[Influence of alimentary zinc deficiency on nitrogen elimination and enzyme activities of the urea cycle].
Influence of alimentary zinc deficiency on nitrogen elimination and activities of urea cycle enzymes This study was conducted to investigate whether the hyperammonaemia shown in earlier zinc-deficiency experiments was the result of disturbed enzyme activities of the urea cycle. For this study 36 male Sprague-Dawley rats with an average body weight of 85 g were divided into three experimental groups of 12 animals each. Group 1 received the semisynthetic zinc-deficient diet (AIN-93G; 1.2 mg Zn/kg DM) ad libitum over 33 experimental days. Group 2 received the zinc-sulphate-supplemented control diet (60 mg Zn/kg DM) ad libitum and group 3 received the same diet matched to the feed intake of the zinc-deficient rats. Alimentary zinc deficiency reduced the zinc concentration and the activity of the alkaline phosphatase in serum by 75 and 67%, respectively. The activity of the glutamate dehydrogenase and the concentrations of ammonia and urea in the serum of the zinc-deficient rats showed no significant differences compared with pair-fed control rats. On the other hand the hepatic activity of the mitochondrial localized glutamate dehydrogenase of the zinc-deficient rats was significantly increased and the carbamoylphosphate synthetase and ornithine carbamoyltransferase were reduced about half in comparison with both control groups. The activities of the cytosolic liver enzymes such as argininosuccinate synthetase, argininosuccinase and arginase were again significantly increased in zinc-deficient rats compared with both control groups. The increased hepatic activity of the glutamate dehydrogenase possibly led to an enhanced NH(3) elimination in addition to urea synthesis. The typical reduction of feed intake in consequence of zinc deficiency is therefore not the cause of hyperammonaemia due to disturbed urea synthesis, as has been hypothesized in earlier studies.
Roth
V H
VH
Institut für Ernährungswissenschaften, Lehrstuhl für Ernährungsphysiologie der Technischen Universität München, Freising-Weihenstephan, Deutschland.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000641:Ammonia / Q000097:blood; D000818:Animals; D002222:Carbamoyl-Phosphate Synthase (Ammonia) / Q000378:metabolism; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D009584:Nitrogen / Q000378:metabolism*; D009954:Ornithine Carbamoyltransferase / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D014508:Urea / Q000097:blood*; D015032:Zinc / Q000172:deficiency*
D000641:Ammonia; D014508:Urea; D005969:Glutamate Dehydrogenase; D009954:Ornithine Carbamoyltransferase; D000469:Alkaline Phosphatase; D002222:Carbamoyl-Phosphate Synthase (Ammonia); D015032:Zinc; D009584:Nitrogen