6533b7d0fe1ef96bd125a5ab

RESEARCH PRODUCT

Vitamin E activates CRABP-II gene expression in cultured human fibroblasts, role of protein kinase C

Amparo GimenoJuan R. ViñaVicente J. MirallesRosa Zaragozá

subject

MaleBisindolylmaleimideTranscription GeneticReceptors Retinoic AcidPhosphatasealpha-TocopherolBiophysicsBiochemistryDephosphorylationchemistry.chemical_compoundStructural BiologyProtein kinase COkadaic AcidGeneticsHumansVitamin ERNA MessengerRetinoic acid bindingPhosphorylationMolecular BiologyProtein kinase CCells CulturedDNA PrimersBase SequenceReverse Transcriptase Polymerase Chain ReactionInfant NewbornRetinoid X receptor αCell BiologyMolecular biologyRetinoic acid receptorCalphostin CchemistryGene Expression RegulationProtein phosphatasePhosphorylationFibroblastCytoplasmic retinoic acid binding protein II

description

The treatment of human fibroblasts with different tocopherols in the presence of retinol caused an increase in cytoplasmic retinoic acid binding protein II (CRABP-II) mRNA and protein. The possibility of an involvement of protein kinase C (PKC) in the response to tocopherols was supported by the results obtained with the PKC-specific inhibitors, calphostin C and bisindolylmaleimide I. The effect of alpha-tocopherol was prevented by okadaic acid, suggesting that a protein phosphatase is responsible for PKC dephosphorylation produced by the presence of tocopherols. The results shown support the hypothesis that phosphorylation/dephosphorylation of RXRalpha via PKC may be involved in the regulation of CRABP-II gene expression.

yearjournalcountryeditionlanguage
2004-06-15FEBS Letters
10.1016/j.febslet.2004.05.073http://dx.doi.org/10.1016/j.febslet.2004.05.073