PLA2G2A

Phospholipase A₂, membrane associated is an enzyme that in humans is encoded by the PLA2G2A gene.

PLA2G2A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AYP, 1BBC, 1DB4, 1DB5, 1DCY, 1J1A, 1KQU, 1KVO, 1N28, 1N29, 1POD, 1POE, 3U8B, 3U8D, 3U8H, 3U8I
Identifiers
Aliases	PLA2G2A, MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, phospholipase A2 group IIA
External IDs	OMIM: 172411; MGI: 104642; HomoloGene: 254; GeneCards: PLA2G2A; OMA:PLA2G2A - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.13 Start 19,975,431 bp End 19,980,416 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 D3|4 70.57 cM Start 138,559,171 bp End 138,562,497 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in palpebral conjunctiva pericardium right coronary artery tendon of biceps brachii mucosa of ileum synovial joint gastric mucosa right auricle left coronary artery rectum Top expressed in crypt of lieberkuhn of small intestine duodenum jejunum Paneth cell ankle joint Ileal epithelium morula gastrula intercostal muscle submandibular gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding calcium-dependent phospholipase A2 activity metal ion binding hydrolase activity phospholipid binding phospholipase A2 activity Cellular component membrane endoplasmic reticulum membrane secretory granule endoplasmic reticulum perinuclear region of cytoplasm extracellular exosome extracellular region plasma membrane extracellular space Biological process phosphatidic acid biosynthetic process phosphatidylserine acyl-chain remodeling positive regulation of inflammatory response phosphatidylethanolamine acyl-chain remodeling lipid metabolism phosphatidylinositol acyl-chain remodeling lipid catabolic process positive regulation of macrophage derived foam cell differentiation low-density lipoprotein particle remodeling positive regulation of ERK1 and ERK2 cascade phosphatidylglycerol acyl-chain remodeling phosphatidic acid metabolic process phosphatidylcholine acyl-chain remodeling defense response to Gram-positive bacterium phospholipid metabolic process antimicrobial humoral response arachidonic acid secretion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5320 18780 Ensembl ENSG00000188257 ENSMUSG00000058908 UniProt P14555 P31482 RefSeq (mRNA) NM_001161729 NM_000300 NM_001161727 NM_001161728 NM_001395463 NM_001082531 NM_011108 RefSeq (protein) NP_000291 NP_001155199 NP_001155200 NP_001155201 NP_001076000 Location (UCSC) Chr 1: 19.98 – 19.98 Mb Chr 4: 138.56 – 138.56 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

See also

• Phospholipase A₂

Further reading

• Kramer RM, Johansen B, Hession C, Pepinsky RB (1990). "Structure and Properties of a Secretable Phospholipase A2 from Human Platelets". Phospholipase A2. Advances in Experimental Medicine and Biology. Vol. 275. pp. 35–53. doi:10.1007/978-1-4684-5805-3_3. ISBN 978-1-4684-5807-7. PMID 2239446.
• Schröder HC, Perovic S, Kavsan V, Ushijima H, Müller WE (1998). "Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death". Neurotoxicology. 19 (4–5): 683–8. PMID 9745929.
• 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. S2CID 13248313.
• Carlquist JF, Muhlestein JB, Anderson JL (2007). "Lipoprotein-associated phospholipase A2: a new biomarker for cardiovascular risk assessment and potential therapeutic target". Expert Rev. Mol. Diagn. 7 (5): 511–7. doi:10.1586/14737159.7.5.511. PMID 17892360. S2CID 23148887.
• Scott DL, White SP, Browning JL, Rosa J, Gelb M, Sigler P (1991). "Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate". Science. 254 (5034): 1007–10. Bibcode:1991Sci...254.1007S. doi:10.1126/science.1948070. PMID 1948070.
• Pruzanski W, Bogoch E, Stefanski E, Wloch M, Vadas P (1991). "Enzymatic activity and distribution of phospholipase A2 in human cartilage". Life Sci. 48 (25): 2457–62. doi:10.1016/0024-3205(91)90381-K. PMID 2046470.
• Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson Jr T, Hermann RB, Kramer RM (1991). "Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution". Nature. 352 (6330): 79–82. Bibcode:1991Natur.352...79W. doi:10.1038/352079a0. PMID 2062381. S2CID 4238043.
• Seilhamer JJ, Randall TL, Johnson LK, Heinzmann C, Klisak I, Sparkes RS, Lusis AJ (1989). "Novel gene exon homologous to pancreatic phospholipase A2: sequence and chromosomal mapping of both human genes". J. Cell. Biochem. 39 (3): 327–37. doi:10.1002/jcb.240390312. PMID 2708461. S2CID 40949411.
• Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M (1989). "The primary structure of a membrane-associated phospholipase A2 from human spleen". Biochem. Biophys. Res. Commun. 163 (1): 42–8. doi:10.1016/0006-291X(89)92096-2. PMID 2775276.
• Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK (1989). "Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid". J. Biol. Chem. 264 (10): 5335–8. doi:10.1016/S0021-9258(18)83549-9. PMID 2925608.
• Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB (1989). "Structure and properties of a human non-pancreatic phospholipase A2". J. Biol. Chem. 264 (10): 5768–75. doi:10.1016/S0021-9258(18)83616-X. PMID 2925633.
• Lai CY, Wada K (1989). "Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme". Biochem. Biophys. Res. Commun. 157 (2): 488–93. doi:10.1016/S0006-291X(88)80275-4. PMID 3202859.
• Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K (1989). "Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid". J. Biochem. 104 (3): 326–8. doi:10.1093/oxfordjournals.jbchem.a122467. PMID 3240982.
• Schevitz RW, Bach NJ, Carlson DG, Chirgadze N, Clawson D, Dillard R, Draheim S, Hartley L, Jones N (1995). "Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2". Nat. Struct. Biol. 2 (6): 458–65. doi:10.1038/nsb0695-458. PMC 7097651. PMID 7664108.
• Ancian P, Lambeau G, Mattéi MG, Lazdunski M (1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization". J. Biol. Chem. 270 (15): 8963–70. doi:10.1074/jbc.270.15.8963. PMID 7721806.
• MacPhee M, Chepenik KP, Liddell RA, Nelson KK, Siracusa LD, Buchberg AM (1995). "The secretory phospholipase A2 gene is a candidate for the Mom1 locus, a major modifier of ApcMin-induced intestinal neoplasia". Cell. 81 (6): 957–66. doi:10.1016/0092-8674(95)90015-2. PMID 7781071. S2CID 16493676.
• Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M (1993). "Purification and characterization of a phospholipase A2 from human ileal mucosa". Biochim. Biophys. Acta. 1170 (2): 125–30. doi:10.1016/0005-2760(93)90061-d. PMID 8399335.
• Sartipy P, Johansen B, Camejo G, Rosengren B, Bondjers G, Hurt-Camejo E (1996). "Binding of human phospholipase A2 type II to proteoglycans. Differential effect of glycosaminoglycans on enzyme activity". J. Biol. Chem. 271 (42): 26307–14. doi:10.1074/jbc.271.42.26307. PMID 8824283.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.