Phospholipase A2 activity in the postnuclear supernatant of lymphocytes has been studied by measuring 14C arachidonate released from labelled phosphatidyl ethanolamine (PE) and phosphatidyl choline (PC) as exogenous substrates. The pH optimum was 7.5-9.0 for PE and 9.0 for PC. Phospholipase A2 was not detected in the presence of 2 mM EGTA. It was optimal with the millimolar calcium concentrations and higher towards PE. Preincubation of lymphocytes with 0.5 M ionophore A-23187 was followed by 2.4 fold stimulation of the phospholipase activity. A stimulatory effect was observed after preincubation of cells with 10 micrograms/ml of phytohemagglutinin, lipopolysaccharide, concanavalin A; it decreased as: lipopolysaccharide greater than phytohemagglutinin greater than concanavalin A. The results obtained have suggested the possibility of existence of different forms of phospholipase A2 in the spleen lymphocytes and participation of the enzyme in the early signalling events.
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