FEBS Letters | |
Activation of protein kinase C in neutrophil cytoplasts | |
Gennaro, Renato1  Romeo, Domenico1  Florio, Chiara1  | |
[1] Istituto di Chimica Biologica dell'Università, 34127 Trieste, Italy | |
关键词: Neutrophil cytoplast; Protein phosphorylation; Protein kinase C; Superoxide anion; Phorbol myristate acetate; PMA; phorbol 12-O-myristate-13acetate; TFP; trifluoperazine; OAG; 1-oleyl-2-acetylglycerol; PBS; phosphate-buffered saline; SDS-PAGE; sodium dodecyl sulfate-polyacrylamide gel electrophoresis; B12BP; vitamin B12 binding protein; | |
DOI : 10.1016/0014-5793(85)81068-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Treatment of enucleated, granule-free neutrophil cytoplasts with the protein kinase C activator phorbol 12O-myristate-13-acetate (PMA) causes an increased -32P-incorporation into a variety of polypeptides. Permeabilization of PMA-stimulated, 32P-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 -32P-labeling is also enhanced by the treatment of cytoplasts with 1-oleyl-2-acetylglycerol, the Ca2+ ionophore ionomycin or latex beads. Furthermore, treatment of cytoplasts with the protein kinase C inhibitor trifluoperazine markedly inhibits the 32P-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.
【 授权许可】
Unknown
【 预 览 】
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