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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1980-7-26
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pubmed:abstractText |
In order to examine the mechanism of the acute response of ureagenesis to amino acid loads, rats were injected intraperitoneally with various doses of a mixture of 20 amino acids. Blood ammonia rose only slightly with doses of 0.5 to 2.0 g/kg, but increased sharply at doses of 3 to 5 g/kg. Carbamyl phosphate synthetase I (EC 2.7.2.5) activity, assayed in intact mitochondria isolated from livers removed 15 min after injection of amino acids, with N-acetylglutamate at its endogenous levels, rose up to 5-fold with increasing doses up to 2 g/kg; no further activation occurred with larger doses. This maximal activity was the same as the activity measured in disrupted mitochondria. Hepatic levels of glutamate and N-acetylglutamate increased approximately linearly with dose of amino acids. The time course of these changes following a dose of 1.5 g/kg was studied. Glutamate, N-acetylglutamate, and carbamyl phosphate synthetase I activity all peaked 5 to 15 min after injection. All of these results were virtually unaltered by omission of arginine from the injected mixture, indicating that the increase in N-acetylglutamate was not attributable to activation by arginine of N-acetylglutamate synthetase. These results indicate that moderate loads of amino acids activate unreagenesis via a rapid increase in N-acetylglutamate levels, secondary to increased mitochondrial glutamate, and independently of injected arginine. This autoregulatory mechanism becomes saturated at large doses of amino acids, and hyperammonemia then supervenes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Carbamoyl-Phosphate Synthase...,
http://linkedlifedata.com/resource/pubmed/chemical/Carbamoyl-Phosphate Synthase...,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylglutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Urea
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
255
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5270-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6246103-Acetyltransferases,
pubmed-meshheading:6246103-Amino Acids,
pubmed-meshheading:6246103-Amino-Acid N-Acetyltransferase,
pubmed-meshheading:6246103-Animals,
pubmed-meshheading:6246103-Arginine,
pubmed-meshheading:6246103-Carbamoyl-Phosphate Synthase (Ammonia),
pubmed-meshheading:6246103-Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing),
pubmed-meshheading:6246103-Female,
pubmed-meshheading:6246103-Glutamates,
pubmed-meshheading:6246103-Kinetics,
pubmed-meshheading:6246103-Liver,
pubmed-meshheading:6246103-Mitochondria, Liver,
pubmed-meshheading:6246103-Ornithine,
pubmed-meshheading:6246103-Phosphotransferases,
pubmed-meshheading:6246103-Rats,
pubmed-meshheading:6246103-Urea
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pubmed:year |
1980
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pubmed:articleTitle |
Short term regulation of ureagenesis.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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