Source:http://linkedlifedata.com/resource/pubmed/id/17179390
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2007-4-2
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| pubmed:abstractText |
A key regulatory point in the control of fatty acid (FA) oxidation is thought to be transport of FAs across the mitochondrial membrane by carnitine palmitoyltransferase I (CPT I). To investigate the role of CPT I in FA metabolism, we used in vivo electrotransfer (IVE) to locally overexpress CPT I in muscle of rodents. A vector expressing the human muscle isoform of CPT I was electrotransferred into the right lateral muscles of the distal hindlimb [tibialis cranialis (TC) and extensor digitorum longus (EDL)] of rats, and a control vector expressing GFP was electrotransferred into the left muscles. Initial studies showed that CPT I protein expression peaked 7 days after IVE (+104%, P<0.01). This was associated with an increase in maximal CPT I activity (+30%, P < 0.001) and a similar increase in palmitoyl-CoA oxidation (+24%; P<0.001) in isolated mitochondria from the TC. Importantly, oxidation of the medium-chain FA octanoyl-CoA and CPT I sensitivity to inhibition by malonyl-CoA were not altered by CPT I overexpression. FA oxidation in isolated EDL muscle strips was increased with CPT I overexpression (+28%, P<0.01), whereas FA incorporation into the muscle triacylglycerol (TAG) pool was reduced (-17%, P<0.01). As a result, intramyocellular TAG content was decreased with CPT I overexpression in both the TC (-25%, P<0.05) and the EDL (-45%, P<0.05). These studies demonstrate that acute overexpression of CPT I in muscle leads to a repartitioning of FAs away from esterification and toward oxidation and highlight the importance of CPT I in regulating muscle FA metabolism.
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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/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Carnitine O-Palmitoyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitates,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitoyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0193-1849
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
292
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
E1231-7
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| pubmed:meshHeading |
pubmed-meshheading:17179390-Animals,
pubmed-meshheading:17179390-Biological Markers,
pubmed-meshheading:17179390-Carnitine O-Palmitoyltransferase,
pubmed-meshheading:17179390-Electroporation,
pubmed-meshheading:17179390-Esterification,
pubmed-meshheading:17179390-Fatty Acids,
pubmed-meshheading:17179390-Hindlimb,
pubmed-meshheading:17179390-Humans,
pubmed-meshheading:17179390-Lipid Metabolism,
pubmed-meshheading:17179390-Male,
pubmed-meshheading:17179390-Mitochondria, Muscle,
pubmed-meshheading:17179390-Muscle, Skeletal,
pubmed-meshheading:17179390-Oxidation-Reduction,
pubmed-meshheading:17179390-Palmitates,
pubmed-meshheading:17179390-Palmitoyl Coenzyme A,
pubmed-meshheading:17179390-Rats,
pubmed-meshheading:17179390-Rats, Wistar,
pubmed-meshheading:17179390-Transfection,
pubmed-meshheading:17179390-Triglycerides
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| pubmed:year |
2007
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| pubmed:articleTitle |
Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces triacylglycerol esterification.
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| pubmed:affiliation |
Diabetes and Obesity Research Program, Garvan Institute of Medical Research, Darlinghurst. clinton.bruce@baker.edu.au
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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