| pubmed-article:7721804 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7721804 | lifeskim:mentions | umls-concept:C1882687 | lld:lifeskim |
| pubmed-article:7721804 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:7721804 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:7721804 | lifeskim:mentions | umls-concept:C0085966 | lld:lifeskim |
| pubmed-article:7721804 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:7721804 | pubmed:dateCreated | 1995-5-19 | lld:pubmed |
| pubmed-article:7721804 | pubmed:abstractText | The expression pattern of mitochondrial carnitine palmitoyltransferase (CPT) enzymes was examined in the developing rat heart. Whereas the specific activity of CPT II increased approximately 3-fold during the first month of life, the profile for CPT I, which is composed of both liver (L) and muscle (M) isoforms, was more complex. Exposure of mitochondria to [3H]etomoxir (a covalent ligand for CPT I), followed by fluorographic analysis of the membrane proteins, established that while in the adult heart L-CPT I represents a very minor constituent, its contribution is much greater in the newborn animal. Use of the related inhibitor, 2-[6-(2,4-dinitrophenoxy)hexyl]oxirane-2-carboxylic acid (specific for L-CPT I), allowed the activities of the two CPT I variants to be quantified separately. The results showed that in the neonatal heart, L-CPT I contributes approximately 25% to total CPT I activity (in Vmax terms), the value falling during growth of the pups (with concomitant increasing expression of the M isoform) to its adult level of 2-3%. Because the myocardial carnitine content is very low at birth and rises dramatically over the next several weeks, it can be estimated that L-CPT I (Km for carnitine of only 30 microM compared with a value of 500 microM for M-CPT I) is responsible for some 60% of total cardiac fatty acid oxidation in the newborn rat; the value falls to approximately 4% in adult animals. Should these findings have a parallel in humans, they could have important implications for understanding the pathophysiological consequences of inherited L-CPT I deficiency syndromes. | lld:pubmed |
| pubmed-article:7721804 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7721804 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7721804 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7721804 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7721804 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7721804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7721804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7721804 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7721804 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7721804 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7721804 | pubmed:author | pubmed-author:McGarryJ DJD | lld:pubmed |
| pubmed-article:7721804 | pubmed:author | pubmed-author:FosterD WDW | lld:pubmed |
| pubmed-article:7721804 | pubmed:author | pubmed-author:BrownN FNF | lld:pubmed |
| pubmed-article:7721804 | pubmed:author | pubmed-author:WeilB JBJ | lld:pubmed |
| pubmed-article:7721804 | pubmed:author | pubmed-author:HustiJ EJE | lld:pubmed |
| pubmed-article:7721804 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7721804 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:7721804 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7721804 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7721804 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7721804 | pubmed:pagination | 8952-7 | lld:pubmed |
| pubmed-article:7721804 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
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| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:meshHeading | pubmed-meshheading:7721804-... | lld:pubmed |
| pubmed-article:7721804 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7721804 | pubmed:articleTitle | Mitochondrial carnitine palmitoyltransferase I isoform switching in the developing rat heart. | lld:pubmed |
| pubmed-article:7721804 | pubmed:affiliation | Department of Internal Medicine, University of Texas Southwestern Medical Center, Southwestern Medical School, Dallas 75235, USA. | lld:pubmed |
| pubmed-article:7721804 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7721804 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7721804 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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