Modulation of fatty acid-binding capacity of heart fatty acid-binding protein by oxygen ? derived free radicals

1990 ◽  
Vol 98 (1-2) ◽  
Author(s):  
RandallM. Jones ◽  
M. Renuka Prasad ◽  
DipakK. Das
Keyword(s):  
Free Radicals ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Capacity ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Oxygen Derived Free Radicals

scholarly journals Localization of a portion of the liver isoform of fatty-acid-binding protein (L-FABP) to peroxisomes

2006 ◽  
Vol 394 (2) ◽  
pp. 475-484 ◽  
Author(s):  
Vasily D. Antonenkov ◽  
Raija T. Sormunen ◽  
Steffen Ohlmeier ◽  
Leen Amery ◽  
Marc Fransen ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Lipid Metabolism ◽  
Fatty Acid Binding Protein ◽  
Binding Capacity ◽  
Binding Protein ◽  
Matrix Proteins ◽  
Protein L ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The liver isoform of fatty-acid-binding protein (L-FABP) facilitates the cellular uptake, transport and metabolism of fatty acids and is also involved in the regulation of gene expressions and cell differentiation. Consistent with these functions, L-FABP is predominantly present in the cytoplasm and to a lesser extent in the nucleus; however, a significant portion of this protein has also been detected in fractions containing different organelles. More recent observations, notably on L-FABP-deficient mice, indicated a possible direct involvement of L-FABP in the peroxisomal oxidation of long-chain fatty acids. In order to clarify the links between L-FABP and peroxisomal lipid metabolism, we reinvestigated the subcellular distribution of the protein. Analytical subcellular fractionation by a method preserving the intactness of isolated peroxisomes, two-dimensional gel electrophoresis of peroxisomal matrix proteins combined with MS analysis, and immunoelectron microscopy of liver sections demonstrate the presence of L-FABP in the matrix of peroxisomes as a soluble protein. Peroxisomal L-FABP was highly inducible by clofibrate. The induction of L-FABP was accompanied by a marked increase in the binding capacity of peroxisomal matrix proteins for oleic acid and cis-parinaric acid. The peroxisomal β-oxidation of palmitoyl-CoA and acyl-CoA thioesterase activity were stimulated by L-FABP, indicating that the protein modulates the function of peroxisomal lipid-metabolizing enzymes. The possible role of intraperoxisomal L-FABP in lipid metabolism is discussed.

scholarly journals Regulation of hepatic level of fatty-acid-binding protein by hormones and clofibric acid in the rat

1994 ◽  
Vol 297 (3) ◽  
pp. 581-584 ◽  
Author(s):  
S Nakagawa ◽  
Y Kawashima ◽  
A Hirose ◽  
H Kozuka
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Capacity ◽  
Binding Protein ◽  
Clofibric Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Adrenalectomized Rats ◽  
Hepatic Level

Regulation of the hepatic level of fatty-acid-binding protein (FABP) by hormones and p-chlorophenoxyisobutyric acid (clofibric acid) was studied. The hepatic level of FABP, measured as the oleic acid-binding capacity of the cytosolic FABP fraction, was decreased in streptozotocin-diabetic rats. The level of FABP was markedly increased in adrenalectomized rats, and the elevation was prevented by the administration of dexamethasone. Hypothyroidism decreased the level of FABP and hyperthyroidism increased it. A high correlation between the incorporation of [14C]oleic acid in vivo into hepatic triacylglycerol and the level of FABP was found for normal, diabetic and adrenalectomized rats. The level of FABP was increased by administration of clofibric acid to rats in any altered hormonal states, as was microsomal 1-acylglycerophosphocholine (1-acyl-GPC) acyltransferase, a peroxisome-proliferator-responsive parameter. These results suggest that the hepatic level of FABP is under regulation by multiple hormones and that clofibric acid induces FABP and 1-acyl-GPC acyltransferase by a mechanism which may be distinct from that by which hormones regulate the level of FABP.

Cytoplasmic transport of fatty acids in rat enterocytes: role of binding to fatty acid-binding protein

1999 ◽  
Vol 277 (2) ◽  
pp. G361-G366 ◽  
Author(s):  
Bruce A. Luxon ◽  
Michael T. Milliano
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Intracellular Transport ◽  
Fatty Acid Binding Protein ◽  
Binding Capacity ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Cytoplasmic Transport ◽  
Rat Enterocytes

The intracellular movement of fatty acids is thought to be facilitated through codiffusion with fatty acid-binding protein (FABP). This facilitation may occur by decreasing binding to immobile membranes, leading to faster cytoplasmic diffusion. The aims of this study were to measure the intracellular transport of 12- N-methyl-(7-nitrobenzo-2-oxa-1,3-diazol)aminostearate (NBD-stearate) in villus rat enterocytes and to determine 1) the mechanism of its cytoplasmic transport and 2) if its transport rate correlated with the known variation of FABP binding capacity along the length of the small intestine. Two-dimensional laser photobleaching was used to measure the movement of a fluorescent fatty acid NBD-stearate in enterocytes isolated from different segments of rat intestine. The fraction of NBD-stearate found in the cytostol of enterocytes was determined by differential centrifugation. Cytoplasmic transport of NBD-stearate occurred solely by diffusion and not by convection. Diffusion was homogeneous (nondirectional), consistent with isotropic diffusion. The diffusion rate varied with location along the intestine, correlating with the local FABP concentration and measured cytosolic binding. We conclude that cytoplasmic proteins like FABP promote the intracellular transport of fatty acids by enhancing their diffusive flux. We suggest that facilitation is not specific for a particular cell type but occurs in a variety of cells that transport fatty acids and may contain different types of FABP.

Calcium-dependent release of adipocyte fatty acid binding protein from human adipocytes

2014 ◽  
Vol 122 (03) ◽  
Author(s):  
I Schlottmann ◽  
M Ehrhart-Bornstein ◽  
M Wabitsch ◽  
SR Bornstein ◽  
V Lamounier-Zepter
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Human Adipocytes ◽  
Fatty Acid Binding ◽  
Calcium Dependent ◽  
Acid Binding Protein

Biochemical and Histochemical Studies of Liver Fatty Acid Binding Protein in Alcohol-Treated Rats.

1993 ◽  
Vol 14 (3) ◽  
pp. 171-181
Author(s):  
Shigeya WATANABE ◽  
Yoshio WAKATSUKI ◽  
Hideyuki YOSHIOKA ◽  
Masami INADA ◽  
Teruo ONO ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein
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