| pubmed-article:9804562 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9804562 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:9804562 | lifeskim:mentions | umls-concept:C0001022 | lld:lifeskim |
| pubmed-article:9804562 | lifeskim:mentions | umls-concept:C2350345 | lld:lifeskim |
| pubmed-article:9804562 | lifeskim:mentions | umls-concept:C2004454 | lld:lifeskim |
| pubmed-article:9804562 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9804562 | pubmed:dateCreated | 1998-12-29 | lld:pubmed |
| pubmed-article:9804562 | pubmed:abstractText | Previous studies have demonstrated that oxygen consumption and fat oxidation remain elevated in the postexercise period. The purpose of this study was to determine whether malonyl-CoA, an inhibitor of fatty acid oxidation, remains depressed in muscle after exercise. Rats were sprinted for 5 min (40 m/min, 5% grade) or run for 30 min (21 m/min, 15% grade). Red quadriceps malonyl-CoA returned to resting values by 90 min postexercise in the sprinting rats and remained significantly lower at least 90 min postexercise in the 30-min exercise group. AMP-activated protein kinase activity remained significantly elevated (P < 0.05) for 10 min after exercise in both groups. The most rapid rate of glycogen repletion was in the first 30 min postexercise. The respiratory exchange ratio decreased from a nonexercise value of 0.87 +/- 0.01 to an average 0.82 +/- 0.01 during the 90-min period after 30 min of exercise. Thus muscle malonyl-CoA remains depressed and fat oxidation is elevated for relatively prolonged periods after a single bout of exercise. This may allow fat oxidation to contribute more to muscle energy requirements, thus leaving more glucose for replenishment of muscle glycogen. | lld:pubmed |
| pubmed-article:9804562 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804562 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9804562 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804562 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9804562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9804562 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9804562 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9804562 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9804562 | pubmed:issn | 8750-7587 | lld:pubmed |
| pubmed-article:9804562 | pubmed:author | pubmed-author:WinderW WWW | lld:pubmed |
| pubmed-article:9804562 | pubmed:author | pubmed-author:RasmussenB... | lld:pubmed |
| pubmed-article:9804562 | pubmed:author | pubmed-author:HancockC RCR | lld:pubmed |
| pubmed-article:9804562 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9804562 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:9804562 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9804562 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9804562 | pubmed:pagination | 1629-34 | lld:pubmed |
| pubmed-article:9804562 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9804562 | pubmed:meshHeading | pubmed-meshheading:9804562-... | lld:pubmed |
| pubmed-article:9804562 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9804562 | pubmed:articleTitle | Postexercise recovery of skeletal muscle malonyl-CoA, acetyl-CoA carboxylase, and AMP-activated protein kinase. | lld:pubmed |
| pubmed-article:9804562 | pubmed:affiliation | Department of Zoology, Brigham Young University, Provo, Utah 84602, USA. | lld:pubmed |
| pubmed-article:9804562 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9804562 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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