6533b823fe1ef96bd127eaef
RESEARCH PRODUCT
Relationship between signal transduction and PPAR alpha-regulated genes of lipid metabolism in rat hepatic-derived Fao cells.
Motojima KDaniel BoscoboinikBrigitte JanninPatricia PassillyMarie-claude ClémencetMichel DauçaHervé SchohnCherkaoui Malki MNorbert Latruffesubject
Cell signalingBiophysicsPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearBiologyBiochemistryCell LinemedicineAnimalschemistry.chemical_classificationKinaseLipid metabolismCell BiologyGeneral MedicineLipid MetabolismRatschemistryBiochemistryNuclear receptorGene Expression RegulationLiverPeroxisome proliferator-activated receptor alphaCiprofibrateSignal transductionmedicine.drugSignal TransductionTranscription Factorsdescription
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 32P-labeled cell lysates shows that the nuclear receptor, PP-activated receptor, alpha 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-05-02 | Cell biochemistry and biophysics |