Tocopherol-binding proteins: their function and physiological significance.

Stocker, Achim; Azzi, Angelo (2000). Tocopherol-binding proteins: their function and physiological significance. Antioxidants & redox signalling, 2(3), pp. 397-404. Mary Ann Liebert 10.1089/15230860050192170

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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.

Item Type:

Journal Article (Review Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Stocker, Achim and Azzi, Angelo

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

1523-0864

Publisher:

Mary Ann Liebert

Language:

English

Submitter:

Anja Ebeling

Date Deposited:

11 Mar 2020 16:33

Last Modified:

11 Mar 2020 16:43

Publisher DOI:

10.1089/15230860050192170

PubMed ID:

11229353

BORIS DOI:

10.7892/boris.141814

URI:

https://boris.unibe.ch/id/eprint/141814

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