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J Membr Biol. 1988 Aug;104(1):21-34.

Evidence implicating protein kinase C in exocytosis from electropermeabilized bovine chromaffin cells.

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MRC Secretory Mechanism Group, Division of Biomedical Sciences, Kings College, London, England.


The calcium sensitivity of exocytosis from electro-permeabilized chromaffin cells is increased by activators of protein kinase C, such as TPA and certain phorbol esters, diacylglycerols, and mezerein. A range of putative inhibitors of protein kinase C block both the phorbol ester-sensitive component of secretion and also the underlying insensitive component. These inhibitors are also shown to inhibit medulla protein kinase C activity in vitro. The extent of secretion is reduced when electro-permeabilized cells are exposed to Ca2+ levels much in excess of 50 microM. The onset of inhibition is faster than the relatively slow rate of Ca-dependent exocytosis and is insensitive to inhibitors of proteolysis. Adrenal medulla protein kinase C activity is also irreversibly inhibited by high Ca2+ concentrations. Both the secretory response and the protein kinase C activity in vitro have similar nucleotide and cation specificities. Although these data do not definitely establish an involvement of protein kinase C in exocytosis, none argue against it.

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