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Protein kinase C regulates leukotriene B 4 receptors in human neutrophils
Author(s) -
O'Flaherty Joseph T.,
Redman Jimmy F.,
Jacobson David P.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80996-6
Subject(s) - protein kinase c , leukotriene b4 , receptor , leukotriene , microbiology and biotechnology , chemistry , biochemistry , myristoylation , biology , signal transduction , membrane , immunology , inflammation , asthma
Three protein kinase C (PKC) activators, viz. phorbol myristate acetate, mezerein, and rac ‐1‐ O ‐myristoyl‐2‐acetylglycerol, inhibited human neutrophil binding of [ 3 H] leukotriene B 4 (LTB 4 ) by reducing the number of high‐affinity receptors available to the arachidonic acid metabolite. The inhibitory effect occurred in whole cells and cytoplasts but not in isolated membranes; it appeared to involve the activation of PKC rather than direct competition for binding sites. PKC may govern cellular responsiveness by regulating the receptor‐linked bioactions of endogenous mediators like LTB 4 .