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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5619
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pubmed:dateCreated |
2003-4-25
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pubmed:abstractText |
Alpha-synuclein (alpha-syn) and tau polymerize into amyloid fibrils and form intraneuronal filamentous inclusions characteristic of neurodegenerative diseases. We demonstrate that alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins. The in vivo relevance of these findings is grounded in the co-occurrence of alpha-syn and tau filamentous amyloid inclusions in humans, in single transgenic mice that express A53T human alpha-syn in neurons, and in oligodendrocytes of bigenic mice that express wild-type human alpha-syn plus P301L mutant tau. This suggests that interactions between alpha-syn and tau can promote their fibrillization and drive the formation of pathological inclusions in human neurodegenerative diseases.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid,
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/SNCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Snca protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/tau Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
300
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
636-40
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:12714745-Amyloid,
pubmed-meshheading:12714745-Animals,
pubmed-meshheading:12714745-Biopolymers,
pubmed-meshheading:12714745-Brain Chemistry,
pubmed-meshheading:12714745-Humans,
pubmed-meshheading:12714745-Mice,
pubmed-meshheading:12714745-Mice, Inbred C3H,
pubmed-meshheading:12714745-Mice, Inbred C57BL,
pubmed-meshheading:12714745-Mice, Transgenic,
pubmed-meshheading:12714745-Microscopy, Electron,
pubmed-meshheading:12714745-Microscopy, Fluorescence,
pubmed-meshheading:12714745-Microscopy, Immunoelectron,
pubmed-meshheading:12714745-Nerve Tissue Proteins,
pubmed-meshheading:12714745-Neurodegenerative Diseases,
pubmed-meshheading:12714745-Neurons,
pubmed-meshheading:12714745-Oligodendroglia,
pubmed-meshheading:12714745-Protein Conformation,
pubmed-meshheading:12714745-Protein Isoforms,
pubmed-meshheading:12714745-Synucleins,
pubmed-meshheading:12714745-Tauopathies,
pubmed-meshheading:12714745-alpha-Synuclein,
pubmed-meshheading:12714745-tau Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Initiation and synergistic fibrillization of tau and alpha-synuclein.
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pubmed:affiliation |
Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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