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J. Biol. Chem., Vol. 266, Issue 23, 14850-14853, Aug, 1991
JD Sharp, DL White, XG Chiou, T Goodson, GC Gamboa, D McClure, S Burgett, J Hoskins, PL Skatrud and JR Sportsman
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.
Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2
Lilly Research Laboratories, Indianapolis, Indiana 46285.
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