The critical role of GRP78 in physiologic and pathologic stress

被引：271

作者：

Pfaffenbach, Kyle T. ^{[1
]}

Lee, Amy S. ^{[1
]}

机构：

[1] Univ So Calif, Keck Sch Med, USC Norris Comprehens Canc Ctr, Dept Biochem & Mol Biol, Los Angeles, CA 90089 USA

来源：

CURRENT OPINION IN CELL BIOLOGY | 2011年 / 23卷 / 02期

基金：

美国国家卫生研究院;

关键词：

ENDOPLASMIC-RETICULUM STRESS; UNFOLDED PROTEIN RESPONSE; PROSTATE-CANCER CELLS; BOX-BINDING PROTEIN-1; COOH-TERMINAL DOMAIN; ER STRESS; CHAPERONE GRP78/BIP; REGULATOR GRP78/BIP; SURFACE GRP78; HEPATIC STEATOSIS;

D O I：

10.1016/j.ceb.2010.09.007

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

GRP78 is a major endoplasmic reticulum chaperone as well as a master regulator of the unfolded protein response. In addition to playing an essential role in early embryonic development, recent studies have emerged specifically implicating GRP78 and chaperone integrity in the aging process and age-related diseases. Another exciting discovery is the regulation of GRP78 by insulin/IGF-1 signaling pathways impacting cell proliferation and survival. Mouse models of cancer, in combination with cell culture studies, validate the critical role of GRP78 in tumorigenesis and tumor angiogenesis. Further, these studies demonstrate the ability of GRP78 to suppress oncogenic PI3K/AKT signaling. The discovery of cell surface GRP78, in cancer cells and cells undergoing ER stress, presents a novel therapeutic strategy.

引用

收藏

页码：150 / 156

页数：7

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