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• W1491708792 abstract "Treatment of enucleated, granule‐free neutrophil cytoplasts with the protein kinase C activator phorbol 12 O ‐myristate‐13‐acetate (PMA) causes an increased ‐ 32 P‐incorporation into a variety of polypeptides. Permeabilization of PMA‐stimulated, 32 P‐labeled cytoplasts by 0.01% digitonin fully releases the majority of these phosphorylated proteins. A statistically significant correlation is found between the extent of PMA‐induced activation of generation of Superoxide anion (O − 2 ) and the phosphorylation of a cytosolic polypeptide with an apparent M r , of 46000, whose ‐ 32 P‐labeling is also enhanced by the treatment of cytoplasts with 1‐oleyl‐2‐acetylglycerol, the Ca 2+ ionophore ionomycin or latex beads. Furthermore, treatment of cytoplasts with the protein kinase C inhibitor trifluoperazine markedly inhibits the 32 P‐labeling of proteins in the 40000 M r range, including the 46 kDa polypeptide, and almost totally abolishes the activation of O − 2 production by PMA." @default.
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• W1491708792 date "1985-01-28" @default.
• W1491708792 modified "2023-09-26" @default.
• W1491708792 title "Activation of protein kinase C in neutrophil cytoplasts" @default.
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• W1491708792 doi "https://doi.org/10.1016/0014-5793(85)81068-1" @default.
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