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

FEBS Lett. 2004 Jul 2;569(1-3):240-4. doi: 10.1016/j.febslet.2004.05.073.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cells, Cultured
  • DNA Primers
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology
  • Humans
  • Infant, Newborn
  • Male
  • Okadaic Acid / pharmacology
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • RNA, Messenger / genetics
  • Receptors, Retinoic Acid / genetics*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transcription, Genetic / drug effects
  • Vitamin E / pharmacology*
  • alpha-Tocopherol / pharmacology


  • DNA Primers
  • RNA, Messenger
  • Receptors, Retinoic Acid
  • retinoic acid binding protein II, cellular
  • Vitamin E
  • Okadaic Acid
  • Protein Kinase C
  • alpha-Tocopherol