Calphostin C, a Potent and Specific Inhibitor of Protein Kinase C, Reduces Phorbol Ester-Induced but Not Primary Call-Induced Catecholamine Secretion from Digitonin-Permeabilized Bovine Adrenal Medullary Cells
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چکیده
Calphostin C, a protein kinase C inhibitor, reduced phorbol ester-induced enhancement of catecholamine secretion but not primary Ca"-induced secretion from digitonin-permeabilized bovine adrenal medullary cells, indicating that this compound selectively inhibited protein kinase C-dependent
منابع مشابه
Regulation of chromaffin cell secretion and protein kinase C activity by chronic phorbol ester treatment.
Bovine adrenal chromaffin cells were exposed to phorbol esters to determine the effects of reduced levels of protein kinase C on secretion of hormones. Treatment with active phorbol esters such as 4 beta-phorbol 12, 13-didecanoate (PDD) reduced levels of protein kinase C activity with a maximal 80-90% reduction in activity after 16-24 h treatment (greater than or equal to 500 nM PDD). Treatment...
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The relationship between catecholamine secretion and arachidonic acid release from digitonin-treated chromaffin cells was investigated. Digitonin renders permeable the plasma membranes of bovine adrenal chromaffin cells to Ca2+, ATP, and proteins. Digitonin-treated cells undergo exocytosis of catecholamine in response to micromolar Ca2+ in the medium. The addition of micromolar Ca2+ to digitoni...
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تاریخ انتشار 2006