Protein kinase C activator inhibits voltage‐sensitive Ca2+ channels and catecholamine secretion in adrenal chromaffin cells
- 13 February 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 359 (2-3) , 137-141
- https://doi.org/10.1016/0014-5793(95)00026-6
Abstract
We have investigated the effects of the phorbol ester 12-myristate 13-acetate (PMA) on depolarization-evoked Ca 2+ influx and catecholamine secretion in bovine adrenal chromaffin cells. PMA (100 nM) strongly inhibited K + -evoked [Ca 2+ ] i transients and Mn 2+ quenching of fura-2 fluorescence. In contrast, 4α-phorbol 12,13-didecanoate, a phorbol ester inactive on protein kinase C (PKC), had no effect. Maximal PMA-mediated inhibition occurred at 5–10 min incubations and were variable from cell to cell, ranging from 25 to 65% of controls. The [Ca 2+ ] i transients evoked by the L-type Ca 2+ channel activator Bay K 8644 were strongly inhibited by 100 nM PMA. PMA (0.1–10 μM) inhibited K + -evoked adrenaline and noradrenaline release by 23–44%. The data indicate that phorbol ester-mediated activation of PKC inhibits voltage-sensitive Ca 2+ channels in chromaffin cells, leading to a prominent depression of depolarization-evoked catecholamine secretion.Keywords
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