Studies on the platelet-activating factor interaction with protein kinase C in human neutrophils.

Platelet-activating factor (PAF) stimulated neutrophils to translocate cytosolic protein kinase C (PKC) to plasmalemma by a Ca(2+)-transient-independent mechanism. Arachidonic acid had these same effects but unlike PAF acted independently, not only of Ca2+ transients but also of other cell Ca2+ pools. The fatty acid (which is released by PAF-challenged cells) may mediate PKC movements and thereby contribute to the many Ca(2+)-independent bioactions of PAF.