Source:http://linkedlifedata.com/resource/pubmed/id/15460447
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2004-10-4
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pubmed:abstractText |
Intraneuronal deposition containing alpha-synuclein is implicated in the pathogenesis of synuclein-opathies including Parkinsons disease (PD). Although it has been demonstrated that cytoplasmic inclusions of wild type alpha-synuclein are observed in the brain of PD patients and that alpha-synuclein mutations such as A30P and A53T accelerate aggregate formation, the exact mechanism by which alpha-synuclein forms insoluble aggregates is still controversial. In the present study, to understand the possible involvement of tissue transglutaminase (tTG) in aggregate formation of alpha-synuclein, SH-SY5Y cell lines stably expressing wild type or mutant (A30P or A53T) alpha-synuclein were created and aggregate formation of alpha-synuclein was observed upon activation of tTG. The data demonstrated that alpha-synuclein negligibly interacted with tTG and that activation of tTG did not result in the aggregate formation of alpha-synuclein in SH-SY5Y cells overexpressing either wild type or mutant alpha-synuclein. In addition, alpha-synuclein was not modified by activated tTG in situ. These data suggest that tTG is unlikely to be a contributing factor to the formation of aggregates of alpha-synuclein in a stable cell model.
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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/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/transglutaminase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0253-6269
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
850-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15460447-Cell Line, Tumor,
pubmed-meshheading:15460447-GTP-Binding Proteins,
pubmed-meshheading:15460447-Humans,
pubmed-meshheading:15460447-Nerve Tissue Proteins,
pubmed-meshheading:15460447-Neuroblastoma,
pubmed-meshheading:15460447-Synucleins,
pubmed-meshheading:15460447-Transglutaminases,
pubmed-meshheading:15460447-alpha-Synuclein
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pubmed:year |
2004
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pubmed:articleTitle |
Tissue transglutaminase is not involved in the aggregate formation of stably expressed alpha-synuclein in SH-SY5Y human neuroblastoma cells.
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pubmed:affiliation |
Department of Pharmacology, College of Medicine, Kangwon National University, Chunchon 200-701, Korea.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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