ureter. Prostaglandins 110-123 15-hydroxyprostaglandin dehydrogenase Homo sapiens 187-191 12679466-1 2003 Prostaglandins (PGs) play a crucial role in mediating parturition events, and their synthesis and metabolism are regulated by PG H synthase and 15-hydroxy-PG dehydrogenase (PGDH), respectively. Prostaglandins 0-14 15-hydroxyprostaglandin dehydrogenase Homo sapiens 144-171 12679466-1 2003 Prostaglandins (PGs) play a crucial role in mediating parturition events, and their synthesis and metabolism are regulated by PG H synthase and 15-hydroxy-PG dehydrogenase (PGDH), respectively. Prostaglandins 0-14 15-hydroxyprostaglandin dehydrogenase Homo sapiens 173-177 12679466-1 2003 Prostaglandins (PGs) play a crucial role in mediating parturition events, and their synthesis and metabolism are regulated by PG H synthase and 15-hydroxy-PG dehydrogenase (PGDH), respectively. Prostaglandins 16-19 15-hydroxyprostaglandin dehydrogenase Homo sapiens 144-171 12679466-1 2003 Prostaglandins (PGs) play a crucial role in mediating parturition events, and their synthesis and metabolism are regulated by PG H synthase and 15-hydroxy-PG dehydrogenase (PGDH), respectively. Prostaglandins 16-19 15-hydroxyprostaglandin dehydrogenase Homo sapiens 173-177 12220539-1 2002 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes NAD(+)-dependent oxidation of prostaglandins and other nonprostanoid compounds. Prostaglandins 105-119 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 12432938-1 2002 The primary catabolic pathway of prostaglandins and related eicosanoids is initiated by the oxidation of 15(S)-hydroxyl group catalyzed by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) followed by the reduction of delta13 double bond catalyzed by NADPH/NADH dependent delta13-15-ketoprostaglandin reductase (13-PGR). Prostaglandins 33-47 15-hydroxyprostaglandin dehydrogenase Homo sapiens 139-191 12432938-1 2002 The primary catabolic pathway of prostaglandins and related eicosanoids is initiated by the oxidation of 15(S)-hydroxyl group catalyzed by NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) followed by the reduction of delta13 double bond catalyzed by NADPH/NADH dependent delta13-15-ketoprostaglandin reductase (13-PGR). Prostaglandins 33-47 15-hydroxyprostaglandin dehydrogenase Homo sapiens 193-200 10838159-1 2000 Pro-inflammatory prostaglandins are known to be first catabolized by NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to inactive metabolites. Prostaglandins 17-31 15-hydroxyprostaglandin dehydrogenase Homo sapiens 69-123 12144871-1 2002 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a member of the short-chain dehydrogenase family, catalyzes the first step in the catabolic pathway of the prostaglandins. Prostaglandins 173-187 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-54 12144871-1 2002 NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a member of the short-chain dehydrogenase family, catalyzes the first step in the catabolic pathway of the prostaglandins. Prostaglandins 173-187 15-hydroxyprostaglandin dehydrogenase Homo sapiens 56-63 11702189-3 2001 Prostaglandins play a key role during in vitro human fetal lung development and are synthesised by prostaglandin H synthase-1 (PGHS-1) and inactivated by 15-hydroxyprostaglandin dehydrogenase (PGDH) with formation of inactive 13,14-dihydro-15-keto-prostaglandins. Prostaglandins 0-14 15-hydroxyprostaglandin dehydrogenase Homo sapiens 193-197 11702189-7 2001 Catabolism by PGDH is a sensitive mechanism for regulating bioavailability of prostaglandins and we propose that active catabolism of prostaglandins within human fetal lung epithelium is an inhibitory mechanism retarding epithelial differentiation in utero. Prostaglandins 78-92 15-hydroxyprostaglandin dehydrogenase Homo sapiens 14-18 11702189-7 2001 Catabolism by PGDH is a sensitive mechanism for regulating bioavailability of prostaglandins and we propose that active catabolism of prostaglandins within human fetal lung epithelium is an inhibitory mechanism retarding epithelial differentiation in utero. Prostaglandins 134-148 15-hydroxyprostaglandin dehydrogenase Homo sapiens 14-18 11422365-1 2001 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the oxidation of the 15(S) hydroxyl group of prostaglandins to a 15-keto group resulting in a significant reduction of the biological activities of prostaglandins. Prostaglandins 118-132 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-52 11422365-1 2001 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the oxidation of the 15(S) hydroxyl group of prostaglandins to a 15-keto group resulting in a significant reduction of the biological activities of prostaglandins. Prostaglandins 118-132 15-hydroxyprostaglandin dehydrogenase Homo sapiens 54-61 11422365-1 2001 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the oxidation of the 15(S) hydroxyl group of prostaglandins to a 15-keto group resulting in a significant reduction of the biological activities of prostaglandins. Prostaglandins 221-235 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-52 11422365-1 2001 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the oxidation of the 15(S) hydroxyl group of prostaglandins to a 15-keto group resulting in a significant reduction of the biological activities of prostaglandins. Prostaglandins 221-235 15-hydroxyprostaglandin dehydrogenase Homo sapiens 54-61 11889207-2 2002 Therefore, the regulation of prostaglandin output by PG synthesizing (PGHS-I and PGHS-II) and metabolizing (PGDH) enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandins 29-42 15-hydroxyprostaglandin dehydrogenase Homo sapiens 108-112 11889207-2 2002 Therefore, the regulation of prostaglandin output by PG synthesizing (PGHS-I and PGHS-II) and metabolizing (PGDH) enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandins 53-55 15-hydroxyprostaglandin dehydrogenase Homo sapiens 108-112 11889207-12 2002 A decrease in PGDH protein and activity occurs in association with active labor and may contribute to the amount of bioactive PGs available to act within the human pregnant myometrium at that time. Prostaglandins 126-129 15-hydroxyprostaglandin dehydrogenase Homo sapiens 14-18 11454515-9 2001 11beta-HSD2 up-regulation may also lead to an increase in PGDH mRNA concentrations that, until term, possibly delays myometrial contractions induced by prostaglandins. Prostaglandins 152-166 15-hydroxyprostaglandin dehydrogenase Homo sapiens 58-62 10837478-2 2000 15-Hydroxyprostaglandin dehydrogenase (15-PGDH) and 15-oxoprostaglandin 13-reductase, also termed leukotriene B(4) 12-hydroxydehydrogenase (PGR/LTB(4)DH), are two enzymatic activities appreciated for their roles in the metabolism of prostaglandins and LTB(4). Prostaglandins 233-247 15-hydroxyprostaglandin dehydrogenase Homo sapiens 39-46 10838159-1 2000 Pro-inflammatory prostaglandins are known to be first catabolized by NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) to inactive metabolites. Prostaglandins 17-31 15-hydroxyprostaglandin dehydrogenase Homo sapiens 125-132 9058733-8 1997 In conclusion, we suggest that modifications in prostaglandin metabolism, induced by the expression of type-I 15-PGDH and the downregulation of cyclooxygenase 2, could be involved in monocytic differentiation. Prostaglandins 48-61 15-hydroxyprostaglandin dehydrogenase Homo sapiens 110-117 10198228-1 1999 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is the key enzyme in the inactivation pathway of prostaglandins. Prostaglandins 112-126 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-52 10198228-1 1999 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) is the key enzyme in the inactivation pathway of prostaglandins. Prostaglandins 112-126 15-hydroxyprostaglandin dehydrogenase Homo sapiens 54-61 9859867-5 1998 Levels of prostaglandin metabolites were generally decreased following incubation with IL-1beta or LPS, which is consistent with a decrease in the activity of 15-hydroxyprostaglandin dehydrogenase (PGDH). Prostaglandins 10-23 15-hydroxyprostaglandin dehydrogenase Homo sapiens 198-202 10692258-2 2000 PGs are rapidly metabolized to inactive metabolites by prostaglandin dehydrogenase (PGDH). Prostaglandins 0-3 15-hydroxyprostaglandin dehydrogenase Homo sapiens 55-82 10692258-2 2000 PGs are rapidly metabolized to inactive metabolites by prostaglandin dehydrogenase (PGDH). Prostaglandins 0-3 15-hydroxyprostaglandin dehydrogenase Homo sapiens 84-88 10692258-12 2000 The presence of PGDH at this site acts to stabilize output of primary PG from the placenta and also as a barrier preventing transfer to the fetal circulation, resulting in the separation of PG homeostasis in the fetus and mother. Prostaglandins 70-72 15-hydroxyprostaglandin dehydrogenase Homo sapiens 16-20 10343931-16 1999 If the enzyme in this region crucially determines the passage and availability of biologically active prostaglandins from amnion and chorion to underlying cervix, then pharmacologic manipulation of PGDH activity may effectively regulate PG transfer in these clinical conditions. Prostaglandins 102-116 15-hydroxyprostaglandin dehydrogenase Homo sapiens 198-202 9677008-10 1998 Recent studies have indicated that glucocorticoids may be important in regulating prostaglandin formation within the human fetal membranes by increasing expression of PGHS-2 in the amnion and decreasing PGDH activity in the chorion. Prostaglandins 82-95 15-hydroxyprostaglandin dehydrogenase Homo sapiens 203-207 9099873-1 1997 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type-I 15-PGDH) inactivates prostaglandins. Prostaglandins 82-96 15-hydroxyprostaglandin dehydrogenase Homo sapiens 0-52 9099873-1 1997 NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type-I 15-PGDH) inactivates prostaglandins. Prostaglandins 82-96 15-hydroxyprostaglandin dehydrogenase Homo sapiens 61-68 9089770-2 1997 Further, we reasoned that a specific reduction in PGDH in the fetal membranes at the lower uterine segment might occur with labour, providing a potential mechanism for local generation of primary prostaglandins (PG) that could contribute to cervical ripening. Prostaglandins 196-210 15-hydroxyprostaglandin dehydrogenase Homo sapiens 50-54 8829211-8 1996 Loss of PGDH activity removes the initial step in activating primary prostaglandins, which are then able to pass unmetabolized to the decidua and myometrium, and contribute to the stimulus to preterm birth. Prostaglandins 69-83 15-hydroxyprostaglandin dehydrogenase Homo sapiens 8-12 8740524-3 1996 Three prostaglandin-metabolizing enzymes induced during pregnancy are NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH), NADPH-dependent carbonyl reductase, and cytochrome P450-dependent prostaglandin omega- or 20-hydroxylase. Prostaglandins 6-19 15-hydroxyprostaglandin dehydrogenase Homo sapiens 70-124 8740524-3 1996 Three prostaglandin-metabolizing enzymes induced during pregnancy are NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH), NADPH-dependent carbonyl reductase, and cytochrome P450-dependent prostaglandin omega- or 20-hydroxylase. Prostaglandins 6-19 15-hydroxyprostaglandin dehydrogenase Homo sapiens 126-130 8740524-3 1996 Three prostaglandin-metabolizing enzymes induced during pregnancy are NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (PGDH), NADPH-dependent carbonyl reductase, and cytochrome P450-dependent prostaglandin omega- or 20-hydroxylase. Prostaglandins 97-110 15-hydroxyprostaglandin dehydrogenase Homo sapiens 126-130