PLA2G4A

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Phospholipase A2, group IVA (cytosolic, calcium-dependent)
File:PBB Protein PLA2G4A image.jpg
PDB rendering based on 1bci.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PLA2G4A ; MGC126350; PLA2G4; cPLA2-alpha
External IDs Template:OMIM5 Template:MGI HomoloGene32059
RNA expression pattern
File:PBB GE PLA2G4A 210145 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 IVA (cytosolic, calcium-dependent), also known as PLA2G4A, is a human gene.[1]

This gene encodes a member of the cytosolic phospholipase A2 group IV family. The enzyme catalyzes the hydrolysis of membrane phospholipids to release arachidonic acid which is subsequently metabolized into eicosanoids. Eicosanoids, including prostaglandins and leukotrienes, are lipid-based cellular hormones that regulate hemodynamics, inflammatory responses, and other intracellular pathways. The hydrolysis reaction also produces lysophospholipids that are converted into platelet-activating factor. The enzyme is activated by increased intracellular Ca(2+) levels and phosphorylation, resulting in its translocation from the cytosol and nucleus to perinuclear membrane vesicles.[1]

References

  1. 1.0 1.1 "Entrez Gene: PLA2G4A phospholipase A2, group IVA (cytosolic, calcium-dependent)".

Further reading

  • Dennis EA (1994). "Diversity of group types, regulation, and function of phospholipase A2". J. Biol. Chem. 269 (18): 13057–60. PMID 8175726.
  • 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.
  • Hirabayashi T, Murayama T, Shimizu T (2005). "Regulatory mechanism and physiological role of cytosolic phospholipase A2". Biol. Pharm. Bull. 27 (8): 1168–73. PMID 15305015.
  • Law MH, Cotton RG, Berger GE (2006). "The role of phospholipases A2 in schizophrenia". Mol. Psychiatry. 11 (6): 547–56. doi:10.1038/sj.mp.4001819. PMID 16585943.
  • Shimizu T, Ohto T, Kita Y (2006). "Cytosolic phospholipase A2: biochemical properties and physiological roles". IUBMB Life. 58 (5–6): 328–33. doi:10.1080/15216540600702289. PMID 16754327.
  • Sharp JD, White DL, Chiou XG; et al. (1991). "Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2". J. Biol. Chem. 266 (23): 14850–3. PMID 1869522.
  • Clark JD, Lin LL, Kriz RW; et al. (1991). "A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP". Cell. 65 (6): 1043–51. PMID 1904318.
  • Tay A, Simon JS, Squire J; et al. (1995). "Cytosolic phospholipase A2 gene in human and rat: chromosomal localization and polymorphic markers". Genomics. 26 (1): 138–41. PMID 7782073.
  • Wu T, Ikezono T, Angus CW, Shelhamer JH (1995). "Characterization of the promoter for the human 85 kDa cytosolic phospholipase A2 gene". Nucleic Acids Res. 22 (23): 5093–8. PMID 7800505.
  • Miyashita A, Crystal RG, Hay JG (1995). "Identification of a 27 bp 5'-flanking region element responsible for the low level constitutive expression of the human cytosolic phospholipase A2 gene". Nucleic Acids Res. 23 (2): 293–301. PMID 7862535.
  • Morri H, Ozaki M, Watanabe Y (1995). "5'-flanking region surrounding a human cytosolic phospholipase A2 gene". Biochem. Biophys. Res. Commun. 205 (1): 6–11. PMID 7999086.
  • Sharp JD, Pickard RT, Chiou XG; et al. (1994). "Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2". J. Biol. Chem. 269 (37): 23250–4. PMID 8083230.
  • Lin LL, Wartmann M, Lin AY; et al. (1993). "cPLA2 is phosphorylated and activated by MAP kinase". Cell. 72 (2): 269–78. PMID 8381049.
  • Flati V, Haque SJ, Williams BR (1996). "Interferon-alpha-induced phosphorylation and activation of cytosolic phospholipase A2 is required for the formation of interferon-stimulated gene factor three". EMBO J. 15 (7): 1566–71. PMID 8612580.
  • de Carvalho MG, McCormack AL, Olson E; et al. (1996). "Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes". J. Biol. Chem. 271 (12): 6987–97. PMID 8636128.
  • Freed KA, Moses EK, Brennecke SP, Rice GE (1997). "Differential expression of type II, IV and cytosolic PLA2 messenger RNA in human intrauterine tissues at term". Mol. Hum. Reprod. 3 (6): 493–9. PMID 9239738.
  • 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.
  • Perisic O, Fong S, Lynch DE; et al. (1998). "Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2". J. Biol. Chem. 273 (3): 1596–604. PMID 9430701.
  • Börsch-Haubold AG, Bartoli F, Asselin J; et al. (1998). "Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells". J. Biol. Chem. 273 (8): 4449–58. PMID 9468497.

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