scholarly journals Small lipid-binding proteins in regulating endothelial and vascular functions: focusing on adipocyte fatty acid binding protein and lipocalin-2

2012 ◽  
Vol 165 (3) ◽  
pp. 603-621 ◽  
Author(s):  
Yu Wang
Keyword(s):  
Fatty Acid ◽  
Binding Proteins ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Lipid Binding ◽  
Lipocalin 2 ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Lipid Binding Proteins

scholarly journals Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode

2019 ◽  
Vol 39 (7) ◽  
Author(s):  
Marina Ibáñez-Shimabukuro ◽  
M. Florencia Rey-Burusco ◽  
Mads Gabrielsen ◽  
Gisela R. Franchini ◽  
Alan Riboldi-Tunnicliffe ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Binding Proteins ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Structural Features ◽  
Lipid Binding ◽  
Head Group ◽  
Resonance Spectroscopy ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

AbstractIntracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid ligand in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes.

scholarly journals The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein

1996 ◽  
Vol 320 (3) ◽  
pp. 729-733 ◽  
Author(s):  
Alfred E. A. THUMSER ◽  
David C. WILTON
Keyword(s):  
Fatty Acid ◽  
Bile Salts ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Physiological Role ◽  
Lipid Binding ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Wide Range

The physiological role of liver fatty acid-binding protein (L-FABP) has yet to be clarified. An important feature of this member of the family of intracellular lipid-binding proteins is the wide range of compounds that have been identified as potential physiological ligands. By using recombinant L-FABP, the binding of cholesterol, bile salts and their derivatives has been investigated under conditions that allow a direct comparison of the binding affinities of these ligands for fatty acids. The results demonstrate an inability of L-FABP to bind cholesterol, although the anionic derivative, cholesteryl sulphate, will bind under similar assay conditions. Of the bile salts examined, lithocholate and taurolithocholate sulphate showed the greatest binding to L-FABP. It is proposed that an important function of L-FABP is to bind certain physiological amphipathic anions, thus preventing the ‘free’ concentrations of these compounds from exceeding their critical micelle concentration, which could result in cell damage.

scholarly journals Studies on fatty acid-binding proteins. Changes in the concentration of hepatic fatty acid-binding protein during development in the rat

1987 ◽  
Vol 242 (3) ◽  
pp. 919-922 ◽  
Author(s):  
M Sheridan ◽  
T C I Wilkinson ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Binding Proteins ◽  
Fatty Acid Binding Protein ◽  
Fluorescence Enhancement ◽  
Binding Protein ◽  
Fold Increase ◽  
Fatty Acid Binding Proteins ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Hepatic Fatty Acid

The concentration of hepatic fatty acid-binding protein was determined in the livers of rats at various stages of development from foetus to young adult. Fatty acid-binding protein concentrations were determined by quantifying the fluorescence enhancement on the binding of the fluorescent probe 11-(dansylamino)-undecanoic acid. A 20-fold increase in the concentration of the protein was observed between the foetus and adult, and this increase was confirmed by immuno-blotting. No other protein in the 14,000-Mr range was observed in the foetus. Possible alternative fatty acid-binding proteins could not be detected in h.p.l.c.-fractionated foetal cytosol by the fluorescence-enhancement method.

scholarly journals Weight loss in prepubertal obese children is associated with a decrease in adipocyte fatty-acid-binding protein without changes in lipocalin-2: a 2-year longitudinal study

2010 ◽  
Vol 163 (6) ◽  
pp. 887-893 ◽  
Author(s):  
Raquel Corripio ◽  
José-Miguel Gónzalez-Clemente ◽  
Jacobo Pérez-Sánchez ◽  
Sílvia Näf ◽  
Lluís Gallart ◽  
...  
Keyword(s):  
Weight Loss ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Resistance Index ◽  
Oral Glucose ◽  
Lipocalin 2 ◽  
Obese Children ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

ContextLipocalin-2 and adipocyte fatty-acid-binding protein (A-FABP or FABP4) are adipokines potentially involved in the pathophysiology of obesity and metabolic syndrome in adults. In children, they have been scarcely studied.ObjectiveTo analyze lipocalin-2 and A-FABP circulating levels before and after 2 years of a dieting and lifestyle intervention in a prepubertal obese cohort.Design and settingCase–control study with a prospective follow-up of cases for 2 years in our referral pediatric endocrine outpatient center.Patients and methodsSeventy-three prepubertal obese children, 8.03±1.08-years old, and 47 age- and gender-matched lean controls were studied. Anthropometric parameters, blood pressure, fasting oral glucose tolerance test, homeostatic model insulin resistance index (HOMA-IR), lipid profile, lipocalin-2, and A-FABP were evaluated. Weight loss was considered ifz-score body mass index (BMI) decreased at least 0.5s.d.ResultsAt baseline, lipocalin-2 and A-FABP were higher in prepubertal obese children than those in lean controls (P<0.001). A-FABP showed a gradual increase, according to the obesity degree (r2=0.632;P<0.001). After 2 years, obese patients who lost weight showed a decrease in A-FABP (a mean 2% reduction in BMI was associated with a mean 29% decrease in A-FABP (P<0.001)) without changes in lipocalin-2 levels. Regression model analysis adjusted by age, sex, BMI, and HOMA showed that A-FABP was lower in males (β=−5.77 (CI 95%: −9.7; −1.84)) and was modified by BMI (β=2.7 (CI 95%: 1.77–3.62),r2=0.659). Lipocalin-2 was not modified by any of these variables.ConclusionsPrepubertal obese children show high plasma lipocalin-2 and A-FABP levels, but only A-FABP is influenced by weight loss.

scholarly journals A surface-associated retinol- and fatty acid-binding protein (Gp-FAR-1) from the potato cyst nematode Globodera pallida: lipid binding activities, structural analysis and expression pattern

2001 ◽  
Vol 356 (2) ◽  
pp. 387-394 ◽  
Author(s):  
Alison PRIOR ◽  
John T. JONES ◽  
Vivian C. BLOK ◽  
Jeremy BEAUCHAMP ◽  
Lindsay McDERMOTT ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Plant Defence ◽  
Fluorescence Emission ◽  
Lipid Binding ◽  
Globodera Pallida ◽  
Tryptophan Residue ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Parasitic nematodes produce at least two structurally novel classes of small helix-rich retinol- and fatty-acid-binding proteins that have no counterparts in their plant or animal hosts and thus represent potential targets for new nematicides. Here we describe a protein (Gp-FAR-1) from the plant-parasitic nematode Globodera pallida, which is a member of the nematode-specific fatty-acid- and retinol-binding (FAR) family of proteins but localizes to the surface of this species, placing it in a strategic position for interaction with the host. Recombinant Gp-FAR-1 was found to bind retinol, cis-parinaric acid and the fluorophore-tagged lipids 11-(dansylamino)undecanoic acid and dansyl-d,l-α-amino-octanoic acid. The fluorescence emission characteristics of the dansylated analogues indicated that the entire ligand enters the binding cavity. Fluorescence competition experiments showed that Gp-FAR-1 binds fatty acids in the range C11 to C24, with optimal binding at C15. Intrinsic fluorescence analysis of a mutant protein into which a tryptophan residue had been inserted supported computer-based predictions of the position of this residue at the protein's interior and possibly also at the binding site. Of direct relevance to plant defence systems was the observation that Gp-FAR-1 binds two lipids (linolenic and linoleic acids) that are precursors of plant defence compounds and the jasmonic acid signalling pathway. Moreover, Gp-FAR-1 was found to inhibit the lipoxygenase-mediated modification of these substrates in vitro. Thus not only does Gp-FAR-1 function as a broad-spectrum retinol- and fatty-acid-binding protein, the results are consistent with the idea that Gp-FAR-1 is involved in the evasion of primary host plant defence systems.

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