Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Phospholipase A2 (PLA2, EC 3.1.1.4) cleaves the sn-2 fatty acid of phospholipids, primarily phosphatidylcholine, to generate lysophosphatidylcholine and arachidonic acid. Most commonly-used inhibitors (e.g. bromoenol lactone, arachidonyl trifluoromethyl ketone or methyl arachidonyl fluorophosphonate) are either non-selective within the family of phospholipase A2 enzymes or have activity against other eicosanoid-metabolising enzymes.
Secreted or extracellular forms: sPLA2-1B, sPLA2-2A, sPLA2-2D, sPLA2-2E, sPLA2-2F, sPLA2-3, sPLA2-10 and sPLA2-12A
Cytosolic, calcium-dependent forms: cPLA2-4A, cPLA2-4B, cPLA2-4C, cPLA2-4D, cPLA2-4E and cPLA2-4F
Other forms: PLA2-G5, iPLA2-G6, PLA2-G7 and PAFAH2 (platelet-activating factor acetylhydrolase 2)
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sPLA2-1B
C
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sPLA2-2D C Show summary »« Hide summary
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sPLA2-2E C Show summary »« Hide summary
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sPLA2-2F C Show summary »« Hide summary
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sPLA2-2A
C
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PLA2-G7
C
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sPLA2-3 C Show summary »« Hide summary
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sPLA2-10 C Show summary »« Hide summary
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sPLA2-12A C Show summary »« Hide summary
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cPLA2-4A
C
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cPLA2-4B C Show summary »« Hide summary
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cPLA2-4C C Show summary »« Hide summary
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cPLA2-4D C Show summary »« Hide summary
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cPLA2-4E C Show summary »« Hide summary
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cPLA2-4F C Show summary »« Hide summary
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PLA2-G5 C Show summary »« Hide summary
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iPLA2-G6 C Show summary »« Hide summary
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platelet activating factor acetylhydrolase 2 C Show summary »« Hide summary
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1. Ancian P, Lambeau G, Lazdunski M. (1995) Multifunctional activity of the extracellular domain of the M-type (180 kDa) membrane receptor for secretory phospholipases A2. Biochemistry, 34 (40): 13146-51. [PMID:7548076]
2. Beck LH, Bonegio RG, Lambeau G, Beck DM, Powell DW, Cummins TD, Klein JB, Salant DJ. (2009) M-type phospholipase A2 receptor as target antigen in idiopathic membranous nephropathy. N. Engl. J. Med., 361 (1): 11-21. [PMID:19571279]
3. Blackie JA, Bloomer JC, Brown MJ, Cheng HY, Hammond B, Hickey DM, Ife RJ, Leach CA, Lewis VA, Macphee CH et al.. (2003) The identification of clinical candidate SB-480848: a potent inhibitor of lipoprotein-associated phospholipase A2. Bioorg. Med. Chem. Lett., 13 (6): 1067-70. [PMID:12643913]
4. Hagishita S, Yamada M, Shirahase K, Okada T, Murakami Y, Ito Y, Matsuura T, Wada M, Kato T, Ueno M et al.. (1996) Potent inhibitors of secretory phospholipase A2: synthesis and inhibitory activities of indolizine and indene derivatives. J. Med. Chem., 39 (19): 3636-58. [PMID:8809154]
5. Ludwig J, Bovens S, Brauch C, Elfringhoff AS, Lehr M. (2006) Design and synthesis of 1-indol-1-yl-propan-2-ones as inhibitors of human cytosolic phospholipase A2alpha. J. Med. Chem., 49 (8): 2611-20. [PMID:16610804]
6. Oslund RC, Cermak N, Gelb MH. (2008) Highly specific and broadly potent inhibitors of mammalian secreted phospholipases A2. J. Med. Chem., 51 (15): 4708-14. [PMID:18605714]
7. Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G. (2003) Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry, 42 (39): 11494-503. [PMID:14516201]
8. Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN. (1994) Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J. Biol. Chem., 269 (37): 23250-4. [PMID:8083230]
9. Wilensky RL, Macphee CH. (2009) Lipoprotein-associated phospholipase A(2) and atherosclerosis. Curr. Opin. Lipidol., 20 (5): 415-20. [PMID:19667981]
Database page citation:
Phospholipase A2. Accessed on 12/07/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=275.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Marrion N, Peters JA, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Southan C, Davies JA and CGTP Collaborators (2015) The Concise Guide to PHARMACOLOGY 2015/16: Enzymes. Br J Pharmacol. 172: 6024-6109.


The sequence of PLA2-2C suggests a lack of catalytic activity, while PLA2-12B (GXIIB, GXIII sPLA2-like) appears to be catalytically inactive [7]. A further fragment has been identified with sequence similarities to Group II PLA2 members. Otoconin 90 (OC90) shows sequence homology to PLA2-G10.
A binding protein for secretory phospholipase A2 has been identified which shows modest selectivity for sPLA2-1B over sPLA2-2A, and also binds snake toxin phospholipase A2 [1]. The binding protein appears to have clearance function for circulating secretory phospholipase A2, as well as signalling functions, and is a candidate antigen for idiopathic membraneous nephropathy [2].
PLA2-G7 and PAFAH2 also express platelet-activating factor acetylhydrolase activity (EC 3.1.1.47).