Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals as well as fish.[3] Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .[2][4]
References
↑Dennis EA (Jun 1994). "Diversity of group types, regulation, and function of phospholipase A2". J Biol Chem. 269 (18): 13057–60. PMID8175726.
↑Sæle O, Nordgreen A, Olsvik PA, Hamre K (2010). "Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)". Br J Nutr. 105 (2): 1–10. doi:10.1017/S0007114510003466. PMID20836903.
↑Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK (1987). "Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung". DNA. 5 (6): 519–27. doi:10.1089/dna.1.1986.5.519. PMID3028739.
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. PMID9745929.
Sapirstein A, Bonventre JV (2000). "Phospholipases A2 in ischemic and toxic brain injury". Neurochem. Res. 25 (5): 745–53. doi:10.1023/A:1007583708713. PMID10905638.
Verheij HM, Westerman J, Sternby B, De Haas GH (1983). "The complete primary structure of phospholipase A2 from human pancreas". Biochim. Biophys. Acta. 747 (1–2): 93–9. doi:10.1016/0167-4838(83)90126-7. PMID6349696.
Sternby B, Akerström B (1984). "Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals". Biochim. Biophys. Acta. 789 (2): 164–9. doi:10.1016/0167-4838(84)90201-2. PMID6477929.
Grataroli R, Dijkman R, Dutilh CE, et al. (1982). "Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region". Eur. J. Biochem. 122 (1): 111–7. doi:10.1111/j.1432-1033.1982.tb05855.x. PMID7060561.
Rönkkö S (1995). "Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 110 (3): 503–9. doi:10.1016/0305-0491(94)00190-6. PMID7584826.
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. PMID7721806.
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. PMID8300559.
Gispert S, Twells R, Orozco G, et al. (1993). "Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1". Nat. Genet. 4 (3): 295–9. doi:10.1038/ng0793-295. PMID8358438.
Cupillard L, Koumanov K, Mattéi MG, et al. (1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J. Biol. Chem. 272 (25): 15745–52. doi:10.1074/jbc.272.25.15745. PMID9188469.
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. doi:10.1097/00042560-199709010-00001. PMID9377118.
Sartipy P, Bondjers G, Hurt-Camejo E (1999). "Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes". Arterioscler. Thromb. Vasc. Biol. 18 (12): 1934–41. doi:10.1161/01.ATV.18.12.1934. PMID9848887.