CD36 signaling inhibits the translation of heat shock protein 70 induced by oxidized low density lipoprotein through activation of peroxisome proliferators-activated receptor gamma.

Experimental & Molecular Medicine
Kyoung Jin LeeJang Hee Hahn

Abstract

Oxidized LDL (OxLDL), a causal factor in atherosclerosis, induces the expression of heat shock proteins (Hsp) in a variety of cells. In this study, we investigated the role of CD36, an OxLDL receptor, and peroxisome proliferator-activated receptor gamma (PPARgamma) in OxLDL-induced Hsp70 expression. Overexpression of dominant-negative forms of CD36 or knockdown of CD36 by siRNA transfection increased OxLDL-induced Hsp70 protein expression in human monocytic U937 cells, suggesting that CD36 signaling inhibits Hsp70 expression. Similar results were obtained by the inhibition of PPARgamma activity or knockdown of PPARgamma expression. In contrast, overexpression of CD36, which is induced by treatment of MCF-7 cells with troglitazone, decreased Hsp70 protein expression induced by OxLDL. Interestingly, activation of PPARgamma through a synthetic ligand, ciglitazone or troglitazone, decreased the expression levels of Hsp70 protein in OxLDL-treated U937 cells. However, major changes in Hsp70 mRNA levels were not observed. Cycloheximide studies demonstrate that troglitazone attenuates Hsp70 translation but not Hsp70 protein stability. PPARgamma siRNA transfection reversed the inhibitory effects of troglitazone on Hsp70 translation. The...Continue Reading

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Citations

Nov 8, 2011·American Journal of Physiology. Heart and Circulatory Physiology·Qingbo XuKaushik Mandal
Nov 6, 2009·Experimental & Molecular Medicine·Joung-Woo Hong, Kye Won Park
Apr 4, 2009·The Journal of Immunology : Official Journal of the American Association of Immunologists·Denise L CecilRobert Terkeltaub

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