Stimulation of glutathione degradation by amino acids: lack of stereospecificity.
The rate of degradation of glutathione by rat kidney slices has been analysed. In the absence of exogenous amino acids a half-life of 84 min is found. In the presence of the L-isomer of three amino acids which are good substrates for gamma-glutamyl transpeptidase the rate of degradation is increased in a concentration-dependent manner. The stimulatory effect is not stereospecific, the D-isomers having a similar effect to their L-enantiomers. These findings indicate that perturbations in glutathione metabolism need not be due to the stimulation of active transport mediated by gamma-glutamyl transpeptidase.
D000409:Alanine / Q000378:metabolism; D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D005973:Glutamine / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism*; D066298:In Vitro Techniques; D007668:Kidney / Q000187:drug effects / Q000378:metabolism*; D007700:Kinetics; D008715:Methionine / Q000378:metabolism; D010101:Oxygen Consumption; D051381:Rats; D011919:Rats, Inbred Strains; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D000596:Amino Acids; D005973:Glutamine; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D008715:Methionine; D005978:Glutathione; D000409:Alanine