Fatty acid binding protein isoforms: structure and function
TL;DR: Which FABPs form biochemically defined or true isoforms versus FABP that form additional forms, operationally defined as isoforms, is critically evaluated.
About: This article is published in Chemistry and Physics of Lipids.The article was published on 1998-03-01. It has received 127 citations till now. The article focuses on the topics: Gene isoform.
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TL;DR: This review deals with the recent progress related to the origin and differentiation of the oligodendrocytes, their relationships to other neural cells, and functional neuroglial interactions under physiological conditions and in demyelinating diseases.
Abstract: Oligodendrocytes, the myelin-forming cells of the central nervous system (CNS), and astrocytes constitute macroglia. This review deals with the recent progress related to the origin and differentiation of the oligodendrocytes, their relationships to other neural cells, and functional neuroglial interactions under physiological conditions and in demyelinating diseases. One of the problems in studies of the CNS is to find components, i.e., markers, for the identification of the different cells, in intact tissues or cultures. In recent years, specific biochemical, immunological, and molecular markers have been identified. Many components specific to differentiating oligodendrocytes and to myelin are now available to aid their study. Transgenic mice and spontaneous mutants have led to a better understanding of the targets of specific dys- or demyelinating diseases. The best examples are the studies concerning the effects of the mutations affecting the most abundant protein in the central nervous myelin, the p...
1,637 citations
Cites background from "Fatty acid binding protein isoforms..."
...P2 is a true fatty acid-binding protein isoform (543)....
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TL;DR: It is demonstrated that FXR/BAR is critical for bile acid and lipid homeostasis by virtue of its role as an intracellular bile Acid sensor.
1,613 citations
Cites background from "Fatty acid binding protein isoforms..."
...Liver fatty acid binding protein (L-FABP), a member of the 14 kDa supergene family of cytosolic lipophilic binding proteins (Schroeder et al., 1998), may facilitate BA uptake and trafficking in hepatocytes and/ or serve as an intracellular buffer to protect against the harmful detergent effects of BAs....
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...Liver fatty acid binding protein (L-FABP), a member of the 14 kDa supergene family of cytosolic lipophilic binding proteins (Schroeder et al., 1998), may facilitate BA uptake and trafficking in hepatocytes and/ or serve as an intracellular buffer to protect against the harmful detergent effects of…...
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TL;DR: A revised nomenclature for the major membrane proteins is proposed and discussed in relation to earlier schemes, and it is recommended that proteins be assigned specific names as they are identified by molecular cloning and sequencing techniques.
374 citations
TL;DR: The sharing of control between CPTI and other enzymes allows for flexible regulation of metabolism and the ability to rapidly adapt beta-oxidation flux to differing requirements in different tissues.
349 citations
TL;DR: Using specific extraction procedures, two major lipid binding protein families, lipid transfer proteins (nsLTP) and indolines have been isolated from cereal kernels, showing ability to synergistically enhancing the antifungal properties of thionins, in vitro.
325 citations
References
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TL;DR: The observations that the ryanodine-senstitive Ca2+-release channel is regulated by long-chain acyl-CoA esters in the presence of a molar excess of acyl -CoA binding protein and that acetyl- coA carboxylase, the AMP kinase kinase and the Escherichia coli transcription factor FadR are affected by low nanomolar concentrations of Acyl- CoA indicate that long- chain acyl
Abstract: The intracellular concentration of free unbound acyl-CoA esters is tightly controlled by feedback inhibition of the acyl-CoA synthetase and is buffered by specific acyl-CoA binding proteins. Excessive increases in the concentration are expected to be prevented by conversion into acylcarnitines or by hydrolysis by acyl-CoA hydrolases. Under normal physiological conditions the free cytosolic concentration of acyl-CoA esters will be in the low nanomolar range, and it is unlikely to exceed 200 nM under the most extreme conditions. The fact that acetyl-CoA carboxylase is active during fatty acid synthesis (Ki for acyl-CoA is 5 nM) indicates strongly that the free cytosolic acyl-CoA concentration is below 5 nM under these conditions. Only a limited number of the reported experiments on the effects of acyl-CoA on cellular functions and enzymes have been carried out at low physiological concentrations in the presence of the appropriate acyl-CoA-buffering binding proteins. Re-evaluation of many of the reported effects is therefore urgently required. However, the observations that the ryanodine-senstitive Ca2+-release channel is regulated by long-chain acyl-CoA esters in the presence of a molar excess of acyl-CoA binding protein and that acetyl-CoA carboxylase, the AMP kinase kinase and the Escherichia coli transcription factor FadR are affected by low nanomolar concentrations of acyl-CoA indicate that long-chain acyl-CoA esters can act as regulatory molecules in vivo. This view is further supported by the observation that fatty acids do not repress expression of acetyl-CoA carboxylase or Delta9-desaturase in yeast deficient in acyl-CoA synthetase.
653 citations
TL;DR: This chapter focuses on the structural analyses and comparisons between members of a multigene family of hydrophobic ligand-binding proteins and provides a detailed comparison of intra- and extracellular lipid binding proteins with known crystal structures.
Abstract: Publisher Summary This chapter focuses on the structural analyses and comparisons between members of a multigene family of hydrophobic ligand-binding proteins. It discusses the structural motif, general characteristics of the binding cavity, ligand entry, and the portal hypothesis and provides a detailed comparison of intra- and extracellular lipid binding proteins with known crystal structures. The members of this family are referred as lipid-binding proteins (LBPs). This collection of proteins can be subdivided into two groups: the intracellular lipid-binding protein family (iLBP) and the extracellular lipid binding protein family (eLBP). The comparison primarily deals with the iLBP branch because this family is becoming structurally well characterized. However, the structural comparisons are extended to some members of the eLBP family because the basic structural motif used to bind hydrophobic ligands applies to both. The products of hydrolysis of the intestinal lipids, including fatty acids, cholesterol, monoglycerides, and lysophospholipids, have very low solubilities and are absorbed by biliary micelles in the gut. These micelles diffuse through the glycocalyx, which stabilizes an unstirred water layer at the surface of the enterocyte. The chapter concludes with a discussion of the results of site-directed mutagenesis studies, the thermodynamics of lipid binding, and considerations of protein stability and folding.
466 citations
TL;DR: It is concluded that the threonine-containing protein may increase absorption and/or processing of dietary fatty acids by the intestine and thereby increase fat oxidation, which has been shown to reduce insulin action.
Abstract: The intestinal fatty acid binding protein locus (FABP2) was investigated as a possible genetic factor in determining insulin action in the Pima Indian population. A polymorphism at codon 54 of FABP2 was identified that results in an alanine-encoding allele (frequency 0.71) and a threonine-encoding allele (frequency 0.29). Pimas who were homozygous or heterozygous for the threonine-encoding allele were found to have a higher mean fasting plasma insulin concentration, a lower mean insulin-stimulated glucose uptake rate, a higher mean insulin response to oral glucose and a mixed meal, and a higher mean fat oxidation rate compared with Pimas who were homozygous for the alanine-encoding allele. Since the FABP2 threonine-encoding allele was found to be associated with insulin resistance and increased fat oxidation in vivo, we further analyzed the FABP2 gene products for potential functional differences. Titration microcalorimetry studies with purified recombinant protein showed that the threonine-containing protein had a twofold greater affinity for long-chain fatty acids than the alanine-containing protein. We conclude that the threonine-containing protein may increase absorption and/or processing of dietary fatty acids by the intestine and thereby increase fat oxidation, which has been shown to reduce insulin action.
375 citations
TL;DR: This study disagrees with earlier investigations in finding that equilibrium binding of FA to FABPs is a sensitive function of FA type and FABP tissue origin and that FA-FABP dissociation constants are submicromolar.
269 citations
TL;DR: The abundance of FABP, its importance in the cytosolic binding of endogenous as well as exogenous fatty acids, and its demonstrated correlation with rates of hepatocyte fatty acid utilization provide additional evidence for its relationship to the cellular metabolism of long chain fatty acids.
265 citations