In vivo stabilization of nuclear retinoid X receptor α in the presence of peroxisome proliferator‐activated receptor α

FEBS Letters

Gonzalez, Frank J.¹  Hora, Kazuhiko³  Tanaka, Naoki²  Kamijo, Yuji²  Makishima, Hideki³  Kiyosawa, Kendo³  Aoyama, Toshifumi² 

[1] Laboratory of Metabolism, National Cancer Institute, Bethesda, MD 20892, USA;Department of Aging Biochemistry, Research Center on Aging and Adaptation, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto 390-8621, Japan;Second Department of Internal Medicine, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto 390-8621, Japan

关键词: Retinoid X receptor α;    Peroxisome proliferator-activated receptor α;    Heterodimer;    Stabilization;    CRBPII;    cellular retinol-binding protein II;    DMSO;    dimethyl sulfoxide;    PPAR;    peroxisome proliferator-activated receptor;    PT;    peroxisomal thiolase;    RXR;    retinoid X receptor;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(03)00423-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Retinoid X receptor α (RXRα) can reveal diverse functions through forming a heterodimer with peroxisome proliferator-activated receptor α (PPARα). However, the mechanism of regulation of the cellular RXRα level is unclear. Thus, quantitative change of RXRα was investigated in mouse liver. Nuclear RXRα level was constitutively lower in PPARα-null mice than in wild-type mice. The level was also increased by clofibrate treatment in wild-type mice without a concomitant increase of RXRα mRNA, but not in PPARα-null mice. Pulse chase experiments demonstrated that the presence of PPARα and its activation by ligands significantly affected the stability of nuclear RXRα. These findings suggest a novel regulatory mechanism of nuclear RXRα in vivo.

【 授权许可】

Unknown