Human fetal liver fatty acid binding proteins. Role on glucose-6-phosphate dehydrogenase activity.
TL;DR: F fetal liver FABPs play a regulatory role in critical aspects of cellular physiology during human embryogenesis and protect glucose-6-phosphate dehydrogenase from the feed-back inhibition exerted by added palmitoyl-CoA and oleate.
About: This article is published in Biochimica et Biophysica Acta.The article was published on 1989-04-03. It has received 16 citations till now. The article focuses on the topics: Fatty acid synthesis & Fatty acid-binding protein.
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TL;DR: Article de synthese sur les donnees recentes de caracteristiques structurales et physicochimiques de divers types of proteines de liaison aux acides gras, avec la signification physiologique de ces diversites.
366 citations
TL;DR: A considerable body of indirect evidence is provided supporting a broad role for the FABP in the intracellular transport and metabolism of long-chain fatty acids and the existence of structure- and tissue-specific specialization of function among different members of the F ABP gene family.
Abstract: Cytosolic fatty acid binding proteins (FABP) belong to a gene family of which eight members have been conclusively identified. These 14–15 kDa proteins are abundantly expressed in a highly tissue-specific manner. Although the functions of the cytosolic FABP are not clearly established, they appear to enhance the transfer of long-chain fatty acids between artificial and native lipid membranes, and also to have a stimulatory effect on a number of enzymes of fatty acid metabolism in vitro. These findings, as well as the tissue expression, ligand binding properties, ontogeny and regulation of these proteins provide a considerable body of indirect evidence supporting a broad role for the FABP in the intracellular transport and metabolism of long-chain fatty acids. The available data also support the existence of structure- and tissue-specific specialization of function among different members of the FABP gene family. Moreover, FABP may also have a possible role in the modulation of cell growth and proliferation, possibly by virtue of their affinity for ligands such as prostaglandins, leukotrienes and fatty acids, which are known to influence cell growth activity. FABP structurally unrelated to the cytosolic gene family have also been identified in the plasma membranes of several tissues (FABPpm). These proteins have not been fully characterized to date, but strong evidence suggests that they function in the transport of long-chain fatty acids across the plasma membrane.
167 citations
TL;DR: Which FABPs form biochemically defined or true isoforms versus FABP that form additional forms, operationally defined as isoforms, is critically evaluated.
127 citations
TL;DR: The identity, nature, function, and pathobiology of these fascinating newly discovered long-chain fatty acyl-CoA binding proteins are explored.
Abstract: The physiological role of long-chain fatty acyl-CoA is thought to be primarily in intermediary metabolism of fatty acids. However, recent data show that nM to μM levels of these lipophilic molecules are potent regulators of cell functionsin vitro. Although long-chain fatty acyl-CoA are present at several hundred μM concentration in the cell, very little long-chain fatty acyl-CoA actually exists as free or unbound molecules, but rather is bound with high affinity to membrane lipids and/or proteins. Recently, there is growing awareness that cytosol contains nonenzymatic proteins also capable of binding long-chain fatty acyl-CoA with high affinity. Although the identity of the cytosolic long-chain fatty acyl-CoA binding protein(s) has been the subject of some controversy, there is growing evidence that several diverse nonenzymatic cytosolic proteins will bind long-chain fatty acyl-CoA. Not only does acyl-CoA binding protein specifically bind medium and long-chain fatty acyl-CoA (LCFA-CoA), but ubiquitous proteins with multiple ligand specificities such as the fatty acid binding proteins and sterol carrier protein-2 also bind LCFA-CoA with high affinity. The potential of these acyl-CoA binding proteins to influence the level of free LCFA-CoA and thereby the amount of LCFA-CoA bound to regulatory sites in proteins and enzymes is only now being examined in detail. The purpose of this article is to explore the identity, nature, function, and pathobiology of these fascinating newly discovered long-chain fatty acyl-CoA binding proteins. The relative contributions of these three different protein families to LCFA-CoA utilization and/or regulation of cellular activities are the focus of new directions in this field.
126 citations
TL;DR: Rat L-FABP isoforms differ markedly in both structure and ligand binding function, and displacement studies indicated that each isoform displayed distinct specificities for fatty acid/fatty acyl CoA chain length and unsaturation.
Abstract: Although native rat liver fatty acid binding protein (L-FABP) is composed of isoforms differing in isoelectric point, their comparative structure and function are unknown. These properties of apo- ...
96 citations
References
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TL;DR: It is concluded that palmitoyl-CoA, unlike the synthetic anionic detergent, perturbs the dehydrogenase subunit structure in a controlled manner which may be important for regulating the activity of lipogenic enzymes.
91 citations
TL;DR: It appears that the small cytosolic fatty acid binding proteins have evolved structural features necessary for lipid-protein interaction which are different from those present in some familiar and better studied extracellular sequences.
85 citations
TL;DR: One of the main objectives of the symposium on ‘Transport by Proteins’ has been to provide a general basis for a meeting which would bring together workers from related fields, thus promoting mutual stimulation and exchange of ideas and new techniques.
85 citations
TL;DR: Using immunoblots and ELISA and immunoblotting techniques, it was determined that rat heart FABP was localized in the cytosol with no detectable intramitochondrial material and Comparisons between myoglobin and FABp showed thatFABP appeared earlier than myoglobin in development, but myoglobin was more abundant than FABB at birth.
81 citations
TL;DR: When a 100000 ×g supernatant from bovine heart was incubated with [1-14C]oleic acid and subjected to isoelectric focusing, two fatty acid binding proteins (FABPs) with isoeLECTric points at 4.9 and 5.1 were detected.
Abstract: When a 100000 ×g supernatant from bovine heart was incubated with [1-14C]oleic acid and subjected to isoelectric focusing, two fatty acid binding proteins (FABPs) with isoelectric points at 4.9 and 5.1 were detected.
The proteins were purified on a large scale first by heat and acid precipitation of a postmitochondrial supernatant, as well as fractionation with ammonium sulfate, then by alternate application of ion-exchange and gel chromatography. The procedure afforded around 60 mg pure proteins from 1.5 kg fresh heart muscle.
Relative molecular masses of 15 300 ± 1600 for both proteins were derived from sodium dodecyl sulfate/polyacrylamide gel electrophoresis, gel chromatography, sedimentation velocity as well as from amino acid analysis. Up to 50% of the proteins' secondary structures consisted of β-sheet. N-termini of the peptide chains were blocked; the amino acid compositions of the two proteins were similar, but differed considerably from those of the two FABPs isolated from bovine liver [Haunerland et al. (1984) Hoppe Seyler's Z. Physiol. Chem. 365, 365–376]. Whereas hepatic FABPs changed their pI upon binding fatty acids, cardiac FABPs did not. Cardiac FABPs were immunologically identical, but did not cross-react with hepatic proteins.
A reversible, concentration-dependent self-association reported for FABP from pig heart [Fournier et al. (1983) Biochemistry 22, 1863–1872] was not observed for FABP from bovine heart. Changes of concentration did not alter secondary structure, intrinsic fluorescence or the sedimentation coefficient of the protein.
70 citations