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The co-chaperone CHIP is induced in various stresses and confers protection to cells.

Abstract：

:The C-terminus of Hsp70 interacting protein (CHIP) is being considered to be a cellular quality control E3 ubiquitin ligase because of its ability to degrade misfolded proteins in association with heat shock chaperones. The neuroprotective role of CHIP also has been implicated in several familial neurodegenerative diseases including polyglutamine diseases. However, the regulation of the expression of CHIP under different stress conditions and its protective role thereon is unknown. Here we have shown that the mRNA level of CHIP is significantly increased in the cells exposed to oxidative, endoplasmic reticulum and proteasomal stress. CHIP also protected from various stress-induced cell death. Finally, we have demonstrated upregulation of CHIP mRNA levels in the expanded polyglutamine protein expressing cells. Our result suggests that the upregulation of CHIP under various stress environments is an adaptive response of the cells to deal with the excess burden of misfolded protein.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Dikshit P,Jana NR

doi

10.1016/j.bbrc.2007.04.018

subject

Has Abstract

pub_date

2007-06-08 00:00:00

pages

761-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00717-6

journal_volume

357

pub_type

杂志文章

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