Phorbol ester stimulates catecholamine synthesis in isolated bovine adrenal medullary cells

FEBS Letters

Houchi, Hitoshi¹  Uddin, Mir Misbah¹  Ohuchi, Takeshi¹  Oka, Motoo¹  Nakanishi, Atsushi¹ 

[1] Department of Pharmacology, Tokushima University School of Medicine, 3-Kwamoto, Tokushima 770, Japan

关键词: Phorbol ester;    Protein kinase C;    Catecholamine synthesis;    Adrenal medullary cell;   

DOI  :  10.1016/0014-5793(85)80372-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In isolated bovine adrenal medullary cells, the phorbol ester 12-O-tetradecanoyl phorbol 13-acetate (TPA), an activator of protein kinase C, stimulated [¹⁴C]catecholamine synthesis from [¹⁴C]tyrosine, but not from [¹⁴C]DOPA. This stimulatory effect of TPA on [¹⁴C]catecholamine synthesis was not dependent upon extracellular Ca²⁺, and TPA did not affect the uptake of ⁴⁵Ca²⁺ 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 [¹⁴C]catecholamine from [¹⁴C]tyrosine. The stimulatory effect of TPA on [¹⁴C]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.

【 授权许可】

Unknown