Putative role of antioxidant enzymes and glyoxalases in carcinogenesis.
The effects various drugs exert on antioxidant enzyme and glyoxalase activity in rat livers were studied. All drugs tested provoked a marked reduction in glutathione peroxidase and a small drop in both glyoxalase I and II activity. It is hypothesized that the substances tested support tumour development by neutralizing organic peroxides, thereby favouring the oxidation of carcinogens and, as a consequence, the formation of metabolites that trigger neoplastic transformation. The reduction in glyoxalase activity is probably attributable to the enhanced cell proliferation induced by the treatment.
Liotti
F S
FS
Institute of General Pathology, University of Perugia, Italy.
Menghini
A R
AR
Guerrieri
P
P
Mariucci
G
G
Armellini
R
R
D000818:Animals; D003634:DDT / Q000494:pharmacology; D003864:Depression, Chemical; D004958:Estradiol / Q000494:pharmacology; D005260:Female; D007791:Lactoylglutathione Lyase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D009374:Neoplasms, Experimental / Q000139:chemically induced* / Q000201:enzymology; D010088:Oxidoreductases / Q000037:antagonists & inhibitors; D010634:Phenobarbital / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D013869:Thiolester Hydrolases / Q000378:metabolism*; D000099301:Hydroxyacylglutathione Hydrolase
D003634:DDT; D004958:Estradiol; D007791:Lactoylglutathione Lyase; D010088:Oxidoreductases; D010634:Phenobarbital; D013755:Tetradecanoylphorbol Acetate; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase