PLA2G7
From Wikipedia, the free encyclopedia
Phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)
|
||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | PLA2G7; PAFAH; LDL-PLA2 | |||||||||||||
External IDs | OMIM: 601690 MGI: 1351327 HomoloGene: 3725 | |||||||||||||
|
||||||||||||||
RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 7941 | 27226 | ||||||||||||
Ensembl | ENSG00000146070 | ENSMUSG00000023913 | ||||||||||||
Uniprot | Q13093 | Q3U1V7 | ||||||||||||
Refseq | NM_005084 (mRNA) NP_005075 (protein) |
XM_001003905 (mRNA) XP_001003905 (protein) |
||||||||||||
Location | Chr 6: 46.78 - 46.81 Mb | Chr 17: 43.03 - 43.08 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma), also known as PLA2G7, is a human gene.[1]
The PLA2G7 gene encodes platelet-activating factor (PAF) acetylhydrolase (EC 3.1.1.47), a secreted enzyme that catalyzes the degradation of PAF to inactive products by hydrolysis of the acetyl group at the sn-2 position, producing the biologically inactive products LYSO-PAF and acetate.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Schröder HC, Perovic S, Kavsan V, et al. (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death.". Neurotoxicology 19 (4-5): 683–8. PMID 9745929.
- Feng Y, Walsh CA (2001). "Protein-protein interactions, cytoskeletal regulation and neuronal migration.". Nat. Rev. Neurosci. 2 (6): 408–16. doi: . PMID 11389474.
- Tjoelker LW, Eberhardt C, Unger J, et al. (1995). "Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad.". J. Biol. Chem. 270 (43): 25481–7. PMID 7592717.
- Tjoelker LW, Wilder C, Eberhardt C, et al. (1995). "Anti-inflammatory properties of a platelet-activating factor acetylhydrolase.". Nature 374 (6522): 549–53. doi: . PMID 7700381.
- Tew DG, Southan C, Rice SQ, et al. (1996). "Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins.". Arterioscler. Thromb. Vasc. Biol. 16 (4): 591–9. PMID 8624782.
- Stafforini DM, Satoh K, Atkinson DL, et al. (1996). "Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase.". J. Clin. Invest. 97 (12): 2784–91. PMID 8675689.
- Yamada Y, Yokota M (1997). "Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation.". Biochem. Biophys. Res. Commun. 236 (3): 772–5. doi: . PMID 9245731.
- Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, et al. (1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes.". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 16 (1): 1–9. PMID 9377118.
- Sapir T, Elbaum M, Reiner O (1998). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit.". EMBO J. 16 (23): 6977–84. doi: . PMID 9384577.
- Hiramoto M, Yoshida H, Imaizumi T, et al. (1998). "A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke.". Stroke 28 (12): 2417–20. PMID 9412624.
- Yamada Y, Ichihara S, Fujimura T, Yokota M (1998). "Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men.". Metab. Clin. Exp. 47 (2): 177–81. PMID 9472966.
- Yoshida H, Imaizumi T, Fujimoto K, et al. (1998). "A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension.". Thromb. Haemost. 80 (3): 372–5. PMID 9759612.
- Lecointe N, Meerabux J, Ebihara M, et al. (1999). "Molecular analysis of an unstable genomic region at chromosome band 11q23 reveals a disruption of the gene encoding the alpha2 subunit of platelet-activating factor acetylhydrolase (Pafah1a2) in human lymphoma.". Oncogene 18 (18): 2852–9. doi: . PMID 10362256.
- Kruse S, Mao XQ, Heinzmann A, et al. (2000). "The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma.". Am. J. Hum. Genet. 66 (5): 1522–30. PMID 10733466.
- Howard KM, Olson MS (2000). "The expression and localization of plasma platelet-activating factor acetylhydrolase in endotoxemic rats.". J. Biol. Chem. 275 (26): 19891–6. doi: . PMID 10748027.
- Min JH, Wilder C, Aoki J, et al. (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. PMID 11294621.
- Quarck R, De Geest B, Stengel D, et al. (2001). "Adenovirus-mediated gene transfer of human platelet-activating factor-acetylhydrolase prevents injury-induced neointima formation and reduces spontaneous atherosclerosis in apolipoprotein E-deficient mice.". Circulation 103 (20): 2495–500. PMID 11369691.
- Unno N, Nakamura T, Mitsuoka H, et al. (2002). "Association of a G994 -->T missense mutation in the plasma platelet-activating factor acetylhydrolase gene with risk of abdominal aortic aneurysm in Japanese.". Ann. Surg. 235 (2): 297–302. PMID 11807372.