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J. Lipid Res.
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A more recent version of this article appeared on January 1, 2006

Papers In Press, published online ahead of print October 17, 2005
J. Lipid Res., doi:10.1194/jlr.M500170-JLR200
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Submitted on May 2, 2005
Revised on September 26, 2005
Accepted on October 17, 2005

Adipose differentiation-related protein is degraded through the proteasome-dependent pathway during regression of lipid-storing cells

Yutaka Masuda, Hiroyuki Itabe, Miho Odaki, Kotaro Hama, Yasuyuki Fujimoto, Masahiro Mori, Naoko Sasabe, Junken Aoki, Hiroyuki Arai, and Tatsuya Takano

Department of Biological Chemistry, Showa University School of Pharmaceutical Sciences, Tokyo 142-8555

Corresponding Author: h-itabe{at}pharm.showa-u.ac.jp

Lipid droplets appear in the cytoplasmic space when massive amounts of neutral lipids accumulate in cells. Adipose differentiation-related protein (ADRP) is a major protein associated with the lipid droplets in various types of cells, including macrophage-derived foam cells and lipid-laden liver cells. However, the role of ADRP in the processes of formation and regression of these cells has not been fully elucidated. When J774 murine macrophages were incubated for 3 days with very low-density lipoprotein (VLDL), their content of ADRP and triacylglycerol (TG) increased 3- and 4-fold, respectively. Addition of oleic acid to the macrophages also increased the contents of ADRP and TG, suggesting the ADRP induction was not dependent on lipoproteins. Induction of ADRP during TG accumulation was not specific for macrophages, since HuH-7 human liver cells increased ADRP upon incubation with oleic acid. VLDL-induced foam cells were treated with triacsin C, a potent inhibitor of acyl-CoA synthase, for 6 h. As the amount of TG decreased in the foam cells, the amount of ADRP protein decreased in parallel. The amount of ADRP in the liver cells pretreated with oleic acid also decreased by addition of triacsin C, indicating the amount of ADRP reduced during regression of the lipid-storing cells. This ADRP decrease was abolished by co-incubation with a proteasome inhibitor. An immunoprecipitation experiment showed that there was accumulation of poly-ubiquitinated ADRP in the presence of a proteasome inhibitor. In addition, the proteasome inhibitor reversed not only the degradation of ADRP but also TG reduction by triacsin C in HuH-7 cells. These results demonstrated a close correlation between the amount of ADRP in cells and their lipid content, and suggest that the ubiquitin-proteasome system is involved in degradation of ADRP during regression of lipid-storing cells.


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