Factors influencing in vitro methylation of arsenicals in rat liver cytosol

Arsenic ◽  
1997 ◽  
pp. 283-295 ◽  
Author(s):  
M. Styblo ◽  
D. J. Thomas
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Factors Influencing ◽  
Rat Liver Cytosol

scholarly journals Rat liver tyrosine aminotransferase activity and induction by dexamethasone upon cadmium intoxication

2003 ◽  
Vol 55 (1-2) ◽  
pp. 3-7 ◽  
Author(s):  
Jadranka Dundjerski ◽  
Jelena Predic ◽  
Aleksandra Cvoro ◽  
Gordana Matic
Keyword(s):  
Enzyme Activity ◽  
Gene Transcription ◽  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Aminotransferase Activity ◽  
Liver Cytosol ◽  
Cadmium Intoxication ◽  
Rat Liver Cytosol

This study was focused on Cd effects on basal and dexamethasone-induced tyrosine aminotransferase (TAT) activity in the rat liver cytosol. Cadmium (Cd), applied in the dose of 2 mg/kg b.w., stimulated both TAT activity and its induction by dexamethasone, inducing the most prominent alterations 24 h after administration. Doses lower than 2 mg Cd/kg b.w. were ineffective while the higher ones (3 and 4 mg Cd/kg b.w) led to the changes similar to those reached by 2 mg Cd/kg. The in vitro application of different Cd concentrations to the liver cytosol rendered the enzyme activity unchanged suggesting that the metal acted at the level of TAT gene transcription.

In vitro Formation of Glucose 6-Phosphate from 3-Phosphoglycerate by Rat Liver Cytosol

1981 ◽  
Vol 362 (1) ◽  
pp. 47-58 ◽  
Author(s):  
Stéphanie MÖRIKOFER-ZWEZ ◽  
Franziska B. STOECKLIN ◽  
Paul WALTER
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Thioredoxin and glutaredoxin systems of rat liver cytosol are not influenced by thyroid dysfunction

1989 ◽  
Vol 67 (7) ◽  
pp. 384-387
Author(s):  
Ganesh B. Bhat ◽  
Brian C. W. Hummel ◽  
Paul G. Walfish
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Thyroid Dysfunction ◽  
Thyroid Status ◽  
Liver Cytosol ◽  
Reverse Triiodothyronine ◽  
Hormone Status ◽  
Rat Liver Cytosol

The relation of thyroid hormone status to the function of hepatic cytosolic components activating microsomal reverse triiodothyronine (rT3) 5′-monodeiodination was studied in rats. Hyperthyroidism was induced by administration of thyroxine and hypothyroidism, by thyroidectomy. The DTT-stimulated microsomal rT3 5′-monodeiodination rate was increased by 125% in hyperthyroid rats and reduced to about 30% in hypothyroid rats (when compared with euthyroid animals). Thyroid status was unrelated to NADPH-dependent activation of microsomal 5′-deiodinase by cytosol components or to cytosolic concentrations of thioredoxin and glutaredoxin, which stimulate in vitro microsomal deiodination of thyroid hormone.Key words: hyperthyroidism, hypothyroidism, glutaredoxin, thioredoxin, 5′-deiodinase.

Mono- and dimethylation of arsenic in rat liver cytosol in vitro

1996 ◽  
Vol 99 (1-3) ◽  
pp. 147-164 ◽  
Author(s):  
Miroslav Styblo ◽  
Marielle Delnomdedieu ◽  
David J. Thomas
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
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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