Liver cytosolic fatty acid-binding proteins

Brandes, Ruth; Arad, Rivka

doi:10.1016/0005-2760(83)90037-1

Cited by 26 publications

(8 citation statements)

References 23 publications

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“…In the present study, the influence of three hormones and clofibric acid on the hepatic level of FABP was investigated. In agreement with a previous study [32], the hepatic level of FABP was lowered in diabetic rats, although insulin failed to prevent the level of FABP falling, suggesting that FABP is not so sensitive to insulin level as an insulin-responsive parameter such as stearoyl-CoA desaturase [33]. The FABP level was confirmed to depend on the level of thyroid hormone and, by contrast, to be reciprocally dependent on the level of glucocorticoid.…”

Section: Discussionsupporting

confidence: 91%

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

Nakagawa

Kawashima

Hirose

et al. 1994

Biochemical Journal

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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.

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Section: Discussionsupporting

confidence: 91%

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

Nakagawa

Kawashima

Hirose

et al. 1994

Biochemical Journal

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“…These effects in turn contributed to FABP1 0 s impact on whole-body phenotype. Significantly, this work underscores the importance for considering FABP1 level in development of FABP1-targeted therapeutics, as hepatic FABP1 levels are pharmacologically inducible (Brandes and Arad 1983;Hashimoto et al 1999;Madsen et al 1999;Richert et al 2003;Rajaraman et al 2007;Rakhshandehroo et al 2009;Sanderson et al 2010;Martin et al 2013;Huang et al 2014), increased or decreased depending on expression of highly prevalent SNP (single nucleotide polymorphism)variant genotypes Peng et al 2015), and up-regulated in human liver pathologies such as obesity (Morrow et al 1979), non-alcoholic fatty liver disease (Yang et al 1987;Baumgardner et al 2007;Charlton et al 2009;Higuchi et al 2011), and alcoholic fatty liver disease (Pignon et al 1987;Gyamfi et al 2008).…”

Section: Mcintoshmentioning

confidence: 88%

Fabp1 gene ablation inhibits high‐fat diet‐induced increase in brain endocannabinoids

Martin

Landrock

Chung

et al. 2016

Journal of Neurochemistry

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The endocannabinoid system shifts energy balance toward storage and fat accumulation, especially in the context of diet-induced obesity. Relatively little is known about factors outside the central nervous system that may mediate the effect of high fat diet (HFD) on brain endocannabinoid levels. One candidate is the liver fatty acid binding protein (FABP1), a cytosolic protein highly prevalent in liver, but not detected in brain, which facilitates hepatic clearance of fatty acids. The impact of Fabp1 gene ablation (LKO) on the effect of high-fat diet (HFD) on brain and plasma endocannabinoid levels was examined and data expressed for each parameter as the ratio of high fat diet/control diet. In male wild-type mice, HFD markedly increased brain N-acylethanolamides, but not 2-monoacylglycerols. LKO blocked these effects of HFD in male mice. In female wild-type mice, HFD slightly decreased or did not alter these endocannabinoids as compared with male wild-type. LKO did not block the HFD effects in female mice. The HFD-induced increase in brain arachidonic acid -derived arachidonoylethanolamide in males correlated with increased brain free and total arachidonic acid. The ability of LKO to block the HFD-induced increase in brain arachidonoylethanolamide correlated with reduced ability of HFD to increase brain free and total arachidonic acid in males. In females, brain free and total arachidonic acid levels were much less affected by either HFD or LKO in the context of HFD. These data showed that LKO markedly diminished the impact of HFD on brain endocannabinoid levels, especially in male mice.

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“…The higher level of FABP1 in female rats, as well as the increased FABP1 content in male animals treated by clofi brate, is not related to differences in the turnover rate of FABP1, but appears to be correlated with an increased content of tissue FABP1 mRNA ( 33 ). Starvation and high-fat content diets also have clear and reciprocal effects on FABP1 levels (34)(35)(36). A high-carbohydrate diet increases FABP1 content in the liver and intestine ( 37 ).…”

mentioning

confidence: 99%

Recent insights into the biological functions of liver fatty acid binding protein 1

Wang

Bonkovsky

Lemos

et al. 2015

Journal of Lipid Research

188

175

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Liver cytosolic fatty acid-binding proteins

Cited by 26 publications

References 23 publications

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

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

Fabp1 gene ablation inhibits high‐fat diet‐induced increase in brain endocannabinoids

Recent insights into the biological functions of liver fatty acid binding protein 1

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