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The Molecular Chaperone Apolipoprotein J/Clusterin as a Sensor of Oxidative Stress: Implications in Therapeutic Approaches - A Mini-Review
Author(s) -
Ioannis P. Trougakos
Publication year - 2013
Publication title -
gerontology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.397
H-Index - 94
eISSN - 1423-0003
pISSN - 0304-324X
DOI - 10.1159/000351207
Subject(s) - clusterin , proteostasis , biology , proteome , microbiology and biotechnology , chaperone (clinical) , oxidative stress , carcinogenesis , neurodegeneration , heat shock protein , proteomics , gene , bioinformatics , genetics , biochemistry , medicine , apoptosis , disease , pathology
Organisms are constantly exposed to physiological and environmental stresses and therefore require an efficient surveillance of genome and proteome quality in order to prevent disruption of homeostasis. Central to the intra- and extracellular proteome surveillance system are the molecular chaperones that contribute to both proteome maintenance and clearance. The conventional protein product of the apolipoprotein J/clusterin (CLU) gene is a heterodimeric secreted glycoprotein (also termed as sCLU) with a ubiquitous expression in human tissues. CLU exerts a small heat shock protein-like stress-induced chaperone activity and has been functionally implicated in numerous physiological processes as well as in ageing and most age-related diseases including tumorigenesis, neurodegeneration, and cardiovascular and metabolic syndromes.

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