STIMULATION OF A HISTONE-H4 PROTEIN-KINASE IN TRITON-X-100 LYSATES OF RABBIT PERITONEAL NEUTROPHILS PRETREATED WITH CHEMOTACTIC FACTORS - LACK OF REQUIREMENTS OF CALCIUM MOBILIZATION AND PROTEIN-KINASE-C ACTIVATION

The characteristics of the activation of a histone H4 kinase activity in Triton X‐100 lysates of rabbit peritoneal neutrophils pretreated with fMet‐Leu‐Phe were studied: The activation of the kinase was (a) inhibited by the antagonist of formylpeptide, t‐Boc‐(Phe‐Leu)2−‐Phe, (b) completely inhibited by pertussis toxin pretreatment, (c) not affected by the pretreatment of neutrophils with an activator of protein kinase C, phorbol‐12‐myristate‐13‐acetate, or an inhibitor of protein kinase C, 1‐(5‐isoquinoline‐sulfonyl)‐2‐methyl‐piperazine, and (d) not inhibited in the cells preloaded with the intracellular calcium chelators, bis‐(o‐aminophenoxy)‐ethane‐N,N,N',N'‐tetra acetic acid acetoxymethyl‐ester (BAPTA/AM). These results suggest that the stimulus‐induced activation of H4 kinase requires functional receptor and GTP‐binding protein but neither calcium mobilization nor protein kinase C activation. Copyright © 1990 Wiley‐Liss, Inc.