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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: Blood-borne fatty acids are delivered to muscle bound to albumin or from triacylglycerols in chylomicrons and very-low-density lipoproteins after hydrolysis by lipoprotein lipase.
Abstract: Fatty acids form the major fuels for energy production of working heart and of skeletal muscle at rest and during moderate and prolonged exercise. Only a small proportion of fatty acids taken up by muscle is used for anabolic processes such as triacylglycerol and phospholipid synthesis, in contrast to adipose tissue and liver. Blood-borne fatty acids are delivered to muscle bound to albumin or from triacylglycerols in chylomicrons and very-low-density lipoproteins after hydrolysis by lipoprotein lipase. The fatty acids are very effectively extracted by the heart from blood, 40-60% during one transmit time (Opie et al., 1973), although they have to pass many barriers and compartments to reach the myocyte mitochondrion, where their main utilization (oxidation) takes place (Fig. I ) . Endothelial cells lining the intravascular space have to extract and transfer the fatty

28 citations

Journal ArticleDOI
TL;DR: Comparing the rates and mechanisms of ligand transfer from the proteins to artificial phospholipid vesicles using a fluorescence resonance energy transfer assay suggest that Sj-FABPc is most likely to be involved in the intracellular targeted transport and metabolism of fatty acids, whereas Ov-FAR-1 and ABA-1A1 may behave in a manner analogous to that of extracellular LBPs such as serum albumin and plasma retinol binding protein.
Abstract: Three different classes of small lipid-binding protein (LBP) are found in helminth parasites. Although of similar size, the ABA-1A1 (also designated As-NPA-A1) and Ov-FAR-1 (formerly known as Ov20) proteins of nematodes are mainly α-helical and have no known structural counterparts in mammals, whereas Sj-FABPc of schistosomes is predicted to form a β-barrel structure similar to the mammalian family of intracellular fatty acid binding proteins. The parasites that produce these proteins are unable to synthesize their own complex lipids and, instead, rely entirely upon their hosts for supply. As a first step in elucidating whether these helminth proteins are involved in the acquisition of host lipid, the process by which these LBPs deliver their ligands to acceptor membranes was examined, by comparing the rates and mechanisms of ligand transfer from the proteins to artificial phospholipid vesicles using a fluorescence resonance energy transfer assay. All three proteins bound the fluorescent fatty acid 2-(9-a...

28 citations

Journal ArticleDOI
TL;DR: A fatty acid‐binding protein was purified from male rat kidney and identified as α2U‐globulin, which is the major male‐specific protein in rat urine, suggesting that the protein has been proteolytically processed in the kidney.

28 citations

Journal ArticleDOI
TL;DR: When a 100,000 x g supernatant from rat intestinal mucosa was incubated with 4,4'-bis([3H]methylsulfonyl)-2,2',5,5'-tetrachlorobiphenyl, a (CT3SO2)2TCB-protein complex was formed and was isolate and purified using gel filtration and ion-exchange chromatography.

28 citations

Journal ArticleDOI
TL;DR: The results identify FABP4 as a molecule involved in diabetic/lipid-induced cardiomyopathy and indicate that this molecule may be an emerging biomarker for diabetic carduomyopathy-related disturbances, such as myocardial neutral lipid accumulation.
Abstract: Objective Fatty acid binding protein 4 (FABP4) is an intracellular lipid chaperone involved in the crosstalk between adipose and peripheral tissues, and it contributes to widespread insulin resistance in cells, including cardiac cells. However, the role of this adipokine in regulating cardiac metabolism and myocardial neutral lipid content in patients with type 2 diabetes has not been elucidated. Methods The impact of circulating FABP4 on the cardiac neutral lipid content was measured by proton magnetic resonance spectroscopy (1H-MRS) in patients with type 2 diabetes. Additionally, circulating FABP4 and the cardiac triglyceride content were analysed in high-fat diet (HFD)-fed mice, and the impact of the exogenous FABP4 was explored in HL-1 cardiac cells. Results Serum FABP4 levels were higher in type 2 diabetic patients compared to healthy individuals. Circulating FABP4 levels were associated with myocardial neutral lipid content in type 2 diabetic patients. In HFD-fed mice, both serum FABP4 and myocardial triglyceride content were increased. In FABP4-challenged HL-1 cells, extracellular FABP4 increased intracellular lipid accumulation, which led to impairment of the insulin-signalling pathway and reduced insulin-stimulated glucose uptake. However, these effects were partially reversed by FABP4 inhibition with BMS309403, which attenuated the intracellular lipid content and improved insulin signalling and insulin-stimulated glucose uptake. Conclusions Taken together, our results identify FABP4 as a molecule involved in diabetic/lipid-induced cardiomyopathy and indicate that this molecule may be an emerging biomarker for diabetic cardiomyopathy-related disturbances, such as myocardial neutral lipid accumulation. Additionally, FABP4 inhibition may be a potential therapeutic target for metabolic-related cardiac dysfunctions.

28 citations


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