Abstract
Recently, it was shown that phospholipase A2 (PLA2) is essential for exposing Mac-1 (CDllb/CD18) on the cell surface of leukocytes1,2. Mac-1 is mandatory for leukocyte migration in vitro, and lack of Mac-1 on human leukocytes is associated with failure of in vitro chemotaxis3. To further substantiate the contribution of PLA2 in cell migration we investigated the effects of PLA2 inhibition on chemotaxis of mixed human leukocytes (MHL) induced by fMLP and the G-protein activator NaF7–9. Migration was measured in a modified 48-well micro-chemotaxis Boyden-chamber6. As PLA2 inhibitors manoalide4, mepacrine5, and BM 16.2115, a new PLA2 inhibitor, were employed.
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