Tocopherol-binding proteins: their function and physiological significance.

Abstract

The present review is a continuation of earlier essays on the uptake mechanisms and the biological function of vitamin E. There are eight naturally occurring homologues of vitamin E, which differ in their structure and in biological activity in vivo and in vitro. Various studies have suggested that after normal gastrointestinal absorption of dietary vitamin E specific mechanisms favor the preferential accumulation of one of its homologues, alpha-tocopherol, in the human body. This process is thought to be mediated in part by the alpha-tocopherol transfer protein (alpha-TTP) in the liver cytoplasm. The mechanism and pathway by which alpha-TTP specifically incorporates alpha-tocopherol into plasma lipoproteins is not yet fully understood. Because alpha-tocopherol is widely distributed in tissues in various concentrations but alpha-TTP resides only in liver, its role as intracellular carrier of alpha-tocopherol seems unlikely. However, recent data indicate that a system of alpha-tocopherol-binding proteins is involved in these processes that favor the localization of alpha-tocopherol at the sites where it is required. The current status of the evidence for the regulation of alpha-tocopherol levels and their impact on cellular signaling is discussed.

Cite this paper

@article{Stocker2000TocopherolbindingPT, title={Tocopherol-binding proteins: their function and physiological significance.}, author={Achim Stocker and Angelo Azzi}, journal={Antioxidants & redox signaling}, year={2000}, volume={2 3}, pages={397-404} }