Dikshit, P and Jana, NR (2007) The co-chaperone CHIP is induced in various stresses and confers protection to cells. Biochemical and Biophysical Research Communications, 357 (3). pp. 761-765.

Text 1-s2.0-S0006291X07007176-main.pdf Restricted to Repository staff only Download (306Kb) | Request a copy

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.

Item Type:	Article
Subjects:	Neurodegenerative Disorders Neuro-Oncological Disorders Neurocognitive Processes Neuronal Development and Regeneration Informatics and Imaging Genetics and Molecular Biology
Depositing User:	Dr. D.D. Lal
Date Deposited:	10 Feb 2020 08:56
Last Modified:	10 Feb 2020 08:56
URI:	http://nbrc.sciencecentral.in/id/eprint/571

Actions (login required)

View Item