DETECTING AND QUANTITATING PHYSIOLOGICAL ENDOPLASMIC RETICULUM STRESS

被引:36
作者
Qi, Ling [1 ,2 ]
Yang, Liu [2 ]
Chen, Hui [1 ]
机构
[1] Cornell Univ, Div Nutr Sci, Ithaca, NY 14853 USA
[2] Cornell Univ, Grad Program Biochem Mol & Cell Biol, Ithaca, NY USA
来源
METHODS IN ENZYMOLOGY: UNFOLDED PROTEIN RESPONSE AND CELLULAR STRESS, VOL 490, PT B | 2011年 / 490卷
关键词
UNFOLDED PROTEIN RESPONSE; GLUCOSE-HOMEOSTASIS; TRANSLATIONAL CONTROL; TRANSCRIPTION FACTOR; BETA-CELLS; PHOSPHORYLATION; PATHWAY; OLIGOMERIZATION; MAINTAINS; DISTINCT;
D O I
10.1016/B978-0-12-385114-7.00008-8
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Unfolded protein response (UPR) is a key cellular defense mechanism associated with many human "conformational" diseases, including heart diseases, neurodegeneration, and metabolic syndrome. One of the major obstacles that have hindered our further understanding of physiological UPR and its future therapeutic potential is our inability to detect and quantitate ER stress and UPR activation under physiological and pathological conditions, where ER stress is perceivably very mild. Here, we describe a Phos-tag-based Western blot approach that allows for direct visualization and quantitative assessment of mild ER stress and UPR signaling, directly at the levels of UPR sensors, in various in vivo conditions. This method will likely pave the foundation for future studies on physiological UPR, aid in the diagnosis of ER-associated diseases, and facilitate therapeutic strategies targeting UPR in vivo.
引用
收藏
页码:137 / 146
页数:10
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