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PKCα is involved in phorbol ester TPA-mediated stabilization of p14ARF

被引：8
作者：
Inoue, R
Shiraishi, T
机构：
[1] Mie Univ, Sch Med, Dept Pathol 2, Tsu, Mie 5148507, Japan
[2] Mie Univ Hosp, Dept Cent Supplies, Tsu, Mie 5148507, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 330卷 / 04期
关键词：
p(14ARF); protein stability; TPA; PKC; p53;
D O I：
10.1016/j.bbrc.2005.03.117
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要：
We generated A21-13 cells expressing p14(ARF) in the presence of doxycycline in order to examine the stability of p14(ARF) protein. The effects of proteasome inhibitor MG132 on p14(ARF) protein stabilization were detectable using our experimental procedure. Introduction of mutant p53 did not affect MG132-mediated p14(ARF) protein stabilization. We found that phorbol ester TPA (12-o-tetradecanoyl-phorbol 13-acetate) stabilized p14(ARF) protein and that p53 status had no effect on TPA-mediated stabilization. TPA-mediated stabilization was abolished by staurosporine but not by lovastatin or U0126. We further investigated which isoforms of PKC were involved in TPA-mediated p14(ARF) stabilization using short-interference RNA. Knockdown of PKC alpha, but not PKC delta, attenuated TPA-mediated p14(ARF) stabilization. These findings suggest that PKC alpha is involved in TPA-mediated stabilization of p14(ARF) protein, and this effect of TPA was not affected by the Ras/MAPK pathway or p53 status. Our results are indicative of a novel role of PKC in p14(ARF) protein stability. (c) 2005 Elsevier Inc. All rights reserved.
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页码：1314 / 1318
页数：5
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