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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1976-7-6
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pubmed:abstractText |
In a group of ten adult obese subjects, maintained for 15 days on a normal caloric intake and balanced diet, the activity of hexokinase (EC 2.7.1.1),6-phosphofructokinase (EC 2.7.1.11), and ATP citratelyase (EC 4.1.3.8) in the adipose tissue was significantly increased, both on a protein and on a fat cell number basis, compared to matched normal subjects. The activity of glucose-6-phosphate dehydrogenase (EC 1.1.1.49), malate dehydrogenase (EC 1.1.1.37), and malate dehydrogenase (decarboxylating) (NADP) (EC 1.1.1.40), on the other hand, was unchanged. Since both hexokinase and 6-phosphofructokinase are rate-limiting in glycolysis, their enhanced activity would indicate the occurrence of an increased capacity to metabolize glucose and therefore to generate alpha-glycerophosphate. The elevation of ATP citrate-lyase would suggest increased lipogenesis, owing to the regulatory role that this enzyme plays in fatty acid synthesis. The normal activity of glucose-6-phosphate dehydrogenase and malate dehydrogenase (decarboxylating) (NADP), which supply NADPH for the reduction of acetyl-CoA to fatty acids, would suggest that the change in lipogenesis is of moderate degree, thereb) affecting only the most rate-limiting enzyme, ATP citrate-lyase. These data, on the whole, are consistent with the occurrence of enhanced triglyceride formation. Whether the enzyme changes observed are adaptive or genetic in nature remains to be clarified.
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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/ATP Citrate (pro-S)-Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosephosphate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphofructokinase-1
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0026-0495
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
483-93
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:131232-ATP Citrate (pro-S)-Lyase,
pubmed-meshheading:131232-Adipose Tissue,
pubmed-meshheading:131232-Adult,
pubmed-meshheading:131232-Aged,
pubmed-meshheading:131232-Clinical Trials as Topic,
pubmed-meshheading:131232-Female,
pubmed-meshheading:131232-Glucosephosphate Dehydrogenase,
pubmed-meshheading:131232-Hexokinase,
pubmed-meshheading:131232-Humans,
pubmed-meshheading:131232-Lipids,
pubmed-meshheading:131232-Malate Dehydrogenase,
pubmed-meshheading:131232-Male,
pubmed-meshheading:131232-Middle Aged,
pubmed-meshheading:131232-Obesity,
pubmed-meshheading:131232-Phosphofructokinase-1
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pubmed:year |
1976
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pubmed:articleTitle |
Enzymes related to lipogenesis in the adipose tissue of obese subjects.
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pubmed:publicationType |
Journal Article,
Clinical Trial,
Comparative Study
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