[HTML][HTML] In vivo stabilization of nuclear retinoid X receptor α in the presence of peroxisome proliferator-activated receptor α

N Tanaka, K Hora, H Makishima, Y Kamijo, K Kiyosawa… - FEBS letters, 2003 - Elsevier
N Tanaka, K Hora, H Makishima, Y Kamijo, K Kiyosawa, FJ Gonzalez, T Aoyama
FEBS letters, 2003Elsevier
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 …
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.
Elsevier