scholarly journals Tissue distribution and subunit structures of the multiple forms of glutathione S-transferase in the rat

1981 ◽  
Vol 193 (1) ◽  
pp. 367-370 ◽  
Author(s):  
N C Scully ◽  
T J Mantle
Keyword(s):  
Tissue Distribution ◽  
Rat Kidney ◽  
Multiple Forms ◽  
Glutathione S Transferase

A study of the subunit structures of the multiple forms of glutathione S-transferase in rat kidney, testis, lung and spleen is shown to be consistent with a proteolytic model for the generation of the multiple forms.

scholarly journals Multiple Forms of Human Glutathione S-Transferase and Their Affinity for Bilirubin

1975 ◽  
Vol 60 (1) ◽  
pp. 153-161 ◽  
Author(s):  
Kazuaki KAMISAKA ◽  
William H. HABIG ◽  
Jeanne N. KETLEY ◽  
Irwin M. ARIAS ◽  
William B. JAKOBY
Keyword(s):  
Multiple Forms ◽  
Glutathione S Transferase

Molecular cloning and tissue distribution of a 26-kilodalton Schistosoma mansoni glutathione S-transferase

1990 ◽  
Vol 41 (1) ◽  
pp. 35-44 ◽  
Author(s):  
François Trottein ◽  
Marie Paule Kieny ◽  
Claudie Verwaerde ◽  
Gérard Torpier ◽  
Raymond J. Pierce ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Tissue Distribution ◽  
Molecular Cloning ◽  
Glutathione S Transferase

scholarly journals Multiple forms of rat kidney mutarotase.

1976 ◽  
Vol 24 (11) ◽  
pp. 2893-2895 ◽  
Author(s):  
JUN OKUDA ◽  
ICHITOMO MIWA ◽  
YUKIYASU TOYODA
Keyword(s):  
Rat Kidney ◽  
Multiple Forms

scholarly journals Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum

1988 ◽  
Vol 252 (1) ◽  
pp. 127-136 ◽  
Author(s):  
G M Trakshel ◽  
M D Maines
Keyword(s):  
Specific Activity ◽  
Rat Kidney ◽  
Male Rats ◽  
Glutathione S Transferase ◽  
Aberrant Form ◽  
Glutathione S Transferases ◽  
Exchange Matrix ◽  
Rat Kidney Cytosol

We have developed chromatographic and mathematical protocols that allowed the high resolution of glutathione S-transferase (GST) subunits, and the identification of a previously unresolved GST monomer in rat kidney cytosol; the monomer was identified tentatively as subunit 6. Also, an aberrant form of GST 7-7 dimer appeared to be present in the kidney. This development was utilized to illustrate the response of rat kidney GST following cis-platinum treatment in vivo. Rat kidney cytosol was separated into three ‘affinity families’ of GST activity after elution from a GSH-agarose matrix. The affinity peaks were characterized by quantitative differences in their subunit and dimeric compositions as determined by subsequent chromatography on a cation-exchange matrix and specific activity towards substrates. By use of these criteria, the major GST dimers of affinity peaks were tentatively identified. The major GST dimers in peak I were GST 1-1 and 1-2, in affinity peak II it was GST 2-2, and in peak III they were GST 3-3 and 7-7. GST 3-6 and/or 4-6, which have not been previously resolved in kidney cytosol, were also present in peak II. Alterations in the kidney cytosolic GST composition of male rats were detected subsequent to the administration of cis-platinum (7.0 mg/kg subcutaneously, 6 days). This treatment caused a pronounced alteration in the GST profile, and the pattern of alteration was markedly different from that reported for other chemicals in the kidney or in the liver. In general, the cellular contents of the GSTs of the Alpha and the Mu classes decreased and increased respectively. It is postulated that the decrease in the Alpha class of GSTs by cis-platinum treatment may be related to renal cortical damage and the loss of GSTs in the urine. The increase in the Mu class of GSTs could potentially stem from a lowered serum concentration of testosterone; the latter is a known effect of cis-platinum treatment.

Expression and tissue distribution of plaice glutathione S-transferase A

1992 ◽  
Vol 34 (1-4) ◽  
pp. 237-241 ◽  
Author(s):  
Michael J. Leaver ◽  
Karen Scott ◽  
Stephen G. George
Keyword(s):  
Tissue Distribution ◽  
Glutathione S Transferase

Regulation of Rho protein binding to membranes by rhoGDI: inhibition of releasing activity by physiological ionic conditions

1999 ◽  
Vol 77 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Diane Bilodeau ◽  
Sylvie Lamy ◽  
Richard R Desrosiers ◽  
Denis Gingras ◽  
Richard Béliveau
Keyword(s):  
Ionic Strength ◽  
Brush Border ◽  
Rat Kidney ◽  
Regulatory Protein ◽  
Rho Proteins ◽  
Glutathione S Transferase ◽  
Free System ◽  
Brush Border Membranes ◽  
A Cell ◽  
Membrane Bound

The Rho GDP dissociation inhibitor (GDI) is an ubiquitously expressed regulatory protein involved in the cycling of Rho proteins between membrane-bound and soluble forms. Here, we characterized the Rho solubilization activity of a glutathione S-transferase (GST) - GDI fusion protein in a cell-free system derived from rat kidney. Addition of GST-GDI to kidney brush border membranes resulted in the specific release of Cdc42 and RhoA from the membranes, while RhoB and Ras were not extracted. The release of Cdc42 and RhoA by GST-GDI was dose dependent and saturable with about 50% of both RhoA and Cdc42 extracted. The unextracted Rho proteins were tightly bound to membranes and could not be solubilized by repeated GST-GDI treatment. These results demonstrated that kidney brush border membranes contained two populations of RhoA and Cdc42. Furthermore, the GST-GDI solubilizing activity on membrane-bound Cdc42 and RhoA was abolished at physiological conditions of salt and temperature in all tissues examined. When using bead-immobilized GST-GDI, KCl did not reduced the binding of Rho proteins. However, washing brush border membranes with KCl prior treatment by GST-GDI inhibited the extraction of Rho proteins. Taken together, these results suggest that the binding of GDI to membrane-bound Cdc42 and RhoA occurs easily under physiological ionic strength conditions, but a complementary factor is required to extract these proteins from membranes. These observations suggest that the shuttling activity of GDI upon Rho proteins could be normally downregulated under physiological conditions.Key words: rhoGDI, rho proteins, ionic strength, kidney.

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