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Protein PLA2G2A PDB 1ayp.png
Available structures
PDB Human UniProt search: PDBe RCSB
Aliases PLA2G2A, MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, phospholipase A2 group IIA
External IDs HomoloGene: 254 GeneCards: PLA2G2A
Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for PLA2G2A
Genomic location for PLA2G2A
Band 1p36.13 Start 19,975,431 bp[1]
End 19,980,416 bp[1]
RNA expression pattern
PBB GE PLA2G2A 203649 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 1: 19.98 – 19.98 Mb n/a
PubMed search [2] n/a
View/Edit Human

Phospholipase A2, membrane associated is an enzyme that in humans is encoded by the PLA2G2A gene.[3][4]

See also[edit]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000188257 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". 
  3. ^ Tischfield JA, Xia YR, Shih DM, Klisak I, Chen J, Engle SJ, Siakotos AN, Winstead MV, Seilhamer JJ, Allamand V, Gyapay G, Lusis AJ (Feb 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. 
  4. ^ "Entrez Gene: PLA2G2A Phospholipase A2, group IIA (platelets, synovial fluid)". 

Further reading[edit]

  • Kramer RM, Johansen B, Hession C, Pepinsky RB (1990). "Structure and properties of a secretable phospholipase A2 from human platelets". Adv. Exp. Med. Biol. 275: 35–53. doi:10.1007/978-1-4684-5805-3_3. PMID 2239446. 
  • 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. 
  • Law MH, Cotton RG, Berger GE (2006). "The role of phospholipases A2 in schizophrenia". Mol. Psychiatry. 11 (6): 547–56. doi:10.1038/ PMID 16585943. 
  • 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. 
  • Scott DL, White SP, Browning JL, et al. (1991). "Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate". Science. 254 (5034): 1007–10. doi:10.1126/science.1948070. PMID 1948070. 
  • Pruzanski W, Bogoch E, Stefanski E, et al. (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, et al. (1991). "Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution". Nature. 352 (6330): 79–82. doi:10.1038/352079a0. PMID 2062381. 
  • Seilhamer JJ, Randall TL, Johnson LK, et al. (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. 
  • Kanda A, Ono T, Yoshida N, et al. (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, et al. (1989). "Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid". J. Biol. Chem. 264 (10): 5335–8. PMID 2925608. 
  • Kramer RM, Hession C, Johansen B, et al. (1989). "Structure and properties of a human non-pancreatic phospholipase A2". J. Biol. Chem. 264 (10): 5768–75. 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, et al. (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. PMID 3240982. 
  • Schevitz RW, Bach NJ, Carlson DG, et al. (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. 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, et al. (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. 
  • Minami T, Tojo H, Shinomura Y, et al. (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, et al. (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.