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July 14, 2011 Heterozygous Deletion of S-Nitrosoglutathione Reductase in Mice Does Not Increase Nitrosative Inactivation of O6-Alkylguanine-DNA Alkyltransferase or Diethylnitrosamine-induced Hepatocarcinogenesis
Dorothy Colagiovanni, Wei Wei, Joan Blonder, Limin Liu, and Gary J. Rosenthal
S-nitrosoglutathione reductase (GSNOR) is the primary enzyme responsible for the metabolism of S-nitrosoglutathione (GSNO).
Through this denitrosylation process, GSNOR plays a central role in regulating the levels of endogenous S-nitrosothiols and protein S-nitrosylation-based signalling. Recent evidence suggests that modulation of proteins via S-nitrosylation may alter DNA repair mechanisms.
For example, the DNA repair enzyme O6-alkylguanine-DNA alkyltransferase (AGT) can be inactivated through S-nitrosylation of the Cys in the active site of AGT. AGT corrects O6-alkylguanines and thus prevents the mispairing of cytotoxic O6-alkylguanines to thymine by DNA polymerases during DNA replication.
Mice deficient in AGT have been shown to be more susceptible to hepatocarcinogenesis induced by dimethylnitrosamine. More…poster PDF(184Kb)
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