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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: Results indicate that fatty acids traverse the plasma membrane and are bound cytoplasmically by the liver fatty acid binding protein, as well as other proteins in the cell, which supports a model in which cy toplasmic lipid carriers solubilize fatty acids as a step in their metabolic utilization.

21 citations

Journal ArticleDOI
TL;DR: The effect of dietary fatty acids on the populational pattern of insulin resistance is not independent of the Ala54Thr polymorphism of FABP2, and an interaction existed between this polymorphism and the intake of dietary fats in a population with a high intake of monounsaturated fatty acids.

21 citations

Journal ArticleDOI
TL;DR: Alteration of hepatic FABP mRNA expression by growth hormone in rat liver may be important in the complex regulation of fatty acid uptake and metabolism.
Abstract: Hepatic fatty acid-binding protein (FABP) is one of several abundant proteins which may participate in fatty acid uptake and utilization. Using differential hybridization to screen for growth hormone-responsive gene products, a complementary deoxyribonucleic acid (cDNA) was isolated which proved to be a hepatic FABP cDNA fragment. Hypophysectomy caused a 60% reduction in hepatic FABP messenger ribonucleic acid (mRNA) levels in rat liver, and growth hormone administration to hypophysectomized rats resulted in restoration of the expression of hepatic FABP mRNA. Other pituitary hormones did not alter these changes in expression. The response to growth hormone occurred within 4 hours of administration. During development, expression of hepatic FABP mRNA in rat liver was low in late fetal life, with increases to 40% of adult values by day 2 of life. Significant increases to adult levels did not occur until after day 25, when weaning is essentially completed. Alteration of hepatic FABP mRNA expression by growth...

21 citations

BookDOI
01 Jan 1990
TL;DR: An overview of studies on fatty acid-binding proteins and their role in cardiac fatty acid oxidation, regulation and relationship to the zonation of fatty acid metabolism.
Abstract: Historic overview of studies on fatty acid-binding proteins.- Detection, tissue distribution and (sub)cellular localization of fatty acid-binding protein types.- Fatty acid oxidation capacity and fatty acid-binding protein content of different cell types isolated from rat heart.- Localization of liver fatty acid-binding protein and its mRNA in the liver and jejunum of rats: an immunohistochemical and in situ hybridization study.- Amino acid sequence and some ligand binding properties of fatty acid-binding protein from bovine brain.- Type-specific immunodetection of human heart fatty acid-binding protein with polyclonal anti-peptide antibodies.- Bifunctional lipid-transfer: fatty acid-binding proteins in plants.- Characteristics of fatty acid-binding proteins and their relation to mammary-derived growth inhibitor.- Expression of a functionally active cardiac fatty acid-binding protein in the yeast, Saccharomyces cerevisiae.- Expression of fatty acid-binding protein from bovine heart in Escherichia coli.- Expression of rat intestinal fatty acid-binding protein in E. coli and its subsequent structural analysis: a model system for studying the molecular details of fatty acid-protein interaction.- Crystal structure of chicken liver basic fatty acid-binding protein at 2.7 A resolution.- 13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proteins produced in the intestinal epithelium.- Assay of the binding of fatty acids by proteins: evaluation of the Lipidex 1000 procedure.- Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels.- Revision of the amino acid sequence of human heart fatty acid-binding protein.- The chemical modification of cysteine-69 of rat liver fatty acid-binding protein (FABP): a fluorescence approach to FABP structure and function.- A comparison of heart and liver fatty acid-binding proteins: interactions with fatty acids and possible functional differences studies with fluorescent fatty acid analogues.- Role of fatty acid-binding proteins in cardiac fatty acid oxidation.- Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen-derived free radicals.- Fatty acid-binding protein expression in the liver: its regulation and relationship to the zonation of fatty acid metabolism.- Effects of linoleic and gamma-linoleic acids (efamol evening primrose oil) on fatty acid-binding proteins of rat liver.- Quantitation of plasma membrane fatty acid-binding protein by enzyme dilution and monoclonal antibody based immunoassay.- The membrane fatty acid-binding protein is not identical to mitochondrial glutamic oxaloacetic transaminase (mGOT).- Renal palmitate transport: possible sites for interaction with a plasma membrane fatty acid-binding protein.- Fatty acid-binding to erythrocyte ghost membranes and transmembrane movement.- Acyl-CoA-binding (ACBP) and its relation to fatty acid-binding protein (FABP): an overview.- Liver fatty acid-binding protein in two cases of human lipid storage.- Nomenclature of fatty acid-binding proteins.- Cellular fatty acid-binding proteins: Current concepts and future directions.

21 citations

Journal ArticleDOI
TL;DR: Stopped-flow experiments indicate that a rate-limiting step exists before the ligand association and this step corresponds to the conversion of the closed form to the open one, and the presence of two excited states: one is native-like, but the other adopts a locally unfolded structure.
Abstract: Fatty acid binding proteins are responsible for the transportation of fatty acids in biology. Despite intensive studies, the molecular mechanism of fatty acid entry to and exit from the protein cavity is still unclear. Here a cap-closed variant of human intestinal fatty acid binding protein was generated by mutagenesis, in which the helical cap is locked to the β-barrel by a disulfide linkage. Structure determination shows that this variant adopts a closed conformation, but still uptakes fatty acids. Stopped-flow experiments indicate that a rate-limiting step exists before the ligand association and this step corresponds to the conversion of the closed form to the open one. NMR relaxation dispersion and H-D exchange data demonstrate the presence of two excited states: one is native-like, but the other adopts a locally unfolded structure. Local unfolding of helix 2 generates an opening for ligands to enter the protein cavity, and thus controls the ligand association rate.

21 citations


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