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Inhibition of neutrophil responsiveness caused by phorbol esters is blocked by the protein kinase C inhibitor H7

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
The protein kinase antagonist H7 was found to inhibit the phosphorylation of the 50 kDa protein kinase C substrate stimulated by phorbol 12-myristate 13-acetate (PMA) but did not affect the quin2 and secretory responses of the neutrophils to fMet-Leu-Phe and leukotriene B/sub 4/. In addition, pretreatment of the cells with H7 blocked the ability of PMA to inhibit the latter two responses to the addition of the chemoattractants. Taken together, these results provide strong evidence for the involvement of protein kinase C in the inhibition of neutrophil - and probably also other cells - responsiveness brought about by preincubation with phorbol esters. Additionally, they invite a reevaluation of the role of protein kinase C in the excitation-response coupling sequence of these cells directed more towards a negative, modulatory, role than that of a critical element in its initiation.
Research Organization:
Univ. of Connecticut Health Center, Farmington
OSTI ID:
5002927
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 137:1; ISSN BBRCA
Country of Publication:
United States
Language:
English