PAFAH2
| Platelet-activating factor acetylhydrolase 2, 40kDa | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | PAFAH2 ; HSD-PLA2 | ||||||||||||
| External IDs | OMIM: 602344 MGI: 2140321 HomoloGene: 37309 ChEMBL: 4144 GeneCards: PAFAH2 Gene | ||||||||||||
| EC number | 3.1.1.47 | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 5051 | 100163 | |||||||||||
| Ensembl | ENSG00000158006 | ENSMUSG00000037366 | |||||||||||
| UniProt | Q99487 | Q8VDG7 | |||||||||||
| RefSeq (mRNA) | NM_000437 | NM_001285872 | |||||||||||
| RefSeq (protein) | NP_000428 | NP_001272801 | |||||||||||
| Location (UCSC) |
Chr 1: 25.96 – 26 Mb |
Chr 4: 134.4 – 134.43 Mb | |||||||||||
| PubMed search | |||||||||||||
Platelet-activating factor acetylhydrolase 2, cytoplasmic is an enzyme that in humans is encoded by the PAFAH2 gene.[1][2][3] It is one of several PAF acetylhydrolases.
Function
This gene encodes platelet-activating factor acetylhydrolase isoform 2, a single-subunit intracellular enzyme that catalyzes the removal of the acetyl group at the SN-2 position of platelet-activating factor (identified as 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). However, this lipase exhibits a broader substrate specificity than simply platelet activating factor. Two other isoforms of intracellular platelet-activating factor acetylhydrolase exist, and both are multi-subunit enzymes. Additionally, there is a single-subunit serum isoform of this enzyme.[3]
References
- ↑ Hattori K, Adachi H, Matsuzawa A, Yamamoto K, Tsujimoto M, Aoki J, Hattori M, Arai H, Inoue K (Dec 1996). "cDNA cloning and expression of intracellular platelet-activating factor (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase". The Journal of Biological Chemistry 271 (51): 33032–8. doi:10.1074/jbc.271.51.33032. PMID 8955149.
- ↑ Rice SQ, Southan C, Boyd HF, Terrett JA, MacPhee CH, Moores K, Gloger IS, Tew DG (Mar 1998). "Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor". The Biochemical Journal. 330 ( Pt 3) (3): 1309–15. PMC 1219277. PMID 9494101.
- 1 2 "Entrez Gene: PAFAH2 platelet-activating factor acetylhydrolase 2, 40kDa".
Further reading
- Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM (Jul 1997). "Platelet-activating factor acetylhydrolases". The Journal of Biological Chemistry 272 (29): 17895–8. doi:10.1074/jbc.272.29.17895. PMID 9218411.
- Umemura K, Kato I, Hirashima Y, Ishii Y, Inoue T, Aoki J, Kono N, Oya T, Hayashi N, Hamada H, Endo S, Oda M, Arai H, Kinouchi H, Hiraga K (Mar 2007). "Neuroprotective role of transgenic PAF-acetylhydrolase II in mouse models of focal cerebral ischemia". Stroke; A Journal of Cerebral Circulation 38 (3): 1063–8. doi:10.1161/01.STR.0000257981.09329.d2. PMID 17272759.
- Schmidt EB, Koenig W, Khuseyinova N, Christensen JH (Jan 2008). "Lipoprotein-associated phospholipase A2 concentrations in plasma are associated with the extent of coronary artery disease and correlate to adipose tissue levels of marine n-3 fatty acids". Atherosclerosis 196 (1): 420–4. doi:10.1016/j.atherosclerosis.2006.11.027. PMID 17157859.
- Unno N, Sakaguchi T, Nakamura T, Yamamoto N, Sugatani J, Miwa M, Konno H (Jul 2006). "A single nucleotide polymorphism in the plasma PAF acetylhydrolase gene and risk of atherosclerosis in Japanese patients with peripheral artery occlusive disease". The Journal of Surgical Research 134 (1): 36–43. doi:10.1016/j.jss.2006.02.058. PMID 16650870.
- Marques M, Pei Y, Southall MD, Johnston JM, Arai H, Aoki J, Inoue T, Seltmann H, Zouboulis CC, Travers JB (Oct 2002). "Identification of platelet-activating factor acetylhydrolase II in human skin". The Journal of Investigative Dermatology 119 (4): 913–9. doi:10.1046/j.1523-1747.2002.01859.x. PMID 12406338.
- Min JH, Wilder C, Aoki J, Arai H, Inoue K, Paul L, Gelb MH (Apr 2001). "Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme". Biochemistry 40 (15): 4539–49. doi:10.1021/bi002600g. PMID 11294621.
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