Caspases involved in ER stress-mediated cell death

被引：175

作者：

Momoi, T

机构：

[1] NCNP, Natl Inst Neurosci, Div Dev, Tokyo 1878502, Japan

[2] NCNP, Natl Inst Neurosci, Div Differentiat, Tokyo 1878502, Japan

来源：

JOURNAL OF CHEMICAL NEUROANATOMY | 2004年 / 28卷 / 1-2期

关键词：

endoplasmic reticulum; unfolded protein response; apoptosis;

D O I：

10.1016/j.jchemneu.2004.05.008

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：

Caspases are cysteine proteases involved in apoptotic pathways. Excess endoplasmic reticulum (ER) stress, induced by the accumulation of unfolded or malfolded proteins, activates various apoptotic pathways. Crosstalk between the mitochondria and ER plays an essential role in ER stress-mediated cell death. The cytochrome c-dependent apoptotic pathway is activated by ER stress. On the other hand, caspase-12, which is located at the ER, is also activated by excess ER stress and results in cell death in the absence of the cytochrome c-dependent pathway. The predominant apoptotic pathway may differ among cell type and differentiation stage. (C) 2004 Elsevier B.V. All rights reserved.

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页码：101 / 105

页数：5

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