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Phorbol ester stimulates catecholamine synthesis in isolated bovine adrenal medullary cells
Author(s) -
Houchi Hitoshi,
Nakanishi Atsushi,
Uddin Mir Misbah,
Ohuchi Takeshi,
Oka Motoo
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80372-0
Subject(s) - phorbol ester , catecholamine , chemistry , medullary cavity , endocrinology , medicine , phorbol , protein kinase c , biochemistry , biology , signal transduction
In isolated bovine adrenal medullary cells, the phorbol ester 12‐ O ‐tetradecanoyl phorbol 13‐acetate (TPA), an activator of protein kinase C, stimulated [ 14 C]catecholamine synthesis from [ 14 C]tyrosine, but not from [ 14 C]DOPA. This stimulatory effect of TPA on [ 14 C]catecholamine synthesis was not dependent upon extracellular Ca 2+ , and TPA did not affect the uptake of 45 Ca 2+ or the release of catecholamine by the cells. TPA also did not affect the intracellular cyclic AMP (cAMP) level. 4α‐Phorbol 12,13‐didecanoate, which is not an activator of protein kinase C, did not stimulate the synthesis of [ 14 C]catecholamine from [ 14 C]tyrosine. The stimulatory effect of TPA on [ 14 C]catecholamine synthesis was additive with that of carbamylcholine, but not with that of dibutyryl cAMP (DB‐cAMP). From these results, it was suggested that protein kinase C is involved in the regulation of tyrosine hydroxylase activity and that this regulatory mechanism might be similar to that involving cAMP.