Interactions of arachidonate metabolism and protein kinase C in mediating neutrophil function

Diglyceride activators of protein kinase C (i.e., 1-0-myristoyl-, 1-0-palmitoyl-, and 1-0-oleoyl-2-acetylglycerol) interacted synergistically with an arachidonate metabolite, 5-hydroxyicosatetraenoate, to stimulate neutrophil degranulation and superoxide anion generation. Contrastingly, combinations of 15-hydroxyicosatetraenoate with the glycerides or 5-hydroxyicosatetraenoate with a dialkylglyceride (1-0-hexadecyl-2-ethylglycerol) produced no such synergy. The data support a view of stimulus-response coupling wherein protein kinase C is activated in parallel with the mobilization of arachidonate. Respective products of these events, e.g., phosphorylated proteins and hydroxyicosatetraenates, then interact to mediate function.