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1 Division of Nutritional Sciences, Cornell University, Ithaca, New York 14853-6301; and 2 Division of Maternal and Child Health Science, National Institute of Health and Nutrition, Shinjuku-ku, Tokyo 162, Japan
Little is known about mechanisms of regulation
of cysteine dioxygenase (CDO), 
-glutamylcysteine synthetase (GCS),
and cysteine-sulfinate decarboxylase (CSDC) in response to diet. Enzyme
activity and Western and Northern or dot blot analyses were conducted
on liver samples from rats fed a basal low-protein diet or diets with
graded levels of protein or methionine for 2 wk. Higher levels of CDO activity and CDO protein but not of CDO mRNA were observed in liver of
rats fed methionine or protein-supplemented diets, indicating that CDO
activity is regulated by changes in enzyme concentration. Lower
concentrations of the heavy or catalytic subunit of GCS (GCS-HS) mRNA
and protein, as well as a lower activity state of GCS-HS in rats fed
methionine- or protein-supplemented diets, indicated that dietary
regulation of GCS occurs by both pretranslational and posttranslational
mechanisms. Lower CSDC activity, CSDC protein concentration, and CSDC
mRNA concentration were found in rats fed the highest level of protein,
and regulation appeared to involve changes in mRNA concentration.
Regulation of key enzymes of cysteine metabolism in response to diet
determines the use of cysteine for synthesis of its essential metabolites.
cysteine dioxygenase; cysteine-sulfinate decarboxylase; -glutamylcysteine synthetase; rats
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