Retinol-binding protein 2 (RBP2): More than just dietary retinoid uptake.

2-monoacylglycerol All-trans-retinoic acid CRBP2 Cellular retinol-binding protein 2 Glucose-dependent insulinotropic polypeptide (GIP) Incretin Obesity RBP2 Retinoids Retinol-binding proteins Vitamin A

Journal

Biochimica et biophysica acta. Molecular and cell biology of lipids
ISSN: 1879-2618
Titre abrégé: Biochim Biophys Acta Mol Cell Biol Lipids
Pays: Netherlands
ID NLM: 101731727

Informations de publication

Date de publication:
08 2022
Historique:
received: 28 12 2021
revised: 28 03 2022
accepted: 22 04 2022
pubmed: 10 5 2022
medline: 3 6 2022
entrez: 9 5 2022
Statut: ppublish

Résumé

Retinol-binding protein 2 (RBP2, also known as cellular retinol-binding protein 2 (CRBP2)) is a member of the fatty acid-binding protein family and has been extensively studied for its role in facilitating dietary vitamin A (retinol) uptake and metabolism within enterocytes of the small intestine. RBP2 is present in highest concentrations in the proximal small intestine where it constitutes approximately 0.1-0.5% of soluble protein. Recent reports have established that RBP2 binds monoacylglycerols (MAGs) with high affinity, including the canonical endocannabinoid 2-arachidonoylglycerol (2-AG). Crystallographic studies reveal that retinol, 2-AG, or other long-chain MAGs alternatively can bind in the retinol-binding pocket of RBP2. It also has been demonstrated recently that Rbp2-deficient mice are more susceptible to developing obesity and associated metabolic phenotypes when exposed to a high fat diet, or as they age when fed a conventional chow diet. When subjected to an oral fat challenge, the Rbp2-deficient mice release into the circulation significantly more, compared to littermate controls, of the intestinal hormone glucose-dependent insulinotropic polypeptide (GIP). These new findings regarding RBP2 structure and actions within the intestine are the focus of this review.

Identifiants

pubmed: 35533980
pii: S1388-1981(22)00069-5
doi: 10.1016/j.bbalip.2022.159179
pmc: PMC9191623
mid: NIHMS1811154
pii:
doi:

Substances chimiques

Monoglycerides 0
Retinoids 0
Retinol-Binding Proteins, Cellular 0
Vitamin A 11103-57-4

Types de publication

Journal Article Review Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

159179

Subventions

Organisme : NIAAA NIH HHS
ID : R21 AA028110
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK132710
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY023948
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK122071
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK068437
Pays : United States

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.

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Auteurs

Jacqueline Plau (J)

Department of Pharmacology and Cleveland Center for Membrane and Structural Biology, Case Western Reserve University, Cleveland, OH, United States of America.

Marcin Golczak (M)

Department of Pharmacology and Cleveland Center for Membrane and Structural Biology, Case Western Reserve University, Cleveland, OH, United States of America.

Jisun Paik (J)

Department of Comparative Medicine, University of Washington, Seattle, WA, United States of America.

Rossana M Calderon (RM)

Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY, United States of America.

William S Blaner (WS)

Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY, United States of America. Electronic address: wsb2@columbia.edu.

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