SYNERGY BETWEEN PHORBOL ESTERS AND RETINOIC ACID IN INDUCING PROTEIN-KINASE-C ACTIVATION

被引:16
|
作者
BOUZINBASEGARD, H [1 ]
FAN, XT [1 ]
PERDERISET, M [1 ]
CASTAGNA, M [1 ]
机构
[1] HOP PAUL BROUSSE,INSERM,U268,F-94800 VILLEJUIF,FRANCE
关键词
D O I
10.1006/bbrc.1994.2433
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
All-trans retinoic acid (RA) activates brain protein kinase C (PKC) in a unique fashion. Co-factors such as Ca2+ or PtdSer are not required for histone phosphorylation. Binding experiments have provided evidence that RA does not act as a phorbol-ester-like activator. However, phorbol esters synergistically enhance this activation in a dose-dependent manner and increase the reaction rate up to five-fold when combined with 10 mu M RA. Phospholipid-interacting drugs such as phenothiazines and 1-N-(6 aminohexyl) 5-chloro-1-naphtalene-sulfonamide (W7), which compete with PtdSer and inhibit phorbol ester / PtdSer-mediated activation, have potentiating effects on the RA-mediated reaction. RA elicites Ca2+-dependent PKC autophosphorylation. The activation resulting from the combined treatment with PtdSer and RA is more than additive in the presence of Ca2+, indicating that PtdSer-and RA-binding sites are distinct. RA shares several characteristics of activation with sodium deoxycholate and arachidonic acid. These present results suggest that the direct activation of PKC may have physiological and/or pharmacological relevance in the signaling triggered by retinoids. (C) 1994 Academic Press, Inc.
引用
收藏
页码:112 / 119
页数:8
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