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J. Biol. Chem., Vol. 266, Issue 23, 14850-14853, Aug, 1991

Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2

JD Sharp, DL White, XG Chiou, T Goodson, GC Gamboa, D McClure, S Burgett, J Hoskins, PL Skatrud and JR Sportsman
Lilly Research Laboratories, Indianapolis, Indiana 46285.

Phospholipases A2 (PLA2s) play a key role in inflammatory processes through production of precursors of eicosanoids and platelet-activating factor. Recently, we described the purification of a novel approximately 100-kDa cytosolic PLA2 (cPLA2) from human monoblast U937 cells that is activated by physiological (intracellular) concentrations of Ca2+ (Kramer, R. M., Roberts, E. F., Manetta, J., and Putnam, J. E. (1991) J. Biol. Chem. 266, 5268-5272). Here we report the isolation of the complementary DNA encoding human cPLA2 and confirm its identity by expression in bacteria and in hamster cells. The predicted 749-amino acid cPLA2 protein has no similarity to the well known secretory PLA2s, but contains a structural element homologous to the C2 region of protein kinase C. The molecular cloning of cPLA2 will allow further studies defining the structure, function, and regulation of this novel PLA2.
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