scholarly journals Divergent evolution of cis-acting peroxisome proliferator-activated receptor elements that differentially control the tandemly duplicated fatty acid-binding protein genes, fabp1b.1 and fabp1b.2, in zebrafish

Genome ◽  
2016 ◽  
Vol 59 (6) ◽  
pp. 403-412 ◽  
Author(s):  
Robert B. Laprairie ◽  
Eileen M. Denovan-Wright ◽  
Jonathan M. Wright
Keyword(s):  
Fatty Acid ◽  
Promoter Activity ◽  
Fatty Acid Binding Protein ◽  
Differential Regulation ◽  
Peroxisome Proliferator ◽  
Duplicated Genes ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Selective Agonist ◽  
Ppar Agonists

Gene duplication is thought to facilitate increasing complexity in the evolution of life. The fate of most duplicated genes is nonfunctionalization: functional decay resulting from the accumulation of mutations. According to the duplication–degeneration–complementation (DDC) model, duplicated genes are retained by subfunctionalization, where the functions of the ancestral gene are sub-divided between duplicate genes, or by neofunctionalization, where one of the duplicates acquires a new function. Here, we report the differential regulation of the zebrafish tandemly duplicated fatty acid-binding protein genes, fabp1b.1 and fabp1b.2, by peroxisome proliferator-activated receptors (PPAR). fabp1b.1 mRNA levels were induced in tissue explants of liver, but not intestine, by PPAR agonists. fabp1b.1 promoter activity was induced to a greater extent by rosiglitazone (PPARγ-selective agonist) compared to WY 14,643 (PPARα-selective agonist) in HEK293A cells. Mutation of a peroxisome proliferator response element (PPRE) at –1232 bp in the fabp1b.1 promoter reduced PPAR-dependent activation. fabp1b.2 promoter activity was not affected by PPAR agonists. Differential regulation of the duplicated fabp1b promoters may be the result of PPRE loss in fabp1b.2 during a meiotic crossing-over event. Retention of PPAR inducibility in fabp1b.1 and not fabp1b.2 suggests unique regulation and function of the fabp1b duplicates.

scholarly journals The anti-inflammatory agent bindarit acts as a modulator of fatty acid-binding protein 4 in human monocytic cells

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Sergio Oddi ◽  
Lucia Scipioni ◽  
Antonio Totaro ◽  
Clotilde Angelucci ◽  
Beatrice Dufrusine ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Molecular Mechanisms ◽  
Binding Protein ◽  
Immunomodulatory Activity ◽  
Peroxisome Proliferator ◽  
Monocytic Cells ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Anti Inflammatory

Abstract We investigated the cellular and molecular mechanisms by which bindarit, a small indazolic derivative with prominent anti-inflammatory effects, exerts its immunoregulatory activity in lipopolysaccharide (LPS) stimulated human monocytic cells. We found that bindarit differentially regulates the release of interleukin-8 (IL-8) and monocyte chemoattractant protein-1 (MCP-1), enhancing the release of IL-8 and reducing that of MCP-1. These effects specifically required a functional interaction between bindarit and fatty acid binding protein 4 (FABP4), a lipid chaperone that couples intracellular lipid mediators to their biological targets and signaling pathways. We further demonstrated that bindarit can directly interact with FABP4 by increasing its expression and nuclear localization, thus impacting on peroxisome proliferator-activated receptor γ (PPARγ) and LPS-dependent kinase signaling. Taken together, these findings suggest a potential key-role of FABP4 in the immunomodulatory activity of bindarit, and extend the spectrum of its possible therapeutic applications to FABP4 modulation.

scholarly journals Studies on fatty acid-binding proteins. The diurnal variation shown by rat liver fatty acid-binding protein

1987 ◽  
Vol 242 (3) ◽  
pp. 913-917 ◽  
Author(s):  
T C I Wilkinson ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Small Variation ◽  
Fatty Acid Binding Proteins ◽  
Peroxisome Proliferator ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

The concentration of fatty acid-binding protein in rat liver was examined by SDS/polyacrylamide-gel electrophoresis, by Western blotting and by quantifying the fluorescence enhancement achieved on the binding of the fluorescent probe 11-(dansylamino)undecanoic acid. A 2-3-fold increase in the concentration of this protein produced by treatment of rats with the peroxisome proliferator tiadenol was readily detected; however, only a small variation in the concentration of the protein due to a diurnal rhythm was observed. This result contradicts the 7-10-fold variation previously reported for this protein [Hargis, Olson, Clarke & Dempsey (1986) J. Biol. Chem. 261, 1988-1991].

IL-6 cooperates with peroxisome proliferator-activated receptor-α-ligands to induce liver fatty acid binding protein (LFABP) up-regulation

2013 ◽  
Vol 33 (7) ◽  
pp. 1019-1028 ◽  
Author(s):  
Margarita Vida ◽  
Antonia Serrano ◽  
Miguel Romero-Cuevas ◽  
Francisco J. Pavón ◽  
Águeda González-Rodriguez ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Peroxisome Proliferator ◽  
Liver Fatty Acid ◽  
Peroxisome Proliferator Activated Receptor ◽  
Fatty Acid Binding ◽  
Acid Binding Protein
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