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PubMed: 12714745

Title
Initiation and synergistic fibrillization of tau and alpha-synuclein.
Journal
Science (New York, N.Y.)
Volume
300
Issue
None
Pages
636-40
Date
2003-04-25
Authors
Higuchi M | Golbe LI | Lee VM | Kotzbauer PT | Giasson BI | Graves CL | Forman MS | Trojanowski JQ

Evidence 8272c3a246
JSON

Recent studies of an individual with Parkinson’s disease (IX-47) of the Contursi kindred with the rare A53T alpha-synuclein mutation revealed widespread -syn and tau inclusions (15). Post-mortem examination of another affected member (IX-51) of this kindred also demonstrated abundant -syn and tau inclusions(figs. S1 and S2). Thus, a pathogenic mutation in alpha-synuclein that is known to increase the propensity of alpha-synuclein to fibrillize (8, 9) also promotes formation of tau inclusions in humans.

complex(GO:"Lewy body") positiveCorrelation g(DBSNP:rs104893877) View Subject | View Object

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

complex(GO:"neurofibrillary tangle") positiveCorrelation g(DBSNP:rs104893877) View Subject | View Object

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

g(DBSNP:rs104893877) positiveCorrelation complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

g(DBSNP:rs104893877) positiveCorrelation complex(GO:"Lewy body") View Subject | View Object

Appears in Networks:
Annotations
Disease Ontology (DO)
Parkinson's disease

Evidence 5366de6bdf
JSON

We also observed that tau and alpha-synuclein synergistically promote and propagate each other’s polymerization into fibrils

composite(p(HGNC:MAPT), p(HGNC:SNCA)) increases complex(GO:"Lewy body") View Subject | View Object

Appears in Networks:

composite(p(HGNC:MAPT), p(HGNC:SNCA)) increases complex(GO:"neurofibrillary tangle") View Subject | View Object

Appears in Networks:

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