Vitamin E intestinal absorption: Regulation of membrane transport across the enterocyte.


Journal

IUBMB life
ISSN: 1521-6551
Titre abrégé: IUBMB Life
Pays: England
ID NLM: 100888706

Informations de publication

Date de publication:
04 2019
Historique:
received: 11 07 2018
revised: 28 08 2018
accepted: 31 08 2018
pubmed: 12 10 2018
medline: 25 1 2020
entrez: 12 10 2018
Statut: ppublish

Résumé

Vitamin E is an essential molecule for our development and health. It has long been thought that it was absorbed and transported through cellular membranes by a passive diffusion process. However, data obtained during the past 15 years showed that its absorption is actually mediated, at least in part, by cholesterol membrane transporters including the scavenger receptor class B type I (SR-BI), CD36 molecule (CD36), NPC1-like transporter 1 (NPC1L1), and ATP-binding cassettes A1 and G1 (ABCA1 and ABCG1). This review focuses on the absorption process of vitamin E across the enterocyte. A special attention is given to the regulation of this process, including the possible competition with other fat-soluble micronutrients, and the modulation of transporter expressions. Overall, recent results noticeably increased the comprehension of vitamin E intestinal transport, but additional investigations are still required to fully appreciate the mechanisms governing vitamin E bioavailability. © 2018 IUBMB Life, 71(4):416-423, 2019.

Identifiants

pubmed: 30308094
doi: 10.1002/iub.1955
doi:

Substances chimiques

ABCG1 protein, human 0
ATP Binding Cassette Transporter, Subfamily G, Member 1 0
ATP-Binding Cassette Transporters 0
CD36 Antigens 0
Chylomicrons 0
Membrane Transport Proteins 0
NPC1L1 protein, human 0
Vitamin E 1406-18-4

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

416-423

Informations de copyright

© 2018 International Union of Biochemistry and Molecular Biology.

Auteurs

Emmanuelle Reboul (E)

Aix Marseille Univ, INSERM, INRA, C2VN, Marseille, France.

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Classifications MeSH