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.

scholarly journals Interaction of LY171883 and other peroxisome proliferators with fatty-acid-binding protein isolated from rat liver

1991 ◽  
Vol 280 (2) ◽  
pp. 387-391 ◽  
Author(s):  
J R Cannon ◽  
P I Eacho
Keyword(s):  
Fatty Acids ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Clofibric Acid ◽  
Peroxisome Proliferation ◽  
Peroxisome Proliferators ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Fatty-acid-binding protein (FABP) is a 14 kDa protein found in hepatic cytosol which binds and transports fatty acids and other hydrophobic ligands throughout the cell. The purpose of this investigation was to determine whether LY171883, a leukotriene D4 antagonist, and other peroxisome proliferators bind to FABP and displace an endogenous fatty acid. [3H]Oleic acid was used to monitor the elution of FABP during chromatographic purification. [14C]LY171883 had a similar elution profile when substituted in the purification, indicating a common interaction with FABP. LY171883 and its structural analogue, LY189585, as well as the hypolipidaemic peroxisome proliferators clofibric acid, ciprofibrate, bezafibrate and WY14,643, displaced [3H]oleic acid binding to FABP. Analogues of LY171883 that do not induce peroxisome proliferation only weakly displaced oleate binding. [3H]Ly171883 bound directly to FABP with a Kd of 10.8 microM, compared with a Kd of 0.96 microM for [3H]oleate. LY171883 binding was inhibited by LY189585, clofibric acid, ciprofibrate and bezafibrate. These findings demonstrate that peroxisome proliferators, presumably due to their structural similarity to fatty acids, are able to bind to FABP and displace an endogenous ligand from its binding site. Interaction of peroxisome proliferators with FABP may be involved in perturbations of fatty acid metabolism caused by these agents as well as in the development of the pleiotropic response of peroxisome proliferation.

Interactions of oleic acid with liver fatty acid binding protein: a carbon-13 NMR study [Erratum to document cited in CA108(7):51580v]

Biochemistry ◽  
1989 ◽  
Vol 28 (8) ◽  
pp. 3628-3628 ◽  
Author(s):  
David P. Cistola ◽  
Mary T. Walsh ◽  
Ronald P. Corey ◽  
James A. Hamilton ◽  
Peter Brecher
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Protein A ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Nmr Study

scholarly journals Studies on the effect of an heterologous fatty acid-binding protein on acyl-CoA oxidase induction in Saccharomyces cerevisiae

1994 ◽  
Vol 301 (2) ◽  
pp. 615-620 ◽  
Author(s):  
I Smaczyńska ◽  
M Skoneczny ◽  
A Kurlandzka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Yeast Cells ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Acyl Coa Oxidase

The participation of fatty acid-binding protein (FABP) in the induction of peroxisomal beta-oxidation of fatty acids was investigated in vivo in an heterologous system. Bovine heart FABP was expressed in Saccharomyces cerevisiae under the control of two different promoters: a constitutive one and an oleic acid-inducible one. Constructs were introduced into yeast cells on multicopy and integrating plasmids. The heterologous FABP was present in yeast cells in two isoforms having pI values of about 5 and was able to bind oleic acid. The heterologous FABP had no significant effect on acyl-CoA oxidase activity at various concentrations of the inducing agent.

scholarly journals Fatty acid-binding protein 5 regulates diet-induced obesity via GIP secretion from enteroendocrine K cells in response to fat ingestion

2015 ◽  
Vol 308 (7) ◽  
pp. E583-E591 ◽  
Author(s):  
Kimitaka Shibue ◽  
Shunsuke Yamane ◽  
Norio Harada ◽  
Akihiro Hamasaki ◽  
Kazuyo Suzuki ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Whole Body ◽  
Dependent Manner ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
K Cells ◽  
Diet Induced Obesity

Gastric inhibitory polypeptide (GIP) is an incretin released from enteroendocrine K cells in response to nutrient intake, especially fat. GIP is one of the contributing factors inducing fat accumulation that results in obesity. A recent study shows that fatty acid-binding protein 5 (FABP5) is expressed in murine K cells and is involved in fat-induced GIP secretion. We investigated the mechanism of fat-induced GIP secretion and the impact of FABP5-related GIP response on diet-induced obesity (DIO). Single oral administration of glucose and fat resulted in a 40% reduction of GIP response to fat but not to glucose in whole body FABP5-knockout (FABP5−/−) mice, with no change in K cell count or GIP content in K cells. In an ex vivo experiment using isolated upper small intestine, oleic acid induced only a slight increase in GIP release, which was markedly enhanced by coadministration of bile and oleic acid together with attenuated GIP response in the FABP5−/− sample. FABP5−/− mice exhibited a 24% reduction in body weight gain and body fat mass under a high-fat diet compared with wild-type (FABP5+/+) mice; the difference was not observed between GIP-GFP homozygous knock-in (GIPgfp/gfp)-FABP5+/+ mice and GIPgfp/gfp-FABP5−/− mice, in which GIP is genetically deleted. These results demonstrate that bile efficiently amplifies fat-induced GIP secretion and that FABP5 contributes to the development of DIO in a GIP-dependent manner.

Effect of clofibric acid and tiadenol on peroxisomal β-oxidation and fatty acid binding protein in intestinal mucosa of rats

1985 ◽  
Vol 78 (3) ◽  
pp. 363-369 ◽  
Author(s):  
Yoichi Kawashima ◽  
Masato Takegishi ◽  
Hatsumi Watanuki ◽  
Haruyo Katoh ◽  
Yuka Tachibana ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Intestinal Mucosa ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Clofibric Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein
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