title: The dogfish shark (Squalus acanthias) increases both hepatic and extrahepatic ornithine urea cycle enzyme activities for nitrogen conservation after feeding.
abstract: Urea not only is utilized as a major osmolyte in marine elasmobranchs but also constitutes their main nitrogenous waste. This study investigated the effect of feeding, and thus elevated nitrogen intake, on nitrogen metabolism in the Pacific spiny dogfish Squalus acanthias. We determined the activities of ornithine urea cycle (O-UC) and related enzymes in liver and nonhepatic tissues. Carbamoyl phosphate synthetase III (the rate-limiting enzyme of the O-UC) activity in muscle is high compared with liver, and the activities in both tissues increased after feeding. The contribution of muscle to urea synthesis in the dogfish body appears to be much larger than that of liver when body mass is considered. Furthermore, enhanced activities of the O-UC and related enzymes (glutamine synthetase, ornithine transcarbamoylase, arginase) were seen after feeding in both liver and muscle and were accompanied by delayed increases in plasma urea, trimethylamine oxide, total free amino acids, alanine, and chloride concentrations, as well as in total osmolality. The O-UC and related enzymes also occurred in the intestine but showed little change after feeding. Feeding did not change the rate of urea excretion, indicating strong N retention after feeding. Ammonia excretion, which constituted only a small percentage of total N excretion, was raised in fed fish, while plasma ammonia did not change, suggesting that excess ammonia in plasma is quickly ushered into synthesis of urea or protein. In conclusion, we suggest that N conservation is a high priority in this elasmobranch and that feeding promotes ureogenesis and growth. Furthermore, exogenous nitrogen from food is converted into urea not only by the liver but also by the muscle and to a small extent by the intestine.
authors.affiliation: Department of Biology, McMaster University, Hamilton, Ontario, Canada. kajimur@mcmaster.ca
authors.forename: Makiko
authors.initials: M
authors.lastname: Kajimura
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Walsh
authors.forename: Thomas P
authors.initials: TP
authors.lastname: Mommsen
authors.forename: Chris M
authors.initials: CM
authors.lastname: Wood
mesh_terms: D000409:Alanine / Q000097:blood; D000641:Ammonia / Q000378:metabolism; D000818:Animals; D001119:Arginase / Q000378:metabolism; D019731:Carbon-Nitrogen Ligases / Q000378:metabolism; D002712:Chlorides / Q000097:blood; D004435:Eating / Q000502:physiology; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D008744:Methylamines / Q000097:blood; D018482:Muscle, Skeletal / Q000201:enzymology / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D009952:Ornithine / Q000378:metabolism*; D009954:Ornithine Carbamoyltransferase / Q000378:metabolism; D048251:Squalus acanthias / Q000378:metabolism*; D014508:Urea / Q000097:blood / Q000378:metabolism*
chemical_list: D002712:Chlorides; D008744:Methylamines; D000641:Ammonia; D014508:Urea; D009952:Ornithine; D009954:Ornithine Carbamoyltransferase; D001119:Arginase; D019731:Carbon-Nitrogen Ligases; D005974:Glutamate-Ammonia Ligase; C024233:carbamoyl-phosphate synthetase (N-acetylglutamate); C005855:trimethyloxamine; D009584:Nitrogen; D000409:Alanine