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Vitamin E activates CRABP‐II gene expression in cultured human fibroblasts, role of protein kinase C
Author(s) -
Gimeno Amparo,
Zaragozá Rosa,
Viña Juan R,
Miralles Vicente J
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.073
Subject(s) - protein kinase c , bisindolylmaleimide , dephosphorylation , retinoic acid , calphostin c , calphostin , okadaic acid , protein kinase a , phosphorylation , kinase , chemistry , phosphatase , biology , biochemistry , microbiology and biotechnology , gene
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 α‐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 RXRα via PKC may be involved in the regulation of CRABP‐II gene expression.