α-Synuclein overexpression promotes aggregation of mutant huntingtin
| Autor: | David C. Rubinsztein, Julia Rankin, Andreas Wyttenbach, Yolanda Narain, Robert A. Furlong |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Alpha-synuclein
congenital hereditary and neonatal diseases and abnormalities Huntingtin Chemistry Mutant Cell Biology Transfection Protein aggregation Biochemistry Molecular biology nervous system diseases Green fluorescent protein chemistry.chemical_compound nervous system mental disorders Huntingtin Protein Nuclear protein Molecular Biology |
| Zdroj: | Biochemical Journal. 346:577-581 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3460577 |
| Popis: | Protein aggregates are a neuropathological feature of Huntington's disease and Parkinson's disease. Mutant huntingtin exon 1 with 72 CAG repeats fused to enhanced green fluorescent protein (EGFP) forms hyperfluorescent inclusions in PC12 cells. Inclusion formation is enhanced in cells co-transfected with EGFP-huntingtin-(CAG)72 and α-synuclein, a major component of Parkinson's disease aggregates. However, α-synuclein does not form aggregates by itself, nor does it appear in huntingtin inclusions in vitro. |
| Databáze: | OpenAIRE |
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