Role of intracellular calcium in the regulation of phospholipase A2 in fMet-Leu-Phe-challenged human polymorph neutrophils.

Abstract

In the present study, we have shown that the protein kinase C (PKC) inhibition by staurosporine augmented fMet-Leu-Phe-(FMLP)-induced arachidonic acid (AA) release in human polymorph neutrophils (PMN). This effect is in contradiction to a recently reported mechanism that besides Ca2+, the phosphorylation of cytosolic phospholipase A2 (cPLA2) is essential for the enzyme activation. In addition, we found that staurosporine elevated the basal concentration of intracellular Ca2+, although initial Ca2+ release was not affected. Since thapsigargin, a blocker of endogenous Ca2+ ATPase, also increased AA release dose-dependently, we believe that the elevation of intracellular Ca2+ is the most essential step and not the phosphorylation of enzyme for the activation of cPLA2.