scholarly journals Publisher Correction: Whole Transcriptome Analysis of Renal Intercalated Cells Predicts Lipopolysaccharide Mediated Inhibition of Retinoid X Receptor alpha Function

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Vijay Saxena ◽  
James Fitch ◽  
John Ketz ◽  
Peter White ◽  
Amy Wetzel ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Retinoid X Receptor ◽  
Intercalated Cells ◽  
Receptor Alpha ◽  
Whole Transcriptome Analysis ◽  
Retinoid X Receptor Alpha ◽  
Whole Transcriptome ◽  
Alpha Function

scholarly journals Whole‐Transcriptome Analysis ofPlasmodium falciparumField Isolates: Identification of New Pathogenicity Factors

2007 ◽  
Vol 196 (11) ◽  
pp. 1603-1612 ◽  
Author(s):  
Anthony Siau ◽  
Fousseyni S. Touré ◽  
Odile Ouwe‐Missi‐Oukem‐Boyer ◽  
Liliane Cicéron ◽  
Nassira Mahmoudi ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Pathogenicity Factors ◽  
Whole Transcriptome Analysis ◽  
Whole Transcriptome

scholarly journals Glucocorticoids increase retinoid-X receptor alpha (RXRalpha) expression and enhance thyroid hormone action in primary cultured rat hepatocytes

1999 ◽  
Vol 22 (1) ◽  
pp. 81-90 ◽  
Author(s):  
S Yamaguchi ◽  
Y Murata ◽  
T Nagaya ◽  
Y Hayashi ◽  
S Ohmori ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Binding Protein ◽  
Rat Hepatocytes ◽  
Retinoid X Receptor ◽  
Type I ◽  
Receptor Alpha ◽  
Primary Cultured Rat Hepatocytes ◽  
Spot 14 ◽  
Cultured Rat Hepatocytes ◽  
Retinoid X Receptor Alpha

We have previously demonstrated that dexamethasone (DEX) enhances the T3-dependent increase in type I 5'-deiodinase (5'DI) mRNA in primary cultured rat hepatocytes grown as spheroids. Here we report that DEX-enhanced T3-responsiveness also occurs in two other T3-regulated hepatic genes, Spot 14 and malic enzyme. This enhancement was inhibited by pretreatment with cycloheximide and the stability of 5'DI and Spot 14 mRNAs was not affected by DEX. We thus hypothesized that a factor(s) that augments T3-responsiveness is induced by DEX. Among the possible candidates examined, retinoid-X receptor alpha (RXRalpha), which is a main heterodimer partner with T3 receptor, appeared to be involved. Whereas DEX increased the amount of RXRalpha mRNA, it did not affect the expression of other possible factors such as steroid receptor coactivator-1 and the binding protein of cAMP response element-binding protein. Northern and Western blot analysis, and electrophoretic mobility shift assay revealed that DEX increased RXRalpha expression at both the mRNA and protein levels. Maximal increase in RXRalpha protein was achieved with the addition of physiological concentrations of DEX (10(-8) M). To test whether the DEX-induced increase in RXRalpha affects ligand-dependent transcriptional activation through other receptors that form heterodimer with RXR, we examined its effect on the retinoic acid (RA)/RA receptor (RAR) system. Indeed, DEX also enhanced the RA-dependent increase in RARbeta mRNA in a cycloheximide-sensitive manner. Increase in the level of RXRalpha in hepatocytes by infection with the RXRalpha-expressing adenovirus resulted in enhancement of the T3-dependent increase in 5'DI mRNA. These results strongly suggest that the DEX-induced augmentation of T3-responsiveness in cultured hepatocytes is mediated, in part, by the increased expression of RXRalpha.

scholarly journals Alterations of Immune and Keratinization Gene Expression in Papulopustular Rosacea by Whole Transcriptome Analysis

2020 ◽  
Vol 140 (5) ◽  
pp. 1100-1103.e4 ◽  
Author(s):  
Yi-Hsien Shih ◽  
Jin Xu ◽  
Anusha Kumar ◽  
Rui Li ◽  
Anne Lynn S. Chang
Keyword(s):  
Gene Expression ◽  
Transcriptome Analysis ◽  
Whole Transcriptome Analysis ◽  
Whole Transcriptome

scholarly journals Stability of the Retinoid X Receptor-alpha Homodimer in the Presence and Absence of Rexinoid and Coactivator Peptide

2020 ◽  
Author(s):  
Zhengrong Yang ◽  
Donald D. Muccio ◽  
Nathalia Melo ◽  
Venkatram R. Atigadda ◽  
Matthew B. Renfrow
Keyword(s):  
Binding Pocket ◽  
Retinoid X Receptor ◽  
Heat Capacity Change ◽  
Scanning Calorimetry ◽  
Receptor Alpha ◽  
Average Value ◽  
A Value ◽  
Capacity Change ◽  
Differential Scanning Fluorimetry ◽  
Retinoid X Receptor Alpha

ABSTRACTDifferential scanning calorimetry and differential scanning fluorimetry were used to measure the thermal stability of human retinoid X receptor-alpha ligand binding domain (RXRα LBD) homodimer in the absence or presence of rexinoid and coactivator peptide, GRIP-1. The apo-RXRα LBD homodimer displayed a single thermal unfolding transition with a Tm of 58.7 °C and an unfolding enthalpy (ΔH) of 673 kJ/mol (12.5 J/g), much lower than average value (35 J/g) of small globular proteins. Using a heat capacity change (ΔCp) of 15 kJ/(mol·K) determined by measurements at different pH values, the free energy of unfolding (ΔG) of the native state was 33 kJ/mol at 37 °C. Rexinoid binding to the apo-homodimer increased Tm by 5 to 9 °C, and increased the ΔG of the native homodimer by 12 to 20 kJ/mol at 37 °C, consistent with the nanomolar dissociation constant (Kd) of the rexinoids. The increase in ΔG was the result of a more favorable entropic change due to interactions between the rexinoid and hydrophobic residues in the binding pocket, with the larger increases caused by rexinoids containing larger hydrophobic end groups. GRIP-1 binding to holo-homodimers containing rexinoid resulted in additional increases in ΔG of 14 kJ/mol, a value same for all three rexinoids. Binding of rexinoid and GRIP-1 resulted in a combined 50% increase in unfolding enthalpy, consistent with reduced structural fluidity and more compact folding observed in other published structural studies. Thermodynamic analysis thus provided a quantitative evaluation of the interactions between RXR and its agonist and coactivator.

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