Showing papers on "Fatty acid-binding protein published in 1992"
TL;DR: 2D gel protein analysis of normal primary keratinocytes cultured for at least 8 d under conditions that promoted incomplete terminal differentiation revealed a strong up-regulation of PA-FABP, psoriasin, calgranulins A and B, and a few other proteins that are highly expressed in psoriatic skin.
251 citations
TL;DR: It is demonstrated here that fatty acids can regulate specific gene expression; mRNAs encoding the fatty acid binding protein adipocyte P2 (aP2) and the Fos-related transcription factor Fra1 are specifically induced at least 20-fold upon treatment of preadipocytes with oleate.
191 citations
TL;DR: The three-dimensional structure of recombinant human muscle fatty acid-binding protein with a bound fatty acid has been solved and refined with x-ray diffraction data and showed the presence of a single bound molecule of a long chain fatty acid within the interior core of the protein.
161 citations
TL;DR: Thermodynamic analysis showed that the free energy of activation for the ffa transfer process arises primarily from an enthalpic component, with only a small entropic contribution, again suggesting the lack of an aqueous phase route of ffa delivery.
83 citations
TL;DR: The Caco-2 cell line will be a useful model system for studying the polarization of FA trafficking/metabolism in enterocytes and defining the role of intracellular fatty acid binding proteins in these processes.
75 citations
TL;DR: It is demonstrated that the rate of transfer of long chain ffa from L-FABP to membranes is substantially affected by aqueous phase variables as well as properties of the ffa ligand itself.
70 citations
TL;DR: Analysis of the amino acid sequence alignment of the MFBs with six mammalian fatty acid-binding proteins revealed a number of shared features: 9 conserved glycines, presumably important in turns of the beta-strands; a basic amino acid in a position corresponding to the residue reported to participate in binding the carboxyl group of the fatty acid.
70 citations
TL;DR: Observations strongly suggest that the intestinal fatty acid-binding protein is a useful biochemical marker for intestinal ischemia, particularly in the early reversible phase.
Abstract: Determination of the serum level of intestinal fatty acid-binding protein has been used to detect rat intestinal ischemia following ligation or 30-min occlusion of the superior mesenteric artery. The normal values were under the minimal detectable level of less than 2 ng/ml in all the 10 rats. The serum fatty acid-binding protein level increased rapidly, to 340.7±54.6, 438.5±40.1, 388.1±37.4, and 292.2±95.7 ng/ml (P<0.01) at 1, 2, 4, and 8 hr after ligation respectively. It also increased, to 347.2±127.7 ng/ml (P<0.01) at 1 hr, after a 30-min transient occlusion and then returned to a normal level. Histological studies showed destruction of the villi, disappearance of the mucosa, and transmural necrosis with the progress of time after ligation, while no remoarkable morphological change was observed following 30-min transieent occlusion. These observations strongly suggest that the intestinal fatty acid-binding protein is a useful biochemical marker for intestinal ischemia, particularly in the early reversible phase.
70 citations
TL;DR: The evidence supports the idea that L-FABP, the target protein of the liver carcinogen, acts specifically in concert with oxygenated metabolites of linoleic acid to modulate the growth of hepatocytes.
Abstract: The hepatic carcinogen N-2-fluorenylacetamide (2-acetylaminofluorene) was shown previously to interact specifically with its target protein, liver fatty acid binding protein (L-FABP), early during hepatocarcinogenesis in rats. In search of the significance of the interaction, rat L-FABP cDNA in the sense and antisense orientations was transfected into a subline of the rat hepatoma HTC cell line that did not express L-FABP. After the transfections, the basal doubling times of the cells were not significantly different. However, at 10(-5)-10(-7) M, linoleic acid, which is an essential fatty acid, a ligand of L-FABP, and the precursor of many eicosanoids and related lipids, stimulated the incorporation of [3H]thymidine in three randomly isolated and stably transfected cell clones that expressed L-FABP, but virtually did not stimulate the incorporation of [3H]thymidine in three L-FABP-nonexpressing clones transfected with the antisense DNA. Linoleic acid at 10(-6) M increased cell number almost 3-fold (38% vs. 14%; P less than 0.0001) and thymidine incorporation nearly 5-fold (23.2% vs. 4.9%; P less than 0.001) in the L-FABP-expressing cells compared to that in the transfected nonexpressing cells. L-FABP acted specifically and cooperatively with linoleic acid, inasmuch as all the proteins other than L-FABP in the transfected L-FABP nonexpressing cells and four other fatty acids (gamma-linolenic acid, dihomo-gamma-linolenic acid, arachidonic acid, and palmitoleic acid) were unable to effect a significant elevation or difference in the level of DNA synthesis that was attributable to the transfection. Metabolism of the linoleic acid to oxygenated derivatives was apparently necessary, since the cyclooxygenase inhibitor indomethacin partly inhibited and the antioxidant lipoxygenase inhibitors nordihydroguariaretic acid and alpha-tocopherol completely abolished the growth stimulation. The evidence supports the idea that L-FABP, the target protein of the liver carcinogen, acts specifically in concert with oxygenated metabolites of linoleic acid to modulate the growth of hepatocytes.
54 citations
TL;DR: Plasma membrane Na/K-ATPase activity in L cells may be regulated in part through expression of cytosolic L-FABP, which appeared to be mediated through alterations in plasma membrane lipids and/or structure.
39 citations
TL;DR: The monoclonal antibody K15/6 represents an organ specific antibody to MFABP which reveals inhibitory action on membrane binding/transport of fatty acids.
TL;DR: The present findings suggest that I‐15P plays a role in the cellular metabolism of steroids.
Abstract: Rat intestinal 15 kDa protein (I-15P) is a member of the family of cytoplasmic fatty acid-binding proteins. Using a specific antiserum against I-15P, we studied the tissue distribution and subcellular localization of this protein in the entire rat body. By immunoblot analysis of cytosolic proteins, I-15P was detected not only in the distal portion of small intestine but also in the ovary and adrenal gland. Immunohistochemically, I-15P was localized to the absorptive epithelial cells as well as a subpopulation of enterochromaffin cells in the intestine, the lutein cells in the ovary, and subpopulations of cortical cells in the adrenal gland. Furthermore, I-15P-like immunoreactivity was also demonstrated in the surface mucous cells of stomach and the granular convoluted tubule cells of submandibular gland. Immuno-electron microscopy showed that the immunoreactivity was confined to the cytoplasmic matrix region, except in the enterochromaffin cells and granular convoluted tubule cells, where it was localized in the secretory granules. The present findings suggest that I-15P plays a role in the cellular metabolism of steroids.© Willey-Liss, Inc.
TL;DR: The methods described very readily identify fatty acid-binding proteins: the fact that even when the sensitivity was increased 500-fold, no evidence was found for the presence of a fatty Acid-binding protein in the inner membrane is consistent with the proposal that fatty acid permeation across the plasma membrane is not protein mediated but occurs by a simple diffusive mechanism.
TL;DR: No significant fatty acid binding by proteins was detected in S. cerevisiae, even when grown on a fatty acid-rich medium, thus indicating that such proteins are not essential to fatty acid metabolism.
Abstract: 1. 1. The presence of soluble proteins with fatty acid binding activity was investigated in cell-free extracts from Saccharomyces cerevisiae and Yarrowia lipolytica cultures. 2. 2. No significant fatty acid binding by proteins was detected in S. cerevisiae , even when grown on a fatty acid-rich medium, thus indicating that such proteins are not essential to fatty acid metabolism. 3. 3. An inducible fatty acid binding protein ( K 0.5 = 3–4 μ M) was found in Y. lipolytica which had grown on a minimal medium with palmitate as the sole source of carbon and energy. 4. 4. The relative molecular mass of this protein was 100,000 as inferred from Sephacryl S-200 gel filtration.
TL;DR: From the abundance of FAHP in tissues with ‘active’ lipid metabolism and the ability to bind fatty acids with high affinity, an involvement o f these proteins in fatty acid metabolism was inferred.
Abstract: Introduction The cardiac fatty acid-binding protein is one type of a family of nonenzymic proteins [ I , 21 that bind hydrophobic ligands. The localization of these fatty acid-binding proteins (FAHPs) is mainly cytosolic kvith concentrations up to 5% 13 I of soluble proteins. A closer inspection of the subcellular distribution by means of immunohistochemical methods and e.1.i.s.a. [ 41, however. reveals a type-specific compartmentation of FAHPs, e.g. the cardiac-type FAHP is associated with myofibrils and mitochondrial matrix, whereas in hepatocytes the so-called hepatic-type FAHP is associated with the endoplasmic reticulum and the outer membrane of mitochondria [S]. Interestingly, both FAHP types are also found inside the nucleus 14, 51. From the abundance of FAHP in tissues with ‘active’ lipid metabolism and the ability to bind fatty acids with high affinity, an involvement o f these proteins in fatty acid metabolism was inferred. Already in the early days of FAHP research a variety of studies related to this field was undertaken even though the proteins were often not available in pure form and structurally not characterized. With the advent of detailed structural information functions were proposed in a more rationalized manner for the nonenzymic FAHPs, e.g. roles in signal transduction and in regulation of cell growth.
TL;DR: By delipidation, the FABP's a-helix was significantly increased and the β-sheet was in turn decreased, as demonstrated by circular dichroism (CD) and one- and two-dimensional nuclear magnetic resonance ( 1 H-NMR) spectroscopy.
Abstract: Only a single isoform (pI 5.0) of multiple rat liver fatty acid binding protein (FABP) was isolated and used throughout this investigation. When the final FABP preparation was partly freed of fatty acids by a mild delipidation technique using Lipidex, the secondary and tertiary structures were significantly changed, as demonstrated by circular dichroism (CD) and one- and two-dimensional nuclear magnetic resonance ( 1 H-NMR) spectroscopy. By delipidation, the FABP's a-helix was significantly increased and the β-sheet was in turn decreased
TL;DR: A fatty acid binding protein (FABP) was isolated from chicken liver and intestinal mucosa which bound [4,4′-bis([ 3 H]methylsulfonyl)-2,2′, 5,5,5′tetrachlorobiphenyl[(CT 3 SO 2 ) 2 TCB] or 3,5-dichlorophenyl [ 14 C]methyl sulfone (DCP[14 C]MSO 2 ).
Patent•
16 Mar 1992
TL;DR: In this article, a method of quantitative assay for a substrate such as triglyceride capable of undergoing enzymatic hydrolysis to release long chain fatty acids in an albumin-containing clinical sample comprises incubating the albumin containing clinical sample with an enzyme such as lipase which acts upon the substrate to be assayed under conditions effective to release fatty acid therefrom.
Abstract: A method of quantitative assay for a substrate such as triglyceride capable of undergoing enzymatic hydrolysis to release long chain fatty acids in an albumin-containing clinical sample comprises incubating the albumin-containing clinical sample with an enzyme such as lipase which acts upon the substrate to be assayed under conditions effective to release fatty acid therefrom, causing the fatty acid thus released to bind to a fatty acid binding protein (FABP) and assaying the binding of the fatty acid to the FABP.
01 Jan 1992
TL;DR: The physical properties of fatty acids in aqueous Systems, the interaction of fatty acid with key structures in the blood (albumin, lipoproteins, and cell membranes), and the interactionof fatty acids with intracellular constituents, specifically fatty acid binding proteins and membranes are covered.
Abstract: This overview covers three topics: 1) the physical properties of fatty acids in aqueous systems, 2) the interaction of fatty acids with key structures in the blood (albumin, lipoproteins, and cell membranes), and 3) the interaction of fatty acids with intracellular constituents, specifically fatty acid binding proteins and membranes
Journal Article•
Journal Article•
TL;DR: Rat liver fatty acid binding protein (FABP) was purified to homogeneity by procedures including Sephadex G-100 and DEAE-cellulose column chromatographies and used as the final preparation.
TL;DR: The differential distribution of cellular brain proteins with the capacity to bind fatty acids in gray matter and white matter suggests that this activity could be related to glial cells or to cell related structures such as myelin.
TL;DR: A highly sensitive, simple and reproducible method for the quantitative determination of fatty acid binding protein in rat liver by post-column high-performance liquid chromatography with fluorescence detection is presented.
Abstract: A highly sensitive, simple and reproducible method for the quantitative determination of fatty acid binding protein in rat liver by post-column high-performance liquid chromatography with fluorescence detection is presented. Fatty acid binding protein in rat liver cytosols is separated by gel-permeation column chromatography, which is followed by fluorescence detection. The detection makes use of the fluorescence enhancement observed when a fluorescent fatty acid probe, dansylundecanoic acid, binds to fatty acid binding protein. The method is rapid, simple to perform and highly sensitive. The method was applied to the determination of fatty acid binding protein in liver from control and hypolipidaemic drug treated rats.
TL;DR: Growth and functional maturation of porcine small intestine was characterized in relation to stage of perinatal development and FABP activity of mucosa from the proximal half of intestine displayed a cubic pattern of change.
TL;DR: The less polar fluorescent analogue of ATP, 2′(3′)‐trinitrophenyl‐5′‐triphosphate bound to rat liver fatty acid‐binding protein with high affinity and 1:1 molar stoichiometry and was displaced by oleic acid and oleoyl CoA.
Journal Article•