Activation of the glycogenolytic cascade in human polymorphonuclear leucocytes by different phagocytic stimuli.

Human polymorphonuclear leucocytes were found to respond to activation by immunoglobulin opsonized latex particles and to complement opsonized zymosan particles with a rapid transient increase in cAMP concentration, dissociation of the cAMP dependent protein kinase, activation of glycogen phosphorylase and glycogen break down. However, since phosphorylase kinase was not activated, the activation of phosphorylase is believed to be secondary to non-covalent activation of phosphorylase kinase by Ca2+. Activation by the soluble stimulator phorbol myristate acetate resulted in activation of phosphorylase and glycogen break down, whereas no changes in cAMP concentration, protein kinase activity, or phosphorylase kinase activity were observed. The activation of phosphorylase is ascribed to an increase in cytosolic Ca2+ concentration. The response to stimulation by zymosan was strongly inhibited by ethylene glycol-bis-(beta-aminoethyl ether)-N,N1-tetraacetic acid, which did not affect stimulation by either latex particles or phorbol myristate acetate. The same differential effect of ethylene glycol-bis(beta-aminoethyl ether)-N,N1-tetraacetic acid was observed when the response of the cells was measured as increase in oxygen consumption and activation of the hexose monophosphate shunt.