Relationship between signal transduction and PPAR alpha-regulated genes of lipid metabolism in rat hepatic-derived Fao cells.
Cell Biochem Biophys
; 32 Spring: 213-20, 2000.
Article
em En
| MEDLINE
| ID: mdl-11330049
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Fatores de Transcrição
/
Receptores Citoplasmáticos e Nucleares
/
Metabolismo dos Lipídeos
/
Fígado
Limite:
Animals
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article