scholarly journals Alanine-scanning Mutagenesis of a C-terminal Ligand Binding Domain of the Insulin Receptor α Subunit

1996 ◽  
Vol 271 (5) ◽  
pp. 2439-2442 ◽  
Author(s):  
Dennis C. Mynarcik ◽  
Gui Qin Yu ◽  
Jonathan Whittaker
1995 ◽  
Vol 270 (7) ◽  
pp. 3012-3016 ◽  
Author(s):  
Paul F. Williams ◽  
Dennis C. Mynarcik ◽  
Gui Qin Yu ◽  
Jonathan Whittaker

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Brigitta Margit Kállai ◽  
Judit Csöndes ◽  
Gergely Kiss ◽  
Lilla Bodrogi ◽  
Zsolt Rónai ◽  
...  

AbstractGlucocorticoids play a central role in the inflammatory response and alleviate the symptoms in critically ill patients. The glucocorticoid action relies on the glucocorticoid receptor (GR) which translocates into the nucleus upon ligand-binding and regulates transcription of a battery of genes. Although the GR is encoded by a single gene, dozens of its splice variants have been described in diverse species. The GRα isoform encodes the full, functionally active protein that is composed of a transactivation, a DNA-binding, and a C-terminal ligand-binding domain. The second most highly expressed receptor variant, the GR-P, is formed by an intron retention that introduces an early stop codon and results in a probably dysfunctional protein with truncated ligand-binding domain. We described the canine ortholog of GR-P and showed that this splice variant is highly abundant in the peripheral blood of dogs. The level of cGRα and cGR-P transcripts are elevated in patients of SIRS and the survival rate is increased with elevated cGRα and cGR-P expression. The ratio of cGRα and cGR-P mRNA did not differ between the survivor and non-survivor patients; thus, the total GR expression is more pertinent than the relative expression of GR isoforms in assessment of the disease outcome.


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