Protein phosphorylation associated with the stimulation of neutrophils. Modulation of superoxide production by protein kinase C and calcium |
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Authors: | Paul G. Heyworth John A. Badwey |
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Affiliation: | (1) Department of Molecular and Experimental Medicine, Research Institute of Scripps Clinic, 92037 La Jolla, California;(2) The Department of Cell Physiology, Boston Biomedical Research Institute, 02114 Boston, Massachusetts;(3) Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 02115 Boston, Massachusetts |
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Abstract: | Neutrophils and other phagocytic cells of the immune system possess a superoxide-generating oxidase system which is essential for the efficient killing of microbes. The system is activated by a wide variety of stimuli, some of which operate through pathways involving protein kinase C (PKC), while others appear not to. The PKC-dependent pathway is probably the major signal transduction route for most of the stimuli. Alterations in cellular Ca2+ and diglyceride levels can have a pronounced stimulatory effect on this pathway by their ability to synergistically activate PKC. This review discusses PKC, the different interactions of this kinase with the plasmalemma that are important in superoxide production, the synergy between Ca2+ and diglyceride, and the nature of the phosphoproteins involved. Evidence supporting the existence of the PKC-independent pathway is also reviewed. |
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Keywords: | Phagocyte neutrophil chronic granulomatous disease protein kinase protein phosphorylation superoxide NADPH oxidase phorbol ester chemotactic peptide synergy |
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