Relationship between signal transduction and PPAR[alpha]-regulated genes of lipid metabolism in rat hepatic-derived Fao cells

• Published in: Cell biochemistry and biophysics Vol. 32; no. 1-3; p. 213
• Main Authors: Latruffe, Norbert, Passilly, Patricia, Jannin, Brigitte, Motojima, Kiyoto, Malki, Mustapha Cherkaoui, Schohn, Hervé, Clemencet, Marie-claude, Boscoboinik, Daniel, Dauça, Michel
• Format: Journal Article
• Language: English
• Published: Totowa Springer Nature B.V 01-04-2000
• Subjects: Kinases; Proteins; Rodents; Signal transduction
• ISSN: 1085-9195; 1559-0283
• DOI: 10.1385/CBB:32:1-3:213

The goal of this study was to characterize phosphorylated proteins and to evaluate the changes in their phosphorylation level under the influence of a peroxisome proliferator (PP) with hypolipidemic activity of the fibrate family. The incubation of rat hepatic derived Fao cells with ciprofibrate leads to an overphosphorylation of proteins, especially one of 85 kDa, indicating that kinase (or phosphatase) activities are modified. Moreover, immunoprecipitation of ^sup 32^P-labeled cell lysates shows that the nuclear receptor, PP-activated receptor, α isoform, can exist in a phosphorylated form, and its phosphorylation is increased by ciprofibrate. This study shows that PP acts at different steps of cell signaling. These steps can modulate gene expression of enzymes involved in fatty acid metabolism and lipid homeostasis, as well as in detoxication processes.[PUBLICATION ABSTRACT]