Nonantioxidant functions of alpha-tocopherol in smooth muscle cells

J Nutr. 2001 Feb;131(2):378S-81S. doi: 10.1093/jn/131.2.378S.


Most tocopherols and tocotrienols, with the exception of alpha-tocopherol, are not retained by humans. This suggests that alpha-tocopherol is recognized uniquely; therefore, it may exert an exclusive function. alpha-Tocopherol possesses distinct properties that are independent of its prooxidant, antioxidant or radical-scavenging ability. alpha-Tocopherol specifically inhibits protein kinase C, the growth of certain cells and the transcription of the CD36 and collagenase genes. Activation events have also been seen on the protein phosphatase 2A (PP(2)A) and on the expression of other genes (alpha-tropomyosin and connective tissue growth factor). Neither ss-tocopherol nor probucol possessed the same specialty functions as alpha-tocopherol. Recently, we isolated a new ubiquitous cytosolic alpha-tocopherol binding protein (TAP). Its motifs suggest that it is a member of the hydrophobic ligand-binding protein family (CRAL-TRIO). TAP may also be involved in the regulation of cellular alpha-tocopherol concentration and alpha-tocopherol-mediated signaling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cells, Cultured
  • Gene Expression Regulation / drug effects
  • Humans
  • Muscle, Smooth / drug effects*
  • Muscle, Smooth / physiology
  • Phosphoprotein Phosphatases
  • Protein Kinase C / antagonists & inhibitors
  • Protein Phosphatase 2
  • Protein Processing, Post-Translational
  • Transcription, Genetic / drug effects
  • Vitamin E / pharmacology*
  • Vitamin E / physiology*


  • Vitamin E
  • Protein Kinase C
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 2