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Fatty acid-binding protein

About: Fatty acid-binding protein is a research topic. Over the lifetime, 1721 publications have been published within this topic receiving 81530 citations. The topic is also known as: FABP.


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Journal ArticleDOI
TL;DR: The path of the dietary fatty acids from digestion to their ultimate fate in the cell and critically address their regulatory roles are followed.
Abstract: Structurally defined fatty acid species, which are the straight-chain monounsaturated and polyunsaturated and the branched-chain building blocks of dietary fats and oils, have the potential to regulate lipid metabolism. Focussing on the situation in rodents and in man we describe first the non-enzymic proteins that confer regulatory properties to fatty acids. These are the ligand activated receptors in the nuclei (peroxisome proliferator activated receptors, hepatic nuclear factor 4, liver-X-receptor), sterol regulatory element binding proteins and the soluble and membrane-bound transport proteins for fatty acids and derivatives (fatty acid binding proteins, acyl-CoA binding protein, fatty acid translocator, fatty acid translocator proteins). Then we follow the path of the dietary fatty acids from digestion to their ultimate fate in the cell and critically address their regulatory roles. Fatty acids and/or derivatives interact either directly with enzymes to affect activity, or with the nuclear transcription factors, or affect the stability of mRNAs encoding proteins involved in lipid metabolism. Knowledge of the effects of fatty acid species on the genetic machinery as a whole could become a starting point for individualization of nutritional needs.

29 citations

Journal ArticleDOI
TL;DR: A fatty acid binding protein of low molecular weight was detected in the white heart muscle of ocean pout and the myoglobin-rich heart Muscle of sea raven, but not the glycolytic white skeletal muscle of Ocean pout.
Abstract: A fatty acid binding protein of low molecular weight (12 800) was detected in the white heart muscle of ocean pout (Macrozoarces americanus) and the myoglobin-rich heart muscle of sea raven (Hemitripterus americanus), but not the glycolytic white skeletal muscle of ocean pout. The interaction of isolated ocean pout fatty acid binding protein with potassium [1-14C]palmitate was examined. Data indicate two binding sites for palmitate with an apparent dissociation constant, Kd, of 0.69 ± 0.03 × 10−6 M. The amount of bound palmitate was influenced by pH and by calcium ion concentration.

29 citations

Journal ArticleDOI
TL;DR: A thorough NMR investigation of glycocholate (GCA) binding to human liver fatty acid binding protein found GCA was found to occupy the large internal cavity of hL‐FABP, without requiring major conformational rearrangement of the protein backbone; rather, this led to increased stability, similar to that estimated for the hL-FABp:oleate complex.
Abstract: Human liver fatty acid binding protein (hL-FABP) has been reported to act as an intracellular shuttle of lipid molecules, thus playing a central role in systemic metabolic homeostasis. The involvement of hL-FABP in the transport of bile salts has been postulated but scarcely investigated. Here we describe a thorough NMR investigation of glycocholate (GCA) binding to hL-FABP. The protein molecule bound a single molecule of GCA, in contrast to the 1:2 stoichiometry observed with fatty acids. GCA was found to occupy the large internal cavity of hL-FABP, without requiring major conformational rearrangement of the protein backbone; rather, this led to increased stability, similar to that estimated for the hL-FABP:oleate complex. Fast-timescale dynamics appeared not to be significantly perturbed in the presence of ligands. Slow motions (unlike for other proteins of the family) were retained or enhanced upon binding, consistent with a requirement for structural plasticity for promiscuous recognition.

29 citations

Journal ArticleDOI
TL;DR: An important role for PPARD is highlighted in the homeostasis of ruminant mammary cells by facilitating fatty acid activation and lipid droplet formation and secretion.

29 citations

Journal ArticleDOI
TL;DR: The identification of a potential biomarker for acute in vivo FABP4 inhibition that is applicable for further investigations and can be implemented in simple and fast-flow injection mass spectrometry assays is reported.
Abstract: The fatty acid binding protein 4 (FABP4) belongs to the family of lipid chaperones that control intracellular fluxes and compartmentalization of their respective ligands (e.g., fatty acids). FABP4, which is almost exclusively expressed in adipocytes and macrophages, contributes to the development of insulin resistance and atherosclerosis in mice. Lack of FABP4 protects against the development of insulin resistance associated with genetic or diet-induced obesity in mice. Furthermore, total or macrophage-specific FABP4 deficiency is protective against atherosclerosis in apolipoprotein E-deficient mice. The FABP4 small-molecule inhibitor BMS309403 has demonstrated efficacy in mouse models for type 2 diabetes mellitus and atherosclerosis, resembling phenotypes of mice with FABP4 deficiency. However, despite the therapeutically attractive long-term effects of FABP4 inhibition, an acute biomarker for drug action is lacking. The authors applied mass spectrometry lipidomics analysis to in vitro and in vivo (plasma and adipose tissue) samples upon inhibitor treatment. They report the identification of a potential biomarker for acute in vivo FABP4 inhibition that is applicable for further investigations and can be implemented in simple and fast-flow injection mass spectrometry assays. In addition, this approach can be considered a proof-of-principle study that can be applied to other lipid-pathway targeting mechanisms.

29 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202368
202272
202142
202044
201950
201851