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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 expression and antioxidative function of liver fatty acid binding protein was investigated using the bile-duct ligated model of cholestasis to find that it likely has important antioxidant function during hepatocellular oxidative stress.

48 citations

Journal ArticleDOI
TL;DR: The isolation and amino acid sequence determination of two FABPs from axolotl (Ambistoma mexicanum) liver indicate that they are paralogous proteins and indicate distinct functional properties of both liver FABP types.
Abstract: Up until now, the primary structure of fatty-acid-binding proteins (FABPs) from the livers of four mammalian (rat, human, cow and pig) and three nonmammalian (chicken, catfish and iguana) species has been determined Based on amino acid sequence comparisons, it has been suggested that mammalian and nonmammalian liver FABPs may be paralogous proteins that originated by gene duplication, rather than as a consequence of mutations of the same gene In this paper we report the isolation and amino acid sequence determination of two FABPs from axolotl (Ambistoma mexicanum) liver One of them is similar to mammalian liver FABPs (L-FABPs) and the other to chicken, catfish and iguana liver FABPs (Lb-FABPs) The finding of both L-FABP and Lb-FABP in a single species, as reported here, indicates that they are paralogous proteins The time of divergence of these two liver FABP types is estimated to be of ≈ 694 million years ago The ligand-binding properties of axolotl liver FABPs were studied by means of parinaric-acid-binding and parinaric-acid-displacement assays L-FABP binds two fatty acids per molecule but Lb-FABP displays a fatty-acid-conformation-dependent binding stoichiometry; L-FABP shows a higher affinity for fatty acids, especially oleic acid, while Lb-FABP has a higher affinity for other hydrophobic ligands, especially retinoic acid In addition, the tissue-expression pattern is different, L-FABP is present in liver and intestinal mucosa while the expression of Lb-FABP is restricted to liver Data indicate distinct functional properties of both liver FABP types

48 citations

Journal ArticleDOI
TL;DR: It is concluded that αS is not likely to act as an intracellular FA carrier, however, binding to negatively charged membranes appears to be an intrinsic property of αS that is most likely related to its physiological role(s) in the cell.

48 citations

Journal ArticleDOI
TL;DR: The findings indicate specific binding of FA to one or more sites in the CRD, and speculate that the binding of SP-D to the fatty acyl chains of surfactant lipids, microbial ligands, or other complex lipids contributes to the diverse biological functions ofSP-D in vivo.
Abstract: Surfactant Protein D (SP-D) plays important roles in antimicrobial host defense, inflammatory and immune regulation, and pulmonary surfactant homeostasis. The best-characterized endogenous ligand is phosphatidylinositol; however, this lipid interaction at least in part involves the carbohydrate moiety. In this study we observed that SP-D binds specifically to saturated, unsaturated, and hydroxylated fatty acids (FA). Binding of biotinylated-SP-D to FAs or biotinylated FA to SP-D was dose-dependent, saturable, and specifically competed by the corresponding unlabeled probe. Specific binding to FA chains was also demonstrated by solution phase competition for FA binding to acrylodan-labeled FA binding protein (ADIFAB), and by overlay of thin layer chromatograms with SP-D. Maximal binding to FA was dependent on calcium, and binding was localized to the neck and carbohydrate recognition domains (CRD) using recombinant trimeric neck+CRDs. Saccharide ligands showed complex, dose-dependent effects on FA binding, and FAs showed dose- and physical state-dependent effects on the binding of SP-D to mannan. In addition, CD spectroscopy suggested alterations in SP-D structure associated with binding to monomeric FA. Together, the findings indicate specific binding of FA to one or more sites in the CRD. We speculate that the binding of SP-D to the fatty acyl chains of surfactant lipids, microbial ligands, or other complex lipids contributes to the diverse biological functions of SP-D in vivo.

48 citations

Journal ArticleDOI
TL;DR: No fatty acid binding protein was observed in the six elasmobranchs studied and the results with crustaceans were ambiguous, so the aspects of functional evolution of serum albumin are discussed.
Abstract: 1. 1. A technique is described to study the binding of fatty acids to albumin in serum by use of thin-layer gel filtration. 2. 2. The presence of a protein which binds [14C]oleate is established in higher vertebrates, teleosts and a petromyzone. 3. 3. No fatty acid binding protein was observed in the six elasmobranchs studied and the results with crustaceans were ambiguous. 4. 4. The aspects of functional evolution of serum albumin are discussed.

48 citations


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