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PubMed1997

Glutathione and glutathione delivery compounds.

Deficiency of GSH (BSO model) demonstrates the need for cellular protection from endogenous ROS. The pathology of various diseases is often associated with ROS and oxidative stress. The several methods for modulating cellular GSH levels presented in this chapter offer selective tools to study mechanisms and offer potential therapy of human diseases associated with GSH deficiency and oxidative stress.

Animals↗
PubMed2002

The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation.

Arsenic trioxide is an effective treatment for acute promyelocytic leukemia, but resistance to metalloid salts is found in humans. Using atomic absorption spectroscopy, we have measured the rate of uptake of arsenic trioxide and of antimony tartrate in GLC4 and GLC4/ADR cells overexpressing MRP1 and the rate of their MRP1-mediated effluxes as a function of the intracellular GSH concentration. In sensitive cells, after 1 h, a pseudosteady state is reached where intra- and extracellular concentrations of metalloid are the same. This precludes the formation, at short term, of complexes between arsenic or antimony with GSH. In resistant cells reduced intracellular accumulation of arsenic (or antimony), reflecting an increased rate of arsenic (or antimony) efflux from the cells, is observed. No efflux of the metalloid is observed in GSH depleted cells. The two metalloids and GSH are pumped out by MRP1 with the same efficiency. Moreover for the three compounds 50% of the efflux is inhibited by 2 microM MK571. This led us to suggest that As- and Sb-containing species could be cotransported with GSH.

Antimony↗
PubMed1988

The conjugation of 4-nitroquinoline 1-oxide, a potent carcinogen, by mammalian glutathione transferases. 4-Nitroquinoline 1-oxide conjugation by human, rat and mouse liver cytosols, extrahepatic organs of mice and purified mouse glutathione transferase isoenzymes.

The conjugation of 4-nitroquinoline 1-oxide with GSH by human, rat and mouse liver cytosols, by purified mouse GSH transferases and by extrahepatic organ cytosols of male and female mice was investigated. 4-Nitroquinoline 1-oxide was as effectively conjugated by human liver cytosol as was 1-chloro-2,4-dinitrobenzene, at a substrate concentration of 0.1 mM. Mouse isoenzymes composed of Yb1 and Yf subunits exhibited high activity towards 4-nitroquinoline 1-oxide. Human, rat and mouse hepatic activities towards this substrate correlated with the hepatic isoenzyme compositions.

4-Nitroquinoline-1-oxide↗
PubMed1989

Mouse hepatic glutathione transferase isoenzymes and their differential induction by anticarcinogens. Specificities of butylated hydroxyanisole and bisethylxanthogen as inducers of glutathione transferases in male and female CD-1 mice.

GSH transferase isoenzymes of class Mu (two forms), class Pi (one form) and class Alpha (two forms) were purified from liver cytosols of female CD-1 mice pretreated with an anticarcinogenic inducer, 2(3)-t-butyl-4-hydroxyanisole. GSH transferases GT-8.7, GT-8.8a and GT-8.8b, GT-9.0, GT-9.3, GT-10.3 and GT-10.6 contained a minimum of six types of subunits distinguishable by structural, catalytic and immunological characteristics. H.p.l.c. analysis of the subunit compositions of affinity-purified GSH transferases from liver cytosols of induced and non-induced male and female CD-1 mice showed that two anticarcinogenic compounds, 2(3)-t-butyl-4-hydroxyanisole and bisethylxanthogen, differed markedly in their specificities as inducers of GSH transferase.

Animals↗