Glutathione-S-transferase, alcohol dehydrogenase and aldehyde reductase activities during diethylnitrosamine-carcinogenesis in rat liver.
Several enzymes metabolize the toxic aldehydes produced during lipid peroxidation, such as 4-hydroxynonenal. During carcinogenesis induced by diethylnitrosamine in rat liver, an increase in aldehyde dehydrogenase, in comparison with normal liver, has already been shown. This paper demonstrates that, although to a lesser extent than aldehyde dehydrogenase, aldehyde reductase and glutathione-S-transferase also increase during carcinogenesis. Of the latter two enzymes, aldehyde reductase increases more markedly in a progressive fashion during the months of development of nodules and hepatoma. The increase of enzymes able to metabolize 4-hydroxynonenal, as well as other aldehydes, is certainly important in protecting tumour cells against cytotoxic effect of aldehydes.
Canuto
R A
RA
Department of Experimental Oncology and Medicine, University of Turin, Italy.
Muzio
G
G
Maggiora
M
M
Biocca
M E
ME
Dianzani
M U
MU
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000378:metabolism*; D000818:Animals; D005982:Glutathione Transferase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008114:Liver Neoplasms, Experimental / Q000139:chemically induced / Q000201:enzymology*; D008297:Male; D051381:Rats; D011916:Rats, Inbred F344
D000426:Alcohol Dehydrogenase; D000449:Aldehyde Reductase; D005982:Glutathione Transferase