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Regulation of intracellular decorin via proteasome degradation in rat mesangial cells

✍ Scribed by Huijuan Wu; Weina Jiang; Yan Zhang; Ye liu; Zhonghua Zhao; Muyi Guo; Duan Ma; Zhigang Zhang

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
381 KB
Volume
111
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

Decorin (DCN) is a member of small leucine‐rich proteoglycan family that neutralizes the bioactivity of transforming growth factor‐beta1 (TGF‐β1). It has been proven to be a promising anti‐fibrotic agent to treat glomerulonephritis. But the underlining mechanism for regulating and degrading intracellular DCN is still not fully understood. In this study, we investigated the roles of ubiquitination in the regulation of cytoplasmic DCN metabolism in rat mesangial cells (MC) by immunoprecipitation and Western blot. The results showed that a proportion of cytoplasmic DCN was ubiquitinated in normal MC and was enhanced in N‐glycosylation inhibitor (tunicamycin)‐treated MC. After being treated with the proteasome inhibitor MG132, ubiquitinated DCN accumulated and displayed a prolonged half‐life, accompanied by decreased TGF‐β1 expression and reduced collagen IV mRNA level in MC. This study demonstrated that the stability and function of cytoplasmic DCN can be regulated by ubiquitin‐proteasome system (UPS) in MC, which implies that regulating the ubiquitination and degradation of DCN might be a novel approach for modulating MC bioactivity. J. Cell. Biochem. 111: 1010–1019, 2010. © 2010 Wiley‐Liss, Inc.

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