Abstract
Metabolism of extracellular GSH, GSSG, the mixed disulfide of cysteine and GSH (CYSSG) and cystinyl-bis-glycine (CYS-GLY) 2 to cysteine and cystine by freshly isolated kidney cells has been examined with and without the presence of a potent γ-glutamyl transpeptidase inhibitor, L-(αS, 5S)-α-amino-3-chloro-4, 5-dihydro-5-isoxazoleacetic acid (AT-125). Irreversible inactivation of γ-glutamyl transpeptidase occurred rapidly which prevented both the conversion of GSH to GSSG and removal of γ-glutamyl moieties from GSH, GSSG and CYSSG by kidney cells. The rapid conversion of cystinyl-bis-glycine to cystine was not affected by AT-125 indicating that this agent had no effect upon cysteinylglycine dipeptidase activity. GSH and GSSG degradation intermediates were sufficiently different to suggest that important thiol disulfide interchange reactions may occur during GSH but not GSSG degradation by kidney cells.
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