The regulation of N-acetylglutamate synthetase in rat liver by protein intake.
Urea cycle enzymes are subjected to regulation by dietary proteins. We have shown that this is also the case for N-acetylglutamate synthetase (EC 2.3.1.1.) (NAGS). Four different groups (n = 7) of male Wistar rats received either a low protein (8.7%) or a high (32% and 51%) protein diet and a control diet of 17% protein. The NAGS-activity in the liver, assayed after 15 days of feeding the different diets, increased from 25 +/- 7 (controls, 17% protein) to 31 +/- 5 (32% protein) and to 52 +/- 17 (51% protein) nmoles.min-1.g-1 wet weight. It decreased in the group with low protein diet (8.7%) to 5 +/- 3. The ratio of the arginine stimulated to the unstimulated enzyme activity remained constant over the range of protein intake. Similar changes were observed for carbamylphosphate synthetase, ornithine carbamyltransferase and arginase. As it is known for these enzymes adaptive mechanisms in relation to variations in dietary protein consumption also could be demonstrated for the enzyme NAGS.
Colombo
J P
JP
Department of Clinical Chemistry, Inselspital, University of Berne, Switzerland.
Pfister
U
U
Cervantes
H
H
D000123:Acetyltransferases / Q000378:metabolism*; D051046:Amino-Acid N-Acetyltransferase; D000818:Animals; D001119:Arginase / Q000378:metabolism; D001120:Arginine / Q000494:pharmacology; D019733:Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; D004044:Dietary Proteins / Q000494:pharmacology*; D008025:Ligases / Q000378:metabolism; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D009954:Ornithine Carbamoyltransferase / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D004044:Dietary Proteins; D001120:Arginine; D009954:Ornithine Carbamoyltransferase; D000123:Acetyltransferases; D051046:Amino-Acid N-Acetyltransferase; D001119:Arginase; D008025:Ligases; D019733:Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; C064716:carbamoyl phosphate synthetase (arginine-specific)