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Journal articles on the topic 'H-Fatty Acid Binding Protein'

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Published: 4 June 2021

Last updated: 5 February 2022

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1

FUJII, Hiroshi. "Fatty Acid-binding Proteins: Their Structure, Function and Gene Expression." Journal of Japan Atherosclerosis Society 24, no. 7-8 (1996): 353–61. http://dx.doi.org/10.5551/jat1973.24.7-8_353.

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2

ZIMMERMAN, Aukje W., Martin RADEMACHER, Heinz RüTERJANS, Christian LüCKE, and Jacques H. VEERKAMP. "Functional and conformational characterization of new mutants of heart fatty acid-binding protein." Biochemical Journal 344, no. 2 (November 24, 1999): 495–501. http://dx.doi.org/10.1042/bj3440495.

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In this study we investigated the possible involvement of several amino acids (not located in the ligand-binding centre) in fatty acid binding and conformational stability of heart fatty acid-binding protein (H-FABP). We prepared recombinant human H-FABP proteins with mutations in the hydrophobic patch (Phe4, Trp8 and Phe64), portal region (Phe16), hinge region (Leu66, Gly67), second portal region (Glu72) and at the protein surface (Lys21) respectively. Oleic acid-binding affinity and conformational stability of human H-FABP are significantly decreased or completely lost by mutation of Trp8 or Phe16. NMR spectra confirmed that these residues are important for the stability of the protein fold. Substitution of Phe4 or Phe64 resulted in less stability, but oleic acid-binding affinity was not affected. Mutation of Lys21 had no effect on either structural integrity or fatty acid-binding affinity. Replacement of Leu66 or Gly67 did not affect fatty acid binding, but protein stability was reduced. Finally, mutation of Glu72 to Ser caused no change of affinity, but NMR spectra and urea-denaturation curves showed the extremely poor stability of this mutant. In conclusion, no relationship was observed between fatty acid-binding affinity and conformational stability.

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3

Wilkinson, T. C., and D. C. Wilton. "Studies on fatty acid-binding proteins. The binding properties of rat liver fatty acid-binding protein." Biochemical Journal 247, no. 2 (October 15, 1987): 485–88. http://dx.doi.org/10.1042/bj2470485.

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1. The fluorescent fatty acid probe 11-(dansylamino)undecanoic acid binds to rat liver fatty acid-binding protein with a 1:1 stoichiometry. 2. The binding of the fluorescent probe is competitive with long-chain fatty acids. 3. Binding displacement studies were performed with a wide range of fatty acids and other ligands and identified C16 and C18 fatty acids as the preferred fatty acids for rat liver fatty acid-binding protein. No preference was observed for unsaturated fatty acids within this group. 4. Fatty acyl-CoA binds less well than the corresponding fatty acid.

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4

Carey, J. O., P. D. Neufer, R. P. Farrar, J. H. Veerkamp, and G. L. Dohm. "Transcriptional regulation of muscle fatty acid-binding protein." Biochemical Journal 298, no. 3 (March 15, 1994): 613–17. http://dx.doi.org/10.1042/bj2980613.

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Heart fatty acid-binding protein (H-FABP) is present in a wide variety of tissues but is found in the highest concentration in cardiac and red skeletal muscle. It has been proposed that the expression of H-FABP correlates directly with the fatty acid-oxidative capacity of the tissue. In the present study, the expression of H-FABP was measured in red and white skeletal muscle under two conditions in which fatty acid utilization is known to be increased: streptozotocin-induced diabetes and fasting. Protein concentration, mRNA concentration and transcription rate were measured under both conditions. The level of both protein and mRNA increased approximately 2-fold under each condition. The transcription rate was higher in red skeletal muscle than in white muscle, was increased 2-fold during fasting, but was unchanged by streptozotocin-induced diabetes. In addition to supporting the hypothesis that H-FABP is induced during conditions of increased fatty acid utilization, these findings demonstrate that the regulation of H-FABP expression may or may not be at the level of transcription depending on the stimulus.

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5

LÜCKE, Christian, Martin RADEMACHER, Aukje W. ZIMMERMAN, Herman T. B. VAN MOERKERK, Jacques H. VEERKAMP, and Heinz RÜTERJANS. "Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)." Biochemical Journal 354, no. 2 (February 22, 2001): 259–66. http://dx.doi.org/10.1042/bj3540259.

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Recent advances in the characterization of fatty acid-binding proteins (FABPs) by NMR have enabled various research groups to investigate the function of these proteins in aqueous solution. The binding of fatty acid molecules to FABPs, which proceeds through a portal region on the protein surface, is of particular interest. In the present study we have determined the three-dimensional solution structure of human heart-type FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in combination with data collected on a F57S mutant we have been able to show that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand. This indicates that during the binding process the protein accommodates the ligand molecule by a ‘selected-fit’ mechanism. In fact, this behaviour appears to be especially pronounced in the heart-type FABP, possibly due to a more rigid backbone structure compared with other FABPs, as suggested by recent NMR relaxation studies. Thus differences in the dynamic behaviours of these proteins may be the key to understanding the variations in ligand affinity and specificity within the FABP family.

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6

PRINSEN, Clemens F. M., and Jacques H. VEERKAMP. "Fatty acid binding and conformational stability of mutants of human muscle fatty acid-binding protein." Biochemical Journal 314, no. 1 (February 15, 1996): 253–60. http://dx.doi.org/10.1042/bj3140253.

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Human muscle fatty acid-binding protein (M-FABP) is a 15 kDa cytosolic protein which may be involved in fatty acid transfer and modulation of non-esterified fatty acid concentration in heart, skeletal muscle, kidney and many other tissues. Crystallographic studies have suggested the importance of the amino acids Thr-40, Arg-106, Arg-126 and Tyr-128 for the hydrogen bonding network of the fatty acid carboxylate group. Two phenylalanines at 16 and 57 are positioned to interact with the acyl chain of the fatty acid. We prepared 13 mutant proteins by site-directed mutagenesis and tested them for fatty acid binding and stability. Substitution of amino acids Phe-16, Arg-106 or Arg-126 created proteins which showed a large decrease in or complete loss of oleic acid binding. Substitution of Phe-57 by Ser or Val and of Tyr-128 by Phe had no great effect. The stability of the mutant proteins was tested by denaturation studies on the basis of fatty acid binding or tryptophan fluorescence and compared with that of the wild-type M-FABP. There was no direct relationship between fatty acid-binding activity and stability. Less stable mutants (F57S and Y128F) did not show a marked change in fatty acid-binding activity. Substitution of Arg-126 by Gln or Arg-106 by Thr eliminated binding activity, but the former mutant protein showed wild-type stability, in contrast to the latter. The results are in agreement with crystallographic data.

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7

Shearer, Jane, Patrick T. Fueger, Jeffrey N. Rottman, Deanna P. Bracy, Bert Binas, and David H. Wasserman. "Heart-type fatty acid-binding protein reciprocally regulates glucose and fatty acid utilization during exercise." American Journal of Physiology-Endocrinology and Metabolism 288, no. 2 (February 2005): E292—E297. http://dx.doi.org/10.1152/ajpendo.00287.2004.

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The role of heart-type cytosolic fatty acid-binding protein (H-FABP) in mediating whole body and muscle-specific long-chain fatty acid (LCFA) and glucose utilization was examined using exercise as a phenotyping tool. Catheters were chronically implanted in a carotid artery and jugular vein of wild-type (WT, n = 8), heterozygous (H-FABP+/−, n = 8), and null (H-FABP−/−, n = 7) chow-fed C57BL/6J mice, and mice were allowed to recover for 7 days. After a 5-h fast, conscious, unrestrained mice were studied during 30 min of treadmill exercise (0.6 mph). A bolus of [125I]-15-( p-iodophenyl)-3- R, S-methylpentadecanoic acid and 2-deoxy-[3H]glucose was administered to obtain rates of whole body metabolic clearance (MCR) and indexes of muscle LCFA (Rf) and glucose (Rg) utilization. Fasting, nonesterified fatty acids (mM) were elevated in H-FABP−/− mice (2.2 ± 0.9 vs. 1.3 ± 0.1 and 1.3 ± 0.2 for WT and H-FABP+/−). During exercise, blood glucose (mM) increased in WT (11.7 ± 0.8) and H-FABP+/− (12.6 ± 0.9) mice, whereas H-FABP−/− mice developed overt hypoglycemia (4.8 ± 0.8). Examination of tissue-specific and whole body glucose and LCFA utilization demonstrated a dependency on H-FABP with exercise in all tissues examined. Reductions in H-FABP led to decreasing exercise-stimulated Rf and increasing Rg with the most pronounced effects in heart and soleus muscle. Similar results were seen for MCR with decreasing LCFA and increasing glucose clearance with declining levels of H-FABP. These results show that, in vivo, H-FABP has reciprocal effects on glucose and LCFA utilization and whole body fuel homeostasis when metabolic demands are elevated by exercise.

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8

Tso, P., A. Nauli, and C. M. Lo. "Enterocyte fatty acid uptake and intestinal fatty acid-binding protein." Biochemical Society Transactions 32, no. 1 (February 1, 2004): 75–78. http://dx.doi.org/10.1042/bst0320075.

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This article reviews our current understanding of the uptake of fatty acids by the enterocytes of the intestine. The micellar solubilization of fatty acids by bile salts and the factors regulating that process are discussed. The mechanism of how micellar solubilization of fatty acids promotes the uptake of fatty acids by enterocytes and their relative importance is reviewed. Additionally, discussion of the various fatty acid transporters located at the brush border membrane of the enterocytes is included. Finally, a summary of our current understanding of the function of fatty-acid-binding proteins inside enterocytes is provided.

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9

Zanotti, Giuseppe. "Muscle fatty acid-binding protein." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1441, no. 2-3 (November 1999): 94–105. http://dx.doi.org/10.1016/s1388-1981(99)00163-8.

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10

Bronský, Jiří, Michal Karpíšek, Eva Bronská, Marta Pechová, Barbora Jančíková, Hana Kotolová, David Stejskal, Richard Průša, and Jiří Nevoral. "Adiponectin, Adipocyte Fatty Acid Binding Protein, and Epidermal Fatty Acid Binding Protein: Proteins Newly Identified in Human Breast Milk." Clinical Chemistry 52, no. 9 (September 1, 2006): 1763–70. http://dx.doi.org/10.1373/clinchem.2005.063032.

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Abstract Background: Breastfeeding may protect children from developing metabolic syndrome and other diseases later in life. We investigated novel proteins in human breast milk that might play a role in this process. Methods: We used ELISA to measure adiponectin, adipocyte and epidermal fatty acid binding proteins (AFABP, EFABP), and leptin concentrations in human breast milk obtained from 59 mothers 48 h after initiation of lactation. Using a questionnaire and medical records, we collected information about the mothers and newborns. Results: Mean (SE) adiponectin concentrations in breast milk were 13.7 (0.8), range 3.9–30.4 μg/L; AFABP concentrations 26.7 (4.4), range 1.2–137.0 μg/L; EFABP concentrations 18.1 (1.4), range 0.8–47.0 μg/L; and leptin concentrations 0.50 (0.05), range 0–1.37 μg/L. We found a significant correlation between AFABP and EFABP concentrations (r = 0.593, P <0.0001). Maternal EFABP concentrations were significantly higher in mothers who delivered boys than in those who delivered girls [21.7 (2.3) vs 15.4 (1.7) μg/L, P = 0.028] and correlated with newborn birth weight (r = 0.266, P = 0.045). Maternal leptin correlated with body weight before pregnancy (r = 0.272, P = 0.043) and at delivery (r = 0.370, P = 0.005), body mass index before pregnancy (r = 0.397, P = 0.003) and at delivery (r = 0.498, P <0.0001), body weight gain during pregnancy (r = 0.267, P = 0.047), and newborn gestational age (r = 0.266, P = 0.048). Leptin was significantly lower in mothers who delivered preterm vs term babies [0.30 (0.09) vs 0.60 (0.05) ug/L, P = 0.026]. Conclusions: Concentrations of adiponectin, AFABP, and EFABP in human breast milk are related to nutritional variables of mothers and newborns and thus may play a role in the protective effects of breastfeeding.

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11

Nelson, J., L. L. Homan, and J. S. Dillon. "FATTY ACID BINDING PROTEIN MODULATES FATTY ACID TRANSCRIPTIONAL EFFECTS." Journal of Investigative Medicine 52 (March 2004): S353. http://dx.doi.org/10.1097/00042871-200403002-00043.

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12

Tweedie, Susan, and Yvonne Edwards. "cDNA sequence for mouse heart fatty acid binding protein, H-FABP." Nucleic Acids Research 17, no. 11 (1989): 4374. http://dx.doi.org/10.1093/nar/17.11.4374.

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13

Lassen, Dirck, Christian L�cke, Arno Kromminga, Axel Lezius, Friedrich Spener, and Heinz R�terjans. "Solution structure of bovine heart fatty acid-binding protein (H-FABPc)." Molecular and Cellular Biochemistry 123, no. 1-2 (1993): 15–22. http://dx.doi.org/10.1007/bf01076470.

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14

Wilton, D. C. "Studies on fatty-acid-binding proteins. The purification of rat liver fatty-acid-binding protein and the role of cysteine-69 in fatty acid binding." Biochemical Journal 261, no. 1 (July 1, 1989): 273–76. http://dx.doi.org/10.1042/bj2610273.

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1. A new, simple and high-yield procedure is described for the purification of hepatic fatty-acid-binding protein from rat liver using naphthylaminodecyl-agarose as an affinity column. 2. Cysteine-69 is shown to react slowly, but quantitatively, with 5,5′-dithiobis-(2-nitrobenzoic acid) (DTNB), indicating that the thiol group is free, but may be buried within the protein. 3. Fatty acids do not affect the DTNB reactivity of this cysteine residue; however, cysteine reactivity is enhanced in the presence of haem and oleoyl-CoA. 4. Fatty-acid-binding protein that has been modified with DTNB is still able to bind the fluorescent fatty acid 11-(dansylamino)undecanoic acid, indicating that cysteine-69 may be remote from the fatty-acid-binding site.

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15

Luxon, B. A., and M. T. Milliano. "Cytoplasmic codiffusion of fatty acids is not specific for fatty acid binding protein." American Journal of Physiology-Cell Physiology 273, no. 3 (September 1, 1997): C859—C867. http://dx.doi.org/10.1152/ajpcell.1997.273.3.c859.

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The intracellular movement of fatty acids is thought to be facilitated through codiffusion with fatty acid binding protein (FABP). Previous work suggested that FABP decreases fatty acid binding to immobile membranes, causing faster cytoplasmic diffusion. However, the specificity for binding to FABP has not been addressed. The aim of the current study was to determine whether specific FABP binding is required or whether binding to other proteins will produce the same effect. A model cytoplasm consisted of a fatty acid, proteins, and liposomes to simulate intracellular membranes. Laser photobleaching (fluorescence recovery after photobleaching) was used to measure the movement of the fluorescent fatty acid 12-N-methyl-7-nitrobenzo-2-oxa-1,3-diazoaminostearate (NBD-stearate) in model cytoplasm, in normal and permeabilized Hep G2 cells, and after incubation of permeabilized cells with bovine serum albumin (BSA) or FABP. Increasing protein in the model cytoplasm increased the diffusion rate in proportion to the extent of protein binding. Cell permeabilization reduced diffusion of NBD-stearate to < 5% of controls. Incubation of permeabilized cells with FABP or BSA resulted in a concentration-dependent increase in the NBD-stearate diffusion rate. BSA was more effective than FABP in binding NBD-stearate and increasing its diffusion rate after permeabilization. Proteins like FABP promote the diffusion of fatty acids. Removal of these proteins drastically reduces cytoplasmic diffusion. Substitution with BSA reestablishes the diffusive flux, suggesting that specific binding to FABP is not required. These data support a role for intracellular binding proteins in facilitating the cytoplasmic movement of fatty acids.

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16

Zhou, S. L., D. Stump, L. Isola, and P. D. Berk. "Constitutive expression of a saturable transport system for non-esterified fatty acids in Xenopus laevis oocytes." Biochemical Journal 297, no. 2 (January 15, 1994): 315–19. http://dx.doi.org/10.1042/bj2970315.

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In the presence of 150 microM BSA, uptake of [3H]oleate by Xenopus laevis oocytes was a saturable function of the unbound oleate concentration (Vmax. 110 +/- 4 pmol/h per oocyte; Km 193 +/- 11 nM unbound oleate). Oleate uptake was three orders of magnitude faster than that of another test substance, [35S]bromosulphophthalein, and was competitively inhibited by 55 nM unbound palmitate (Vmax. 111 +/- 14 pmol/h per oocyte; Km 424 +/- 63 nM unbound oleate) (P < 0.01). Oleate uptake was also inhibited by antibodies to a 43 kDa rat liver plasma-membrane fatty acid-binding protein, a putative transporter of long-chain fatty acids in mammalian cells; uptake of the medium-chain fatty acid [14C]octanoate was unaffected. Immunofluorescence and immunoblotting demonstrated that the antiserum reacted with a single 43 kDa protein on the oocyte surface. Hence a protein related to the mammalian plasma-membrane fatty acid-binding protein may play a role in saturable uptake of long-chain fatty acids by Xenopus oocytes.

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17

MEUNIER-DURMORT, Claire, Hélène POIRIER, Isabelle NIOT, Claude FOREST, and Philippe BESNARD. "Up-regulation of the expression of the gene for liver fatty acid-binding protein by long-chain fatty acids." Biochemical Journal 319, no. 2 (October 15, 1996): 483–87. http://dx.doi.org/10.1042/bj3190483.

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The role of fatty acids in the expression of the gene for liver fatty acid-binding protein (L-FABP) was investigated in the well-differentiated FAO rat hepatoma cell line. Cells were maintained in serum-free medium containing 40 µM BSA/320 µM oleate. Western blot analysis showed that oleate triggered an approx. 4-fold increase in the cytosolic L-FABP level in 16 h. Oleate specifically stimulated L-FABP mRNA in time-dependent and dose-dependent manners with a maximum 7-fold increase at 16 h in FAO cells. Preincubation of FAO cells with cycloheximide prevented the oleate-mediated induction of L-FABP mRNA, showing that protein synthesis was required for the action of fatty acids. Run-on transcription assays demonstrated that the control of L-FABP gene expression by oleate was, at least in part, transcriptional. Palmitic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid were similarly potent whereas octanoic acid was inefficient. This regulation was also found in normal hepatocytes. Therefore long-chain fatty acids are strong inducers of L-FABP gene expression. FAO cells constitute a useful tool for studying the underlying mechanism of fatty acid action.

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18

Puspitawati, Ira, I. Nyoman G. Sudana, Setyawati Setyawati, and Usi Sukorini. "HEART FATTY ACID BINDING PROTEIN SEBAGAI PETANDA BIOLOGIS DIAGNOSIS SINDROM KORONER AKUT." INDONESIAN JOURNAL OF CLINICAL PATHOLOGY AND MEDICAL LABORATORY 22, no. 2 (March 27, 2018): 127. http://dx.doi.org/10.24293/ijcpml.v22i2.1114.

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Heart-Fatty Acid-Binding Protein (H-FABP) is a membrane-bound protein that facilitates transport of fatty acids from the blood intothe heart. It is a low molecular weight cytoplasmic protein. Because of its small size and location, it is released rapidly into the bloodfollowing myocardial damage. The H-FABP levels rise as early as between 1−3 hours after the onset of Acute Coronary Syndrome, thepeak situation between 6−-8 hours, and returns to normal within 24 hours. The purpose of this study was to know the cut-off value ofHeart Fatty Acid Binding Protein with a sensitivity of at least 90% in patients with acute coronary syndrome in the Dr. Sardjito HospitalYogyakarta. The researchers undertook a cross sectional evaluation of 75 consecutive patients admitted with acute chest pain suggestiveof acute coronary syndrome (ACS). The H-FABP was measured by using immunoturbidimetry assay methods. The receiver operatingcharacteristic (ROC) analysis was calculated for the cut off point, sensitivity and specificity estimation. A total of 75 patients (59 in theACS group and 16 in the control group) were included in this study, and the majority of the ACS group (64 [76.2%]) were male patientswith AMI, 20 (26.7%) had an ST-elevation myocardial infarction and the rest (21 [28%]) had a non–ST-elevation myocardial infarction.The optimized cut-off obtained for h-FABP was 15 ng/mL, showing a sensitivity and specificity of the H-FABP assay for detecting ACSas 98.31 (95% CI 90 to 100) and 93.75% (95% CI 86 to 99), respectively. The areas under the receiver operator characteristic (ROC)curves to distinguish ACS from non-ACS were 0.983 (95% CI: 0.927– 0.999) for H-FABP. The optimized cut-off obtained for H-FABPwas 15 ng/mL, showing a 98.31% sensitivity and 93.75% specificity for detecting ACS in the Dr. Sardjito Hospital Yogyakarta.

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19

Stewart, J. M. "Fatty acid-binding protein and facilitated diffusion of fatty acids." Biochemical Journal 280, no. 3 (December 15, 1991): 835–36. http://dx.doi.org/10.1042/bj2800835b.

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20

Nelson, J., L. L. Homan, and J. S. Dillon. "43 FATTY ACID BINDING PROTEIN MODULATES FATTY ACID TRANSCRIPTIONAL EFFECTS." Journal of Investigative Medicine 52, Suppl 2 (March 1, 2004): S353.2—S353. http://dx.doi.org/10.1136/jim-52-suppl2-43.

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21

Guglielmo, Christopher G., Norbert H. Haunerland, Peter W. Hochachka, and Tony D. Williams. "Seasonal dynamics of flight muscle fatty acid binding protein and catabolic enzymes in a migratory shorebird." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 282, no. 5 (May 1, 2002): R1405—R1413. http://dx.doi.org/10.1152/ajpregu.00267.2001.

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We developed an ELISA to measure heart-type fatty acid binding protein (H-FABP) in muscles of the western sandpiper ( Calidris mauri), a long-distance migrant shorebird. H-FABP accounted for almost 11% of cytosolic protein in the heart. Pectoralis H-FABP levels were highest during migration (10%) and declined to 6% in tropically wintering female sandpipers. Premigratory birds increased body fat, but not pectoralis H-FABP, indicating that endurance flight training may be required to stimulate H-FABP expression. Juveniles making their first migration had lower pectoralis H-FABP than adults, further supporting a role for flight training. Aerobic capacity, measured by citrate synthase activity, and fatty acid oxidation capacity, measured by 3-hydroxyacyl-CoA-dehydrogenase and carnitine palmitoyl transferase activities, did not change during premigration but increased during migration by 6, 12, and 13%, respectively. The greater relative induction of H-FABP (+70%) with migration than of catabolic enzymes suggests that elevated H-FABP is related to the enhancement of uptake of fatty acids from the circulation. Citrate synthase, 3-hydroxyacyl-CoA-dehydrogenase, and carnitine palmitoyl transferase were positively correlated within individuals, suggesting coexpression, but enzyme activities were unrelated to H-FABP levels.

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22

Azzazy, Hassan ME, Maurice MAL Pelsers, and Robert H. Christenson. "Unbound Free Fatty Acids and Heart-Type Fatty Acid–Binding Protein: Diagnostic Assays and Clinical Applications." Clinical Chemistry 52, no. 1 (January 1, 2006): 19–29. http://dx.doi.org/10.1373/clinchem.2005.056143.

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Abstract Background: A biomarker that reliably detects myocardial ischemia in the absence of necrosis would be useful for initial identification of unstable angina patients and for differentiating patients with chest pain of an etiology other than coronary ischemia, and could provide clinical utility complementary to that of cardiac troponins, the established markers of necrosis. Unbound free fatty acids (FFAu) and their intracellular binding protein, heart-type fatty acid–binding protein (H-FABP), have been suggested to have clinical utility as indicators of cardiac ischemia and necrosis, respectively. Methods: We examined results of clinical assessments of FFAu and H-FABP as biomarkers of cardiac ischemia and necrosis. Data published on FFAu and H-FABP over the past 30 years were used as the basis for this review. Results: Although little clinical work has been done on FFAu since the initial reports, recent studies documented an association between increased serum FFAs and ventricular dysrhythmias and death in patients with acute myocardial infarction (AMI). Recent data suggest that serum FFAu concentrations increase well before markers of cardiac necrosis and are sensitive indicators of ischemia in AMI. H-FABP is abundant in cardiac muscle and is presumed to be involved in myocardial lipid homeostasis. Similar to myoglobin, plasma H-FABP increases within 3 h after AMI and returns to reference values within 12–24 h. Conclusions: FFAu may have a potential role in identifying patients with cardiac ischemia. H-FABP is useful for detecting cardiac injury in acute coronary syndromes and predicting recurrent cardiac events in acute coronary syndromes and in congestive heart failure patients. Assays are available for both markers that could facilitate further clinical investigations to assess their possible roles as markers of cardiac ischemia and/or necrosis.

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23

Stewart, John M., Gordon W. Slysz, Mary Anne Pritting, and Ursula Muller-Eberhard. "Ferriheme and ferroheme are isosteric inhibitors of fatty acid binding to rat liver fatty acid binding protein." Biochemistry and Cell Biology 74, no. 2 (March 1, 1996): 249–55. http://dx.doi.org/10.1139/o96-026.

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In addition to fatty acids, liver fatty acid binding protein (L-FABP) also interacts with ferriheme, which it binds with an affinity approximately one order of magnitude greater than that for oleic acid. We have, therefore, examined the effect of ferroheme and ferriheme on the binding of oleate to rat L-FABP, also called heme-binding protein. Both oxidation states of heme behaved as isosteric inhibitors for the binding of the fatty acid confirming a common binding site. The reduced form of heme (Fe(II)) is a threefold better competitor of oleate binding than ferriheme. To show whether the diffusion of heme would be affected by the presence of the binding protein, we measured the effect of the fatty acid binding protein on the diffusional flux of a water-soluble heme derivative, iron-deuteroporphyrin. The diffusional flux of iron-deuteroporphyrin did not change in the presence of the protein. This suggested that the binding affinity of fatty acid binding protein for iron-deuteroporphyrin is too great to allow rapid equilibrium between bound and unbound ligand across the system in an appropriate time frame.Key words: fatty acid binding protein, heme, diffusion, liver, oleic acid.

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24

Mogensen, I. B., H. Schulenberg, H. O. Hansen, F. Spener, and J. Knudsen. "A novel acyl-CoA-binding protein from bovine liver. Effect on fatty acid synthesis." Biochemical Journal 241, no. 1 (January 1, 1987): 189–92. http://dx.doi.org/10.1042/bj2410189.

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Bovine liver was shown to contain a hitherto undescribed medium-chain acyl-CoA-binding protein. The protein co-purifies with fatty-acid-binding proteins, but was, unlike these proteins, unable to bind fatty acids. The protein induced synthesis of medium-chain acyl-CoA esters on incubation with goat mammary-gland fatty acid synthetase. The possible function of the protein is discussed.

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25

Das, Undurti N. "Heart-type fatty acid-binding protein (H-FABP) and coronary heart disease." Indian Heart Journal 68, no. 1 (January 2016): 16–18. http://dx.doi.org/10.1016/j.ihj.2015.07.030.

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26

Poirier, H., I. Niot, P. Degrace, M. C. Monnot, A. Bernard, and P. Besnard. "Fatty acid regulation of fatty acid-binding protein expression in the small intestine." American Journal of Physiology-Gastrointestinal and Liver Physiology 273, no. 2 (August 1, 1997): G289—G295. http://dx.doi.org/10.1152/ajpgi.1997.273.2.g289.

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The effects of dietary oil intake and fatty acid infusions on the expression of intestinal and liver fatty acid-binding proteins (I-FABP and L-FABP, respectively) were investigated in the small intestine of mice. A daily force-feeding for 7 days with 0.2 ml sunflower oil specifically increased L-FABP mRNA and protein levels in duodenum and proximal jejunum. This upregulation was mediated in time- and dose-dependent manners by a minute quantity of linoleic acid, the main fatty acid found in sunflower oil. The L-FABP induction was only found with long-chain fatty acids, with the nonmetabolizable, substituted fatty acid alpha-bromopalmitate being far more active. A hormonally mediated effect is unlikely because long-chain fatty acids induced L-FABP mRNA in the Caco-2 cell line cultured in serum-free medium. Therefore, long-chain fatty acids are strong inducers of L-FABP gene expression in the small intestine. In contrast to data found in the rat, I-FABP gene expression appears to be unaffected by a lipid-enriched diet in the mouse.

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27

Storch, J., N. M. Bass, and A. M. Kleinfeld. "Studies of the Fatty Acid-binding Site of Rat Liver Fatty Acid-binding Protein Using Fluorescent Fatty Acids." Journal of Biological Chemistry 264, no. 15 (May 1989): 8708–13. http://dx.doi.org/10.1016/s0021-9258(18)81850-6.

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Stewart, J. M., T. E. English, and K. B. Storey. "Comparisons of the effects of temperature on the liver fatty acid binding proteins from hibernator and nonhibernator mammals." Biochemistry and Cell Biology 76, no. 4 (August 1, 1998): 593–99. http://dx.doi.org/10.1139/o98-018.

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Hibernating mammals rely heavily on lipid metabolism to supply energy during hibernation. We wondered if the fatty acid binding protein from a hibernator responded to temperature differently than that from a nonhibernator. We found that the Kd for oleate of the liver fatty acid binding protein (1.5 micromolar) isolated from ground squirrel (Spermophilus richardsonii) was temperature insensitive over 5-37°C, while the rat liver fatty acid binding protein was affected with the Kd at 37°C being about half (0.8 micromolar) that found at lower temperatures. This same trend was observed when comparing the specificity of various fatty acids of differing chain length and degree of unsaturation for the two proteins at 5 and 37°C. At the lower temperature, ground squirrel protein bound long-chain unsaturated fatty acids, particularly linoleate and linolenate, at least as well as at the higher temperature and matched requirements for these fatty acids in the diet. The most common long-chain fatty acid, palmitate, was a more effective ligand for ground squirrel liver fatty acid binding protein at 5°C than at 37°C, with the opposite occurring in the eutherm. Rat protein was clearly not adapted to function optimally at temperatures lower than the animal's body temperature.Key words: fatty acid binding protein, temperature, hibernation.

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29

Hai, Abdul, Nadeem A. Kizilbash, Syeda Huma H. Zaidi, and Jamal Alruwaili. "Indirect Evidence for Self Association of Muscle Fatty Acid Binding Protein from Locusta migratoria." International Journal of Bioscience, Biochemistry and Bioinformatics 4, no. 5 (2014): 419–22. http://dx.doi.org/10.7763/ijbbb.2014.v4.380.

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30

LÜCKE, Christian, Martin RADEMACHER, Aukje W. ZIMMERMAN, Herman T. B. van MOERKERK, Jacques H. VEERKAMP, and Heinz RÜTERJANS. "Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)." Biochemical Journal 354, no. 2 (March 1, 2001): 259. http://dx.doi.org/10.1042/0264-6021:3540259.

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31

Wilkinson, T. C. I., and D. C. Wilton. "Studies on fatty acid-binding proteins. The diurnal variation shown by rat liver fatty acid-binding protein." Biochemical Journal 242, no. 3 (March 15, 1987): 913–17. http://dx.doi.org/10.1042/bj2420913.

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The concentration of fatty acid-binding protein in rat liver was examined by SDS/polyacrylamide-gel electrophoresis, by Western blotting and by quantifying the fluorescence enhancement achieved on the binding of the fluorescent probe 11-(dansylamino)undecanoic acid. A 2-3-fold increase in the concentration of this protein produced by treatment of rats with the peroxisome proliferator tiadenol was readily detected; however, only a small variation in the concentration of the protein due to a diurnal rhythm was observed. This result contradicts the 7-10-fold variation previously reported for this protein [Hargis, Olson, Clarke & Dempsey (1986) J. Biol. Chem. 261, 1988-1991].

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32

OSUMI, Noriko. "Polyunsaturated Fatty Acids and Fatty Acid Binding Protein Involvements in Neurogenesis." Oleoscience 11, no. 10 (2011): 359–63. http://dx.doi.org/10.5650/oleoscience.11.359.

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33

Huang, Huan, Olga Starodub, Avery McIntosh, Ann B. Kier, and Friedhelm Schroeder. "Liver Fatty Acid-binding Protein Targets Fatty Acids to the Nucleus." Journal of Biological Chemistry 277, no. 32 (May 22, 2002): 29139–51. http://dx.doi.org/10.1074/jbc.m202923200.

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34

Friedman, Ran, Esther Nachliel, and Menachem Gutman. "Fatty Acid Binding Proteins: Same Structure but Different Binding Mechanisms? Molecular Dynamics Simulations of Intestinal Fatty Acid Binding Protein." Biophysical Journal 90, no. 5 (March 2006): 1535–45. http://dx.doi.org/10.1529/biophysj.105.071571.

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35

Roepstorff, C., J. Wulff Helge, B. Vistisen, and B. Kiens. "Studies of plasma membrane fatty acid-binding protein and other lipid-binding proteins in human skeletal muscle." Proceedings of the Nutrition Society 63, no. 2 (May 2004): 239–44. http://dx.doi.org/10.1079/pns2004332.

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The first putative fatty acid transporter identified was plasma membrane fatty acid-binding protein (FABPpm). Later it was demonstrated that this protein is identical to the mitochondrial isoform of the enzyme aspartate aminotransferase. In recent years data from several cell types have emerged, indicating that FABPpm plays a role in the transport of long-chain saturated and unsaturated fatty acids. In the limited number of studies in human skeletal muscle it has been demonstrated that dietary composition and exercise training can influence the content of FABPpm. Ingestion of a fat-rich diet induces an increase in FABPpm protein content in human skeletal muscle in contrast to the decrease seen during consumption of a carbohydrate-rich diet. A similar effect of a fat-rich diet is also observed for cytosolic fatty acid-binding protein and fatty acid translocase/CD36 protein expression. Exercise training up regulates FABPpm protein content in skeletal muscle, but only in male subjects; no significant differences were observed in muscle FABPpm content in a cross-sectional study of female volunteers of varying training status, even though muscle FABPpm content did not depend on gender in the untrained state. A higher utilization of plasma long-chain fatty acids during exercise in males compared with females could explain the gender-dependent influence of exercise training on FABPpm. The mechanisms involved in the regulation of the function and expression of FABPpm protein remain to be clarified.

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36

Prows, Daniel R., Eric J. Murphy, Dino Moncecchi, and Friedhelm Schroeder. "Intestinal fatty acid-binding protein expression stimulates fibroblast fatty acid esterification." Chemistry and Physics of Lipids 84, no. 1 (November 1996): 47–56. http://dx.doi.org/10.1016/s0009-3084(96)02619-9.

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37

Veerkamp, J. H., and H. T. B. van Moerkerk. "Fatty acid-binding protein and its relation to fatty acid oxidation." Molecular and Cellular Biochemistry 123, no. 1-2 (June 1993): 101–6. http://dx.doi.org/10.1007/bf01076480.

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38

Nam, Ki Hyun. "Crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid." Acta Crystallographica Section D Structural Biology 77, no. 7 (June 29, 2021): 954–65. http://dx.doi.org/10.1107/s2059798321005763.

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The brain-type fatty acid-binding protein FABP7, which is expressed in astrocytes and neural progenitors, is a member of the intracellular lipid-binding protein family. This protein is not only involved in various cellular functions such as metabolism, inflammation and energy homeostasis, but also in diseases such as cognitive disorders and tumors. Structures of unsaturated fatty acids, such as oleic acid (OA) and docosahexaenoic acid (DHA), bound to FABP7 have been elucidated; however, structures of saturated fatty acids bound to FABP7 remain unknown. To better understand fatty acid recognition, here the crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid (PA), a saturated fatty acid, is reported at a resolution of 1.6 Å. The PA bound to the fatty acid-binding pocket of FABP7 assumed a U-shaped conformation. The carboxylate moiety of PA interacted with Tyr129, Arg127 and, via a water bridge, with Arg107 and Thr54, whereas its aliphatic chain was stabilized by hydrophobic interactions with Met21, Leu24, Thr30, Thr37, Pro39, Phe58 and Asp77. Structural comparison showed that PA, OA and DHA exhibited unique binding conformations in the fatty acid-binding pocket, stabilized by distinct amino-acid interactions. The binding of PA to FABP7 exhibits a unique binding conformation when compared with other human FABPs (FABP3–FABP5 and FABP8) expressed in other tissues. Based on the crystal and fatty acid structures, it was suggested that PA, which prefers a linear form in nature, required a greater conformational change in its aliphatic chain to bind to the fatty acid-binding pocket in a U-shaped conformation, compared with the cis configurations of OA or DHA. This, together with the length of the aliphatic chain, was considered to be one of the factors determining the binding affinity of PA to FABP7. These results provide a better understanding of fatty acid recognition by FABP7 and expand the knowledge of the binding of PA to FABPs.

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39

Ishino, Mitsunori, Tetsuro Shishido, Takanori Arimoto, Hiroki Takahashi, Takehiko Miyashita, Takuya Miyamoto, Joji Nitobe, Tetsu Watanabe, and Isao Kubota. "Heart-Type Fatty Acid Binding Protein (H-FABP) in Acute Decompensated Heart Failure." Journal of Cardiac Failure 16, no. 9 (September 2010): S166. http://dx.doi.org/10.1016/j.cardfail.2010.07.183.

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40

Thumser, A. E., and D. C. Wilton. "Characterization of binding and structural properties of rat liver fatty-acid-binding protein using tryptophan mutants." Biochemical Journal 300, no. 3 (June 15, 1994): 827–33. http://dx.doi.org/10.1042/bj3000827.

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Rat liver fatty-acid-binding protein (FABP) does not contain tryptophan. Three mutant proteins have been produced in which a single tryptophan residue has been inserted by site-directed mutagenesis at positions 3 (F3W), 18 (F18W) and 69 (C69W). These tryptophans have been strategically located in order to provide fluorescent reporter groups to study the binding and structural characteristics of rat liver FABP. Two fluorescent fatty acid analogues, DAUDA (11-[(5-dimethylaminonaphthalene-1- sulphonyl)amino]undecanoic acid) and 3-[p-(6-phenyl)-hexa-1,3,5-trienyl]phenylpropionic acid, showed no significant difference in binding affinities for the different mutant proteins, although maximum fluorescence values were decreased for F3W and increased for C69W. These findings were confirmed by studies of DAUDA displacement by oleate. Protein-denaturation studies in the presence of urea indicated subtle differences for the three mutants which could be explained by multiple unfolding pathways. Fatty acid binding increased tryptophan fluorescence emission in the case of the F18W protein, but had no effect on the F3W and C69W proteins. Fluorescence quenching studies with 2-bromopalmitate showed that a fatty acid carboxylate is close to the tryptophan in the F18W protein. Energy-transfer studies showed that the fluorescent moiety of DAUDA is equidistant from the three mutated amino acids and is bound within the beta-clam solvent cavity of liver FABP. This interpretation of the fluorescence quenching and energy-transfer data supports the difference in ligand orientation between intestinal and liver FABP observed in previous studies.

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41

Alvite, Gabriela, Santiago M. Di Pietro, José A. Santomé, Ricardo Ehrlich, and Adriana Esteves. "Binding properties of Echinococcus granulosus fatty acid binding protein." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1533, no. 3 (October 2001): 293–302. http://dx.doi.org/10.1016/s1388-1981(01)00164-0.

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42

Atshaves, Barbara P., Gregory G. Martin, Heather A. Hostetler, Avery L. McIntosh, Ann B. Kier, and Friedhelm Schroeder. "Liver fatty acid-binding protein and obesity." Journal of Nutritional Biochemistry 21, no. 11 (November 2010): 1015–32. http://dx.doi.org/10.1016/j.jnutbio.2010.01.005.

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43

Thumser, A. E., C. Evans, A. F. Worrall, and D. C. Wilton. "Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein." Biochemical Journal 297, no. 1 (January 1, 1994): 103–7. http://dx.doi.org/10.1042/bj2970103.

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Rat liver fatty acid-binding protein is able to accommodate a wide range of non-polar anions in addition to long-chain fatty acids. The two arginine residues of rat liver fatty acid-binding protein, Arg122 and Arg126, have been mutated and the effect of mutation on ligand binding investigated. No significant decrease in affinity for the fluorescent fatty acid analogue, 11-(5-dimethylaminonaphthalenesulphonyl amino)undecanoic acid, or oleate was observed. However, the apparent affinity for oleoyl-CoA was slightly increased with the mutations Ala122 and Gln122 such that oleoyl-CoA rather than oleate became the preferred ligand for these mutants. Small changes in protein stability were observed with the Arg122 mutations. The lack of notable ionic involvement of the conserved internal residue Arg122 in ligand binding is consistent with the hypothesis that the mode of ligand binding in liver fatty acid-binding protein is markedly different from that of other members of this lipid-binding protein family.

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44

Sheridan, M., T. C. I. Wilkinson, and D. C. Wilton. "Studies on fatty acid-binding proteins. Changes in the concentration of hepatic fatty acid-binding protein during development in the rat." Biochemical Journal 242, no. 3 (March 15, 1987): 919–22. http://dx.doi.org/10.1042/bj2420919.

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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.

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45

Rodilla-Sala, E., G. C. Lunazzi, W. Stremmel, and C. Tiribelli. "BSP-bilirubin binding protein, fatty acid binding protein and bilitranslocase are immunological distinct proteins." Journal of Hepatology 11 (January 1990): S53. http://dx.doi.org/10.1016/0168-8278(90)91545-8.

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46

Wang, Qigui, Hui Li, Shuang Liu, Guihua Wang, and Yuxiang Wang. "Cloning and Tissue Expression of Chicken Heart Fatty Acid-Binding Protein and Intestine Fatty Acid-Binding Protein Genes." Animal Biotechnology 16, no. 2 (January 2005): 191–201. http://dx.doi.org/10.1080/10495390500276882.

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47

Alpers, D. H., N. M. Bass, M. J. Engle, and K. DeSchryver-Kecskemeti. "Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1483, no. 3 (January 2000): 352–62. http://dx.doi.org/10.1016/s1388-1981(99)00200-0.

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48

DeMarco, A. C., P. P. Patterson, R. C. Cantrill, and D. F. Horrobin. "Modification of the fatty acid binding profile of liver fatty acid binding protein (L-FABP)." Journal of Nutritional Biochemistry 4, no. 9 (September 1993): 515–22. http://dx.doi.org/10.1016/0955-2863(93)90087-d.

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49

Podjarny, Alberto, Matthew Blakeley, Michael Haertlein, Andre Mitschler, Alexandra Cousido-Siah, Tatiana Petrova, Benoit Guillot, Roland Stote, Martine Moulin, and Eduardo Howard. "UHR PX and NPC studies of H-FABP water network with tiny perdeuterated crystals." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1200. http://dx.doi.org/10.1107/s2053273314087993.

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We have obtained very detailed information about the internal water molecules in the large internal cavity inside fatty acid binding (FABP) proteins , in the presence of bound fatty acids (FA), by Ultra High Resolution X-Ray Crystallography (UHR) to 0.7 Å and Neutron Protein Crystallography (NPC) to 1.9 Å using a "radically small" (V=0.05 mm3) crystal. These waters form a very well ordered dense cluster of 12 molecules, positioned between the hydrophilic internal wall of the cavity and the fatty acid molecule. This information has been used for a detailed electrostatic analysis based on the charge distribution description modeled in the multipole formalism and on the Atoms in Molecules theory. This information is also being used in molecular dynamics simulations of H-FABP and its complex with FA in order to quantify the energetic contribution of these internal waters to the binding energy. The experiment has been done with oleic acid, coming with the protein expressed in E. Coli. The results have been analyzed in order to understand the interactions between the FA, the internal water and the protein, and in particular the role played by the water molecules in determining the potency and specificity of FA binding to FABPs. The major tool for visualizing the water molecules inside the H-FABP cavity is UHR X-Ray Crystallography combined with NPC. UHR crystallographic structures give the positions of hydrogen and oxygen atoms for well-ordered water molecules. NPC determines hydrogen atom positions, particularly of water molecules which have multiple conformations, leading to the best possible crystallographic model. This model was then complemented by a transferred charge distribution to accurately determine the electrostatic and topological properties in the binding pocket, providing a description of the way water molecules in hydration layer contribute to the binding of ligand, which is essential to understand and model ligand binding.

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50

Luxon, B. A. "Inhibition of binding to fatty acid binding protein reduces the intracellular transport of fatty acids." American Journal of Physiology-Gastrointestinal and Liver Physiology 271, no. 1 (July 1, 1996): G113—G120. http://dx.doi.org/10.1152/ajpgi.1996.271.1.g113.

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Male livers, containing lesser amounts of fatty acid binding protein (FABP), utilize fatty acids more slowly than female livers. Conventional wisdom dictates that FABP stimulates fatty acid use by increasing cytoplasmic transport rates. Previously, we showed that the cytoplasmic diffusion of a fatty acid analogue [12-N-methyl-7-nitrobenzo-2-oxa-1,3-diazol-amino stearate (NBD-stearate)] is faster in female hepatocytes, paralleling the larger amounts of FABP. Sex differences in other cytoplasmic factors could also lead to faster diffusion, independent of FABP levels. The aim of this study was to determine the effect of inhibition of fatty acid binding to FABP on the directly measured intracellular transport rate of NBD-stearate. The binding of NBD-stearate to FABP was reduced by incubating hepatocytes isolated from male and female rats with alpha-bromo-palmitate (0-1,500 microM), a modified long-chain fatty acid that binds to FABP. The inhibition by alpha-bromo-palmitate on NBD-stearate binding to FABP was measured with the use of centrifugation to separate cytosol from cytoplasmic membranes. Laser photobleaching (fluorescence recovery after photobleaching) was used to measure the cytoplasmic diffusion of NBD-stearate in hepatocytes. Alpha-Bromo-palmitate incubation reduced NBD-stearate binding to FABP in a dose-dependent manner. The measured diffusion rate was also reduced in proportion to the degree of binding inhibition. We conclude that cytoplasmic transport of NBD-stearate is modulated by binding to soluble proteins like FABP. FABP enhances diffusive transport by reducing binding to immobile cytosolic membranes.

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