ArticleProtein science : a publication of the Protein Society2020
Two fatty acid-binding proteins expressed in the intestine interact differently with endocannabinoids.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Tissue-Specific Ablation of Liver Fatty Acid-Binding Protein Induces a Metabolically Healthy Obese Phenotype in Female Mice.bioRxiv : the preprint server for biology · 2025Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein 1 (FABP1) and FABP1 Binding Alters Drug Metabolism.Molecular pharmacology · 2024Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.bioRxiv : the preprint server for biology · 2024Article
- The Multifunctional Family of Mammalian Fatty Acid-Binding Proteins.Annual review of nutrition · 2023Review
- The proximal intestinal Fatty Acid-Binding Proteins liver FABP (LFABP) and intestinal FABP (IFABP) differentially modulate whole body energy homeostasis but are not centrally involved in net dietary lipid absorption: Studies of the LFABP/IFABP double knockout mouse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023Article
- Mechanisms of endocannabinoid transport in the brain.British journal of pharmacology · 2022Review
- Gut Microbiota and Phenotypic Changes Induced by Ablation of Liver- and Intestinal-Type Fatty Acid-Binding Proteins.Nutrients · 2022Article
- Two fatty acid-binding proteins expressed in the intestine interact differently with endocannabinoids.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
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
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.