A Proteomic Analysis of Bromobenzene Reactive Metabolite Targets in Rat Liver Cytosol in Vivo

2007 ◽  
Vol 20 (3) ◽  
pp. 511-519 ◽  
Author(s):  
Yakov M. Koen ◽  
Natalia V. Gogichaeva ◽  
Michail A. Alterman ◽  
Robert P. Hanzlik
Keyword(s):  
Rat Liver ◽  
Proteomic Analysis ◽  
Reactive Metabolite ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol

1975 ◽  
Vol 149 (3) ◽  
pp. 785-788 ◽  
Author(s):  
B Mannervik ◽  
K Axelsson
Keyword(s):  
Glutathione Reductase ◽  
Rat Liver ◽  
Direct Reduction ◽  
Liver Cytosol ◽  
Disulphide Bonds ◽  
Enzymic Reaction ◽  
Spontaneous Reaction ◽  
Rat Liver Cytosol

The reduction of mixed disulphides of some proteins and GSH [Protein(-SSG)n] is accomplished with GSH as a reductant and a thioltransferase from rat liver as a catalyst, thus: See article. The spontaneous reaction is negligible in comparison with the enzymic reaction in vivo, and any direct reduction with glutathione reductase is not detectable with the substrates used. The reduction is only indirectly dependent on NADPH, which is required for the regeneration of GSH from GSSG. Other protein disulphides apparently are reduced via analogous GSH-dependent reactions

In Vivo Effects of Molybdate on Activation of Rat Liver Cytosol Glucocorticoid Receptor

1988 ◽  
Vol 20 (09) ◽  
pp. 566-569
Author(s):  
A. Yoshida ◽  
S. Taniguchi ◽  
Y. Mitani ◽  
Y. Ueda ◽  
K. Urabe ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Liver Cytosol ◽  
In Vivo Effects ◽  
Rat Liver Cytosol

scholarly journals Heterogeneity and properties of hepatic dexamethasone-binding proteins

1979 ◽  
Vol 180 (1) ◽  
pp. 187-193 ◽  
Author(s):  
S L H Liu ◽  
T E Webb
Keyword(s):  
Rat Liver ◽  
Binding Proteins ◽  
Binding Protein ◽  
Novikoff Hepatoma ◽  
Liver Cytosol ◽  
Activated Complex ◽  
Simple Dissociation ◽  
Rat Liver Cytosol

Evidence from experiments in vivo and in vitro is presented for the presence of three species of dexamethasone-binding proteins in rat liver, which are identified by chromatography on Sepharose 6B or by isoelectric focusing. Although two of these species (DI and DII) possess properties characteristic of a true receptor, the third binding protein (i.e. DIII), which migrates most slowly on Sepharose 6B, but has stability properties similar to protein DII, exhibits a 3-fold lower affinity for dexamethasone and the activated complex neither binds to DNA-cellulose nor translocates to the nucleus. Only the predominant liver receptor (DI), which is eluted first from Sepharose 6B, is present in Novikoff-hepatoma cytosol, suggesting that the major and minor species are not interconverted through simple dissociation during their isolation. The binding activities of all three species in the liver cytosol increase approx. 2-fold in vivo after adrenalectomy and show a transient 2-fold fall in vivo after the administration of cortisol. These changes in vivo in protein DIII shows a marked lag compared with those in proteins DI and DII, which change in parallel. It is therefore proposed that rat liver cytosol contains two dexamethasone receptors and a dexamethasone-binding protein that may be derived from these receptors.

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