Exp Mol Med.  2004 Oct;36(5):499-503.

Age-related decline in expression of calnexin

Affiliations
  • 1Department of Biochemistry, Chonbuk National University Medical School, Jeonju 561-756, Korea. jsukim@chonbuk.ac.kr

Abstract

Aging is accompanied by the changes in the cells that decrease their capacity to respond to various forms of stress. Cells are known to respond to stresses through expression of stress- response proteins, heat-shock proteins composed of molecular chaperones. Recent studies suggest that chaperone level and stress-induced chaperone expression could decrease with aging. The aim of the present study is to identify chaperones that show a significant change in protein expression with aging. We used an in vitro aging model system of human diploid fibroblasts (HDF). Proteome analysis of HDF showed that endoplasmic reticulum (ER) chaperone, calnexin, significantly decreased with aging. Oxidative stress-induced expression of calnexin also attenuated in old HDF compared to young cells. These findings suggest calnexin decreases with aging and might contribute to a cytoprotection in a variety of human age-related diseases.

Keyword

Calnexin; Chaperone; Heat shock protein; Proteomics; Senescence

MeSH Terms

Calnexin/analysis/*metabolism
*Cell Aging
Cells, Cultured
Down-Regulation
Endoplasmic Reticulum/metabolism
Fibroblasts/metabolism
Humans
Molecular Chaperones/analysis/*metabolism
Oxidative Stress/*physiology
Proteomics
Research Support, Non-U.S. Gov't
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