The peroxisome proliferator-activated receptor alpha is a phosphoprotein: regulation by insulin.

Détails

ID Serval
serval:BIB_8C98DFCA45A4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The peroxisome proliferator-activated receptor alpha is a phosphoprotein: regulation by insulin.
Périodique
Endocrinology
Auteur(s)
Shalev A., Siegrist-Kaiser C.A., Yen P.M., Wahli W., Burger A.G., Chin W.W., Meier C.A.
ISSN
0013-7227[print], 0013-7227[linking]
Statut éditorial
Publié
Date de publication
10/1996
Volume
137
Numéro
10
Pages
4499-4502
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Peroxisome proliferator-activated receptors (PPARs) are members of the nuclear hormone receptor superfamily implicated in adipocyte differentiation. The observations that PPAR alpha is a regulator of hepatic lipid metabolism and that the insulin-sensitizing thiazolidinediones are ligands for PPAR gamma suggest that cross-talk might exist between insulin signaling and PPAR activity, possibly through insulin-induced PPAR phosphorylation. Immunoprecipitation of endogenous PPAR alpha from primary rat adipocytes prelabeled with [32P]-orthophosphate and pretreated for 2 h with vanadate and okadaic acid demonstrated for the first time that PPAR alpha is a phosphoprotein in vivo. Treatment with insulin induced a time-dependent increase in PPAR phosphorylation showing a 3-fold increase after 30 min. Insulin also increased the phosphorylation of human PPAR alpha expressed in CV-1 cells. These changes in phosphorylation were paralleled by enhanced transcriptional activity of PPAR alpha and gamma. Transfection studies in CV-1 cells and HepG2 cells revealed a nearly 2-fold increase of PPAR activity in the presence of insulin. In contrast, insulin had no effect on the transcriptional activity of transfected thyroid hormone receptor in CV-1 cells, suggesting a PPAR-specific effect. Thus, insulin stimulates PPAR alpha phosphorylation and enhances the transcriptional activity of PPAR, suggesting that the transcriptional activity of this nuclear hormone receptor might be modulated by insulin-mediated phosphorylation.
Mots-clé
Animals, Cell Line, Humans, Insulin/pharmacology, Phosphoproteins/physiology, Phosphorylation/drug effects, Rats, Rats, Sprague-Dawley, Receptors, Cytoplasmic and Nuclear/genetics, Receptors, Cytoplasmic and Nuclear/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Transcription, Genetic/drug effects
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 17:04
Dernière modification de la notice
08/05/2019 21:46
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