hydroxyprostaglandin dehydrogenase

ヒドロキシプロスタグランジン脱水素酵素、ヒドロキシプロスタグランジンデヒドロゲナーゼ

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/24 18:50:29」(JST)

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Hydroxyprostaglandin dehydrogenase 15-(NAD)
PDB rendering based on 2gdz.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2GDZ​
Identifiers
Symbols	HPGD ; 15-PGDH; PGDH; PGDH1; PHOAR1; SDR36C1
External IDs	OMIM: 601688 MGI: 108085 HomoloGene: 68095 ChEMBL: 1293255 GeneCards: HPGD Gene
EC number	1.1.1.141
Gene ontology Molecular function • catalytic activity • prostaglandin E receptor activity • 15-hydroxyprostaglandin dehydrogenase (NAD+) activity • protein homodimerization activity • NAD binding • NAD+ binding Cellular component • cytosol • basolateral plasma membrane • extracellular exosome Biological process • prostaglandin metabolic process • transforming growth factor beta receptor signaling pathway • female pregnancy • parturition • arachidonic acid metabolic process • cyclooxygenase pathway • lipoxygenase pathway • ovulation • small molecule metabolic process • negative regulation of cell cycle • oxidation-reduction process • thrombin receptor signaling pathway • ductus arteriosus closure • lipoxin metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3248	15446
Ensembl	ENSG00000164120	ENSMUSG00000031613
UniProt	P15428	Q8VCC1
RefSeq (mRNA)	NM_000860	NM_008278
RefSeq (protein)	NP_000851	NP_032304
Location (UCSC)	Chr 4: 174.49 – 174.52 Mb	Chr 8: 56.29 – 56.32 Mb
PubMed search	[1]	[2]

Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved official symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase [NAD+], is an enzyme that in humans is encoded by the HPGD gene.

In melanocytic cells HPGD gene expression may be regulated by MITF.

See alsoEdit

• Primary hypertrophic osteoathropathy

ReferencesEdit

Further readingEdit

• Erwich JJ, Keirse MJ (1992). "Placental localization of 15-hydroxy-prostaglandin dehydrogenase in early and term human pregnancy.". Placenta 13 (3): 223–9. doi:10.1016/0143-4004(92)90037-T. PMID 1635910. 
• Ensor CM, Yang JY, Okita RT, Tai HH (1990). "Cloning and sequence analysis of the cDNA for human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase.". J. Biol. Chem. 265 (25): 14888–91. PMID 1697582. 
• Ensor CM, Tai HH (1991). "Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme.". Biochem. Biophys. Res. Commun. 176 (2): 840–5. doi:10.1016/S0006-291X(05)80262-1. PMID 2025296. 
• Krook M, Marekov L, Jörnvall H (1990). "Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family.". Biochemistry 29 (3): 738–43. doi:10.1021/bi00455a021. PMID 2337593. 
• Pichaud F, Frendo JL, Delage-Mourroux R, et al. (1995). "Sequence of a novel mRNA coding for a C-terminal-truncated form of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase.". Gene 162 (2): 319–22. doi:10.1016/0378-1119(95)00319-2. PMID 7557451. 
• Sangha RK, Walton JC, Ensor CM, et al. (1994). "Immunohistochemical localization, messenger ribonucleic acid abundance, and activity of 15-hydroxyprostaglandin dehydrogenase in placenta and fetal membranes during term and preterm labor.". J. Clin. Endocrinol. Metab. 78 (4): 982–9. doi:10.1210/jc.78.4.982. PMID 8157731. 
• Krook M, Ghosh D, Duax W, Jörnvall H (1993). "Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase).". FEBS Lett. 322 (2): 139–42. doi:10.1016/0014-5793(93)81554-D. PMID 8482380. 
• Pichaud F, Delage-Mourroux R, Pidoux E, et al. (1997). "Chromosomal localization of the type-I 15-PGDH gene to 4q34-q35.". Hum. Genet. 99 (2): 279–81. doi:10.1007/s004390050354. PMID 9048936. 
• Delage-Mourroux R, Pichaud F, Frendo JL, et al. (1997). "Cloning and sequencing of a new 15-hydroxyprostaglandin dehydrogenase related mRNA.". Gene 188 (1): 143–8. doi:10.1016/S0378-1119(96)00800-1. PMID 9099873. 
• Patel FA, Clifton VL, Chwalisz K, Challis JR (1999). "Steroid regulation of prostaglandin dehydrogenase activity and expression in human term placenta and chorio-decidua in relation to labor.". J. Clin. Endocrinol. Metab. 84 (1): 291–9. doi:10.1210/jc.84.1.291. PMID 9920098. 
• Zhou H, Tai HH (1999). "Threonine 188 is critical for interaction with NAD+ in human NAD+-dependent 15-hydroxyprostaglandin dehydrogenase.". Biochem. Biophys. Res. Commun. 257 (2): 414–7. doi:10.1006/bbrc.1999.0356. PMID 10198228. 
• Greenland KJ, Jantke I, Jenatschke S, et al. (2000). "The human NAD+-dependent 15-hydroxyprostaglandin dehydrogenase gene promoter is controlled by Ets and activating protein-1 transcription factors and progesterone.". Endocrinology 141 (2): 581–97. doi:10.1210/en.141.2.581. PMID 10650939. 
• Conner CE, Kelly RW, Hume R (2001). "Regulation of prostaglandin availability in human fetal lung by differential localisation of prostaglandin H synthase-1 and prostaglandin dehydrogenase.". Histochem. Cell Biol. 116 (4): 313–9. doi:10.1007/s004180100323. PMID 11702189. 
• Giannoulias D, Patel FA, Holloway AC, et al. (2002). "Differential changes in 15-hydroxyprostaglandin dehydrogenase and prostaglandin H synthase (types I and II) in human pregnant myometrium.". J. Clin. Endocrinol. Metab. 87 (3): 1345–52. doi:10.1210/jc.87.3.1345. PMID 11889207. 
• Cho H, Tai HH (2003). "Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis.". Prostaglandins Leukot. Essent. Fatty Acids 66 (5-6): 505–9. doi:10.1054/plef.2002.0391. PMID 12144871. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Tai HH, Ensor CM, Zhou H, Yan F (2003). "Structure and function of human NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase.". Adv. Exp. Med. Biol. 507: 245–50. doi:10.1007/978-1-4615-0193-0_37. PMID 12664592. 
• McKeown KJ, Challis JR (2003). "Regulation of 15-hydroxy prostaglandin dehydrogenase by corticotrophin-releasing hormone through a calcium-dependent pathway in human chorion trophoblast cells.". J. Clin. Endocrinol. Metab. 88 (4): 1737–41. doi:10.1210/jc.2002-021369. PMID 12679466. 
• Patel FA, Funder JW, Challis JR (2003). "Mechanism of cortisol/progesterone antagonism in the regulation of 15-hydroxyprostaglandin dehydrogenase activity and messenger ribonucleic acid levels in human chorion and placental trophoblast cells at term.". J. Clin. Endocrinol. Metab. 88 (6): 2922–33. doi:10.1210/jc.2002-021710. PMID 12788907. 
• Nandy A, Jenatschke S, Hartung B, et al. (2004). "Genomic structure and transcriptional regulation of the human NAD+-dependent 15-hydroxyprostaglandin dehydrogenase gene.". J. Mol. Endocrinol. 31 (1): 105–21. doi:10.1677/jme.0.0310105. PMID 12914529. 

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• 細胞質型プロスタグランジンE₂合成酵素

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Related Links

• HPGD hydroxyprostaglandin dehydrogenase 15-(NAD) - Gene ...

HPGD hydroxyprostaglandin dehydrogenase 15-(NAD) Also known as: PGDH; PGDH1; PHOAR1; 15-PGDH; SDR36C1 See all available tests in GTR for this gene Go to complete Gene record for HPGD Go to Variation Viewer for ...

• HPGD hydroxyprostaglandin dehydrogenase 15-(NAD) [ (human)]

This gene encodes a member of the short-chain nonmetalloenzyme alcohol dehydrogenase protein family. The encoded enzyme is responsible for the metabolism of prostaglandins, which function in a variety of ...

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★リンクテーブル★

リンク元	「ヒドロキシプロスタグランジン脱水素酵素」「ヒドロキシプロスタグランジンデヒドロゲナーゼ」
関連記事	「dehydrogenase」「dehydrogenases」

「ヒドロキシプロスタグランジン脱水素酵素」

　　[★]

英

hydroxyprostaglandin dehydrogenase

関

ヒドロキシプロスタグランジンデヒドロゲナーゼ

「ヒドロキシプロスタグランジンデヒドロゲナーゼ」

　　[★]

英

hydroxyprostaglandin dehydrogenase

関

ヒドロキシプロスタグランジン脱水素酵素

「dehydrogenase」

　　[★] 脱水素酵素 デヒドロゲナーゼ

「dehydrogenases」

　　[★] 脱水素酵素 デヒドロゲナーゼ