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• W2093557710 abstract "Selective protein kinase C (PKC) activators and inhibitors were used to investigate the involvement of specific PKC isoforms in the modulation of voltage-sensitive Ca(2+) channels (VSCCs) in bovine adrenal chromaffin cells. Exposure to the phorbol ester phorbol-12,13-dibutyrate (PDBu) inhibited the Ca(2+) currents elicited by depolarizing voltage steps. This inhibition was occluded by the PKC-specific inhibitor Ro 31-8220 but remained unaffected by Gö 6976, a selective inhibitor of conventional PKC isoforms. PDBu treatment caused the translocation of PKC-alpha and -epsilon isoforms from cytosol to membranes. PKC-iota and -zeta showed no signs of translocation. It is concluded that VSCCs are specifically inhibited by the activation of PKC-epsilon in chromaffin cells. This may be relevant to the action of phospholipase-linked receptors involved in the control of Ca(2+) influx, both in catecholaminergic cells and other cell types." @default.
• W2093557710 created "2016-06-24" @default.
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• W2093557710 date "2001-03-07" @default.
• W2093557710 modified "2023-10-14" @default.
• W2093557710 title "Isoform-specific inhibition of voltage-sensitive Ca²⁺channels by protein kinase C in adrenal chromaffin cells" @default.
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• W2093557710 doi "https://doi.org/10.1016/s0014-5793(01)02252-9" @default.
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