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rdf:type |
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lifeskim:mentions |
umls-concept:C0017687,
umls-concept:C0023884,
umls-concept:C0024735,
umls-concept:C0034693,
umls-concept:C0075444,
umls-concept:C0087111,
umls-concept:C0442805,
umls-concept:C0456205,
umls-concept:C0521451,
umls-concept:C0547047,
umls-concept:C1550605,
umls-concept:C2260318
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pubmed:issue |
1
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pubmed:dateCreated |
1989-12-7
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pubmed:abstractText |
1. The activity of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (EC 4.1.3.5) in extracts of rapidly frozen rat livers was doubled in animals treated in various ways to increase ketogenic flux. 2. Some 90% of the activity measured was mitochondrial, and changes in mitochondrial activity dominated changes in total enzyme activity. 3. The elevated HMG-CoA synthase activities persisted throughout the isolation of liver mitochondria. 4. Intramitochondrial succinyl-CoA content was lower in whole liver homogenates and in mitochondria isolated from animals treated with glucagon or mannoheptulose. 5. HMG-CoA synthase activity in mitochondria from both ox and rat liver was negatively correlated with intramitochondrial succinyl-CoA levels when these were manipulated artificially. Under these conditions, the differences between mitochondria from control and hormone-treated rats were abolished. 6. These findings show that glucagon can decrease intramitochondrial succinyl-CoA concentration, and that this in turn can regulate mitochondrial HMG-CoA synthase. They support the hypothesis that the formation of ketone bodies from acetyl-CoA may be regulated by the extent of succinylation of mitochondrial HMG-CoA synthase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-1133169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-164460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-235540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-240844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-2860895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-2867762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-2896605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3028411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3277623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3281653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3426552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3518632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3593202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3593203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-360007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3814087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-3902546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-4291787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-46337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-4700191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-4803501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-5127428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-5449124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-5667251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6052434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6092358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6094292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6118268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6131897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6152703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6157353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6251802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-6435625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-874089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2573345-93966
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-64
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2573345-Acyl Coenzyme A,
pubmed-meshheading:2573345-Animals,
pubmed-meshheading:2573345-Enzyme Activation,
pubmed-meshheading:2573345-Female,
pubmed-meshheading:2573345-Glucagon,
pubmed-meshheading:2573345-Heptoses,
pubmed-meshheading:2573345-Hydroxymethylglutaryl-CoA Synthase,
pubmed-meshheading:2573345-Ketoglutaric Acids,
pubmed-meshheading:2573345-Mannoheptulose,
pubmed-meshheading:2573345-Mitochondria, Liver,
pubmed-meshheading:2573345-Oxo-Acid-Lyases,
pubmed-meshheading:2573345-Rats,
pubmed-meshheading:2573345-Rats, Inbred Strains
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pubmed:year |
1989
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pubmed:articleTitle |
Treatment of rats with glucagon or mannoheptulose increases mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase activity and decreases succinyl-CoA content in liver.
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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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