| pubmed-article:10086395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10086395 | lifeskim:mentions | umls-concept:C0002736 | lld:lifeskim |
| pubmed-article:10086395 | lifeskim:mentions | umls-concept:C0003069 | lld:lifeskim |
| pubmed-article:10086395 | lifeskim:mentions | umls-concept:C0599779 | lld:lifeskim |
| pubmed-article:10086395 | lifeskim:mentions | umls-concept:C0010286 | lld:lifeskim |
| pubmed-article:10086395 | lifeskim:mentions | umls-concept:C0815279 | lld:lifeskim |
| pubmed-article:10086395 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10086395 | pubmed:dateCreated | 1999-4-13 | lld:pubmed |
| pubmed-article:10086395 | pubmed:abstractText | Mitochondria are particularly vulnerable to oxidative stress, and mitochondrial swelling and vacuolization are among the earliest pathologic features found in two strains of transgenic amyotrophic lateral sclerosis (ALS) mice with SOD1 mutations. Mice with the G93A human SOD1 mutation have altered electron transport enzymes, and expression of the mutant enzyme in vitro results in a loss of mitochondrial membrane potential and elevated cytosolic calcium concentration. Mitochondrial dysfunction may lead to ATP depletion, which may contribute to cell death. If this is true, then buffering intracellular energy levels could exert neuroprotective effects. Creatine kinase and its substrates creatine and phosphocreatine constitute an intricate cellular energy buffering and transport system connecting sites of energy production (mitochondria) with sites of energy consumption, and creatine administration stabilizes the mitochondrial creatine kinase and inhibits opening of the mitochondrial transition pore. We found that oral administration of creatine produced a dose-dependent improvement in motor performance and extended survival in G93A transgenic mice, and it protected mice from loss of both motor neurons and substantia nigra neurons at 120 days of age. Creatine administration protected G93A transgenic mice from increases in biochemical indices of oxidative damage. Therefore, creatine administration may be a new therapeutic strategy for ALS. | lld:pubmed |
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| pubmed-article:10086395 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10086395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10086395 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10086395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10086395 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10086395 | pubmed:issn | 1078-8956 | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:FerranteR JRJ | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:MuellerGG | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:MatthewsR TRT | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:KleinA MAM | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:BealM FMF | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:BogdanovM BMB | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:Kaddurah-Daou... | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:AndreassenO... | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:KlivenyiPP | lld:pubmed |
| pubmed-article:10086395 | pubmed:author | pubmed-author:WermerMM | lld:pubmed |
| pubmed-article:10086395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10086395 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:10086395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10086395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10086395 | pubmed:pagination | 347-50 | lld:pubmed |
| pubmed-article:10086395 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10086395 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10086395 | pubmed:articleTitle | Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis. | lld:pubmed |
| pubmed-article:10086395 | pubmed:affiliation | Neurochemistry Laboratory, Neurology Service, Massachusetts General Hospital and Harvard Medical School, Boston 02118, USA. | lld:pubmed |
| pubmed-article:10086395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10086395 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10086395 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10086395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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