Protection of Bcl-2 by salubrinal

被引：31
作者：
Kessel, David [1 ]
机构：
[1] Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA
[2] Wayne State Univ, Sch Med, Dept Med, Detroit, MI 48201 USA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 346卷 / 04期
关键词：
apoptosis; autophagy; Bcl-2; photodynamic; salubrinal; PHOTODAMAGE; APOPTOSIS;
D O I：
10.1016/j.bbrc.2006.06.056
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：
The drug salubrinal has been identified as an inhibitor of phosphatases that act on the eukaryotic translation initiation factor 2 subunit (6IF2 alpha). The resulting maintenance of protein phosphorylation results in enhanced protection from the adverse effects of initiators of the unfolded protein response. We found that salubrinal can also interact with the anti-apoptotic protein Bcl-2, inhibiting binding of the non-peptidic antagonist HA14-1 and of a porphycene that can catalyze Bcl-2 photodamage. As a result, salubrinal offers protection from the apoptotic and autophagic effects that can result from loss of Bcl-2 function. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码：1320 / 1323
页数：4
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