Source:http://linkedlifedata.com/resource/pubmed/id/20123086
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2010-3-8
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pubmed:abstractText |
Parkinson's disease (PD) is a common neurodegenerative disorder. The motor neuron degeneration 2 mutant (mnd2) mouse exhibits loss of striatal neurons, muscle wasting, weight loss, and death within 40days of birth, and is considered to be a useful animal model of PD. mnd2 was identified as an autosomal recessive mutation in the HtrA2/Omi gene, which encodes a mitochondrial serine protease. Omi-deficient mitochondria are more sensitive to mitochondrial permeability transition (mPT), which raises the possibility that mPT plays a role in motor neurodegeneration in mnd2 mice. Given that cyclophilin D (CypD)-deficient mitochondria are resistant to mPT, we examined whether CypD-dependent mPT is involved in the pathogenesis of neurodegenerative disorders in mnd2 mice by generating CypD-deficient mnd2 mice. Brain mitochondria isolated from CypD-deficient mnd2 mice were more resistant to Ca(2+)-induced mPT than those of mnd2 mice. However, both mnd2 mice and CypD-deficient mnd2 mice showed similar survival periods and phenotypes, including the lack of weight gain, muscle wasting, and resting tremor. Our data suggest that CypD-dependent mPT does not play a major role in neurodegeneration in mnd2 mice.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclophilins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Omi serine protease,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/cyclophilin D
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1090-2104
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pubmed:author | |
pubmed:copyrightInfo |
2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
393
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
264-7
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pubmed:meshHeading |
pubmed-meshheading:20123086-Animals,
pubmed-meshheading:20123086-Brain,
pubmed-meshheading:20123086-Cyclophilins,
pubmed-meshheading:20123086-Mice,
pubmed-meshheading:20123086-Mice, Mutant Strains,
pubmed-meshheading:20123086-Mitochondria,
pubmed-meshheading:20123086-Mitochondrial Membranes,
pubmed-meshheading:20123086-Mitochondrial Proteins,
pubmed-meshheading:20123086-Neurodegenerative Diseases,
pubmed-meshheading:20123086-Parkinson Disease,
pubmed-meshheading:20123086-Permeability,
pubmed-meshheading:20123086-Serine Endopeptidases
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pubmed:year |
2010
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pubmed:articleTitle |
Cyclophilin D-dependent mitochondrial permeability transition is not involved in neurodegeneration in mnd2 mutant mice.
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pubmed:affiliation |
Department of General Thoracic Surgery, Osaka University Medical School, Yamadaoka, Suita, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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