Two fatty acid-binding proteins expressed in the intestine interact differently with endocannabinoids.

NMR chemical shift perturbation endocannabinoid ligand binding affinity endocannabinoids fatty acid ethanolamide fatty acid-binding protein fatty acids fluorescence intestinal FABP liver-type FABP

Journal

Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750

Informations de publication

Date de publication:
07 2020
Historique:
received: 06 01 2020
revised: 08 04 2020
accepted: 12 04 2020
pubmed: 17 4 2020
medline: 16 1 2021
entrez: 17 4 2020
Statut: ppublish

Résumé

Two different members of the fatty acid-binding protein (FABP) family are found in enterocyte cells of the gastrointestinal system, namely liver-type and intestinal fatty acid-binding proteins (LFABP and IFABP, also called FABP1 and FABP2, respectively). Striking phenotypic differences have been observed in knockout mice for either protein, for example, high fat-fed IFABP-null mice remained lean, whereas LFABP-null mice were obese, correlating with differences in food intake. This finding prompted us to investigate the role each protein plays in directing the specificity of binding to ligands involved in appetite regulation, such as fatty acid ethanolamides and related endocannabinoids. We determined the binding affinities for nine structurally related ligands using a fluorescence competition assay, revealing tighter binding to IFABP than LFABP for all ligands tested. We found that the head group of the ligand had more impact on binding affinity than the alkyl chain, with the strongest binding observed for the carboxyl group, followed by the amide, and then the glycerol ester. These trends were confirmed using two-dimensional

Identifiants

pubmed: 32298508
doi: 10.1002/pro.3875
pmc: PMC7314394
doi:

Substances chimiques

Endocannabinoids 0
Fabp1 protein, mouse 0
Fabp2 protein, mouse 0
Fatty Acid-Binding Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

1606-1617

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK038389
Pays : United States
Organisme : NIH HHS
ID : CO6RR015495
Pays : United States
Organisme : NIMHD NIH HHS
ID : G12 MD007603
Pays : United States
Organisme : NIMHD NIH HHS
ID : 5G12-MD007603-30
Pays : United States
Organisme : NCRR NIH HHS
ID : C06 RR015495
Pays : United States
Organisme : NIH HHS
ID : 5R01-DK038389-31
Pays : United States

Informations de copyright

© 2020 The Protein Society.

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Auteurs

May Poh Lai (MP)

Department of Chemistry and Biochemistry, CUNY City College of New York, New York, New York, USA.
Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York (CUNY), New York, New York, USA.
CUNY Institute for Macromolecular Assemblies, New York, New York, USA.

Francine S Katz (FS)

Department of Chemistry and Biochemistry, CUNY City College of New York, New York, New York, USA.
CUNY Institute for Macromolecular Assemblies, New York, New York, USA.

Cédric Bernard (C)

Department of Chemistry and Biochemistry, CUNY City College of New York, New York, New York, USA.
CUNY Institute for Macromolecular Assemblies, New York, New York, USA.

Judith Storch (J)

Department of Nutritional Sciences and Rutgers Center for Lipid Research, School of Environmental and Biological Sciences, Rutgers University, New Brunswick, New Jersey, USA.

Ruth E Stark (RE)

Department of Chemistry and Biochemistry, CUNY City College of New York, New York, New York, USA.
Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York (CUNY), New York, New York, USA.
CUNY Institute for Macromolecular Assemblies, New York, New York, USA.

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Classifications MeSH