(Q67465770)

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Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation

scientific article published on 01 November 1992

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13 September 2019

Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation (English)

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13 September 2019

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8 September 2022

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M. L. Vitale

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8 September 2022

A. Rodríguez Del Castillo

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8 September 2022

J. M. Trifaró

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1 November 1992

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13 September 2019

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13 September 2019

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463-474

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Phorbol esters enhance exocytosis from chromaffin cells by two mechanisms

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Ca2+-Activated, phospholipid-dependent protein kinase catalyzes the phosphorylation of actin-binding proteins

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The phorbol ester TPA increases the affinity of exocytosis for calcium in 'leaky' adrenal medullary cells

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Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C

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Phorbol esters increase the amount of Ca2+, phospholipid-dependent protein kinase associated with plasma membrane

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Characterization of anti-actin antibodies and their use in immunocytochemical studies on the localization of actin in adrenal chromaffin cells in culture

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10.1016/0306-4522(92)90330-5

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1281530%20AND%20SRC:MED&resulttype=core&format=json

13 September 2019

1 reference

Europe PubMed Central

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13 September 2019

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