PLA2G5
| Phospholipase A2, group V | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbols | PLA2G5 ; DKFZp686C2294; GV-PLA2; MGC46205; PLA2-10; hVPLA(2) | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 716 | ||||||||||
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| RNA expression pattern | |||||||||||
| File:PBB GE PLA2G5 206178 at tn.png | |||||||||||
| File:PBB GE PLA2G5 215870 s at tn.png | |||||||||||
| File:PBB GE PLA2G5 gnf1h03549 s at tn.png | |||||||||||
| More reference expression data | |||||||||||
| Orthologs | |||||||||||
| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
| Ensembl | n/a | n/a | |||||||||
| UniProt | n/a | n/a | |||||||||
| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
| PubMed search | n/a | n/a | |||||||||
Phospholipase A2, group V, also known as PLA2G5, is a human gene.[1]
This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory phospholipase A2 genes on chromosome 1. The encoded enzyme catalyzes the hydrolysis of membrane phospholipids to generate lysophospholipids and free fatty acids including arachidonic acid. It preferentially hydrolyzes linoleoyl-containing phosphatidylcholine substrates. Secretion of this enzyme is thought to induce inflammatory responses in neighboring cells. Alternatively spliced transcript variants have been found, but their full-length nature has not been determined.[1]
References
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.
- Cho W (2001). "Structure, function, and regulation of group V phospholipase A(2)". Biochim. Biophys. Acta. 1488 (1–2): 48–58. PMID 11080676.
- de Beer FC, Webb NR (2006). "Inflammation and atherosclerosis: Group IIa and Group V sPLA2 are not redundant". Arterioscler. Thromb. Vasc. Biol. 26 (7): 1421–2. doi:10.1161/01.ATV.0000227561.89488.9a. PMID 16794232.
- Chen J, Engle SJ, Seilhamer JJ, Tischfield JA (1994). "Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2". J. Biol. Chem. 269 (4): 2365–8. PMID 8300559.
- Tischfield JA, Xia YR, Shih DM; et al. (1997). "Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human". Genomics. 32 (3): 328–33. doi:10.1006/geno.1996.0126. PMID 8838795.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
- 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.
- Chen Y, Dennis EA (1998). "Expression and characterization of human group V phospholipase A2". Biochim. Biophys. Acta. 1394 (1): 57–64. PMID 9767110.
- Bingham CO, Fijneman RJ, Friend DS; et al. (1999). "Low molecular weight group IIA and group V phospholipase A(2) enzymes have different intracellular locations in mouse bone marrow-derived mast cells". J. Biol. Chem. 274 (44): 31476–84. PMID 10531350.
- Johansen B, Rakkestad K, Balboa MA, Dennis EA (2000). "Expression of cytosolic and secreted forms of phospholipase A(2) and cyclooxygenases in human placenta, fetal membranes, and chorionic cell lines". Prostaglandins Other Lipid Mediat. 60 (4–6): 119–25. PMID 10751642.
- Kim KP, Han SK, Hong M, Cho W (2000). "The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2". Biochem. J. 348 Pt 3: 643–7. PMID 10839997.
- Seeds MC, Jones KA, Duncan Hite R; et al. (2000). "Cell-specific expression of group X and group V secretory phospholipases A(2) in human lung airway epithelial cells". Am. J. Respir. Cell Mol. Biol. 23 (1): 37–44. PMID 10873151.
- Bernatchez PN, Winstead MV, Dennis EA, Sirois MG (2001). "VEGF stimulation of endothelial cell PAF synthesis is mediated by group V 14 kDa secretory phospholipase A2". Br. J. Pharmacol. 134 (1): 197–205. doi:10.1038/sj.bjp.0704215. PMID 11522612.
- Degousee N, Ghomashchi F, Stefanski E; et al. (2002). "Groups IV, V, and X phospholipases A2s in human neutrophils: role in eicosanoid production and gram-negative bacterial phospholipid hydrolysis". J. Biol. Chem. 277 (7): 5061–73. doi:10.1074/jbc.M109083200. PMID 11741884.
- Kim YJ, Kim KP, Han SK; et al. (2002). "Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2". J. Biol. Chem. 277 (39): 36479–88. doi:10.1074/jbc.M205399200. PMID 12124392.
- Hichami A, Joshi B, Simonin AM, Khan NA (2003). "Role of three isoforms of phospholipase A2 in capacitative calcium influx in human T-cells". Eur. J. Biochem. 269 (22): 5557–63. PMID 12423354.
- 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. PMID 12477932.
- Muñoz NM, Kim YJ, Meliton AY; et al. (2003). "Human group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human eosinophils". J. Biol. Chem. 278 (40): 38813–20. doi:10.1074/jbc.M302476200. PMID 12796497.
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