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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1990-3-20
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pubmed:abstractText |
ATP-driven citrulline synthesis by mitochondria treated with oligomycin, uncoupler and Ca2+ ionophore is stimulated more than 2-fold by an increase in extramitochondrial free [Ca2+] in the range 1-5 microM. Stimulation increases with the length of preincubation of mitochondria with Ca2+. EGTA prevents stimulation if added at the start of the preincubation period, but is without effect if added at the end, suggesting that Ca2+ acts indirectly on citrulline synthesis via the accumulation of an intermediate. Neither carbamoyl-phosphate synthase (ammonia) nor ornithine carbamoyltransferase are stimulated by up to 50 microM free Ca2+ in mitochondrial extracts, but N-acetylglutamate synthase is stimulated about 30% by 10 microM free Ca2+. We propose that an increase in the activity of N-acetylglutamate synthase in response to an increase in free [Ca2+] in the mitochondrial matrix may contribute to hormonal stimulation of the urea cycle.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Amino-Acid N-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carbamoyl-Phosphate Synthase...,
http://linkedlifedata.com/resource/pubmed/chemical/Citrulline,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylglutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Oligomycins,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Carbamoyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
1033
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2105747-Acetyltransferases,
pubmed-meshheading:2105747-Adenosine Triphosphate,
pubmed-meshheading:2105747-Amino-Acid N-Acetyltransferase,
pubmed-meshheading:2105747-Animals,
pubmed-meshheading:2105747-Calcimycin,
pubmed-meshheading:2105747-Calcium,
pubmed-meshheading:2105747-Carbamoyl-Phosphate Synthase (Ammonia),
pubmed-meshheading:2105747-Citrulline,
pubmed-meshheading:2105747-Egtazic Acid,
pubmed-meshheading:2105747-Female,
pubmed-meshheading:2105747-Glutamates,
pubmed-meshheading:2105747-Magnesium,
pubmed-meshheading:2105747-Mitochondria, Liver,
pubmed-meshheading:2105747-Oligomycins,
pubmed-meshheading:2105747-Ornithine Carbamoyltransferase,
pubmed-meshheading:2105747-Rats,
pubmed-meshheading:2105747-Rats, Inbred Strains
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pubmed:year |
1990
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pubmed:articleTitle |
The mechanism of Ca2+ stimulation of citrulline and N-acetylglutamate synthesis by mitochondria.
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pubmed:affiliation |
Department of Biochemistry, University of Cambridge, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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