A Phos-Tag-Based Approach Reveals the Extent of Physiological Endoplasmic Reticulum Stress

被引：63

作者：

Yang, Liu ^{[1
]}

Xue, Zhen ^{[2
]}

He, Yin ^{[3
]}

Sun, Shengyi ^{[1
]}

Chen, Hui ^{[4
]}

Qi, Ling ^{[1
,2
,3
,4
]}

机构：

[1] Cornell Univ, Grad Program Biochem Mol & Cell Biol, Ithaca, NY 14853 USA

[2] Cornell Univ, Grad Program Nutr, Ithaca, NY USA

[3] Cornell Univ, Grad Program Genet & Dev, Ithaca, NY USA

[4] Cornell Univ, Div Nutr Sci, Ithaca, NY USA

来源：

PLOS ONE | 2010年 / 5卷 / 07期

关键词：

UNFOLDED PROTEIN RESPONSE; TRANSMEMBRANE PROTEIN; CELL; ER; PANCREAS; KINASE; DEFICIENCY; INDUCTION; TRANSPORT; DISTINCT;

D O I：

10.1371/journal.pone.0011621

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Cellular response to endoplasmic reticulum (ER) stress or unfolded protein response (UPR) is a key defense mechanism associated with many human diseases. Despite its basic and clinical importance, the extent of ER stress inflicted by physiological and pathophysiological conditions remains difficult to quantitate, posing a huge obstacle that has hindered our further understanding of physiological UPR and its future therapeutic potential. Here we have optimized a Phos-tag-based system to detect the activation status of two proximal UPR sensors at the ER membrane. This method allowed for a quantitative assessment of the level of stress in the ER. Our data revealed quantitatively the extent of tissue-specific basal ER stress as well as ER stress caused by the accumulation of misfolded proteins and the fasting-refeeding cycle. Our study may pave the foundation for future studies on physiological UPR, aid in the diagnosis of ER-associated diseases and improve and facilitate therapeutic strategies targeting UPR in vivo.

引用

页数：7

共 32 条

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