Co-association of parkin and α-synuclein
| Autor: | Leonard Petrucelli, Heather Snyder, Dennis Sparkman, Benjamin Wolozin, Peter Choi, Matthew Chong, Elizabeth J. Cochran, Natalie Golts, J.M. Lee, John Hardy |
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| Rok vydání: | 2001 |
| Předmět: |
Pathology
medicine.medical_specialty Dopamine Ubiquitin-Protein Ligases animal diseases Synucleins Nerve Tissue Proteins Antibodies Parkin Ligases chemistry.chemical_compound Degenerative disease Ubiquitin mental disorders Tumor Cells Cultured medicine Humans Ferrous Compounds Aged Alpha-synuclein Binding Sites biology Lewy body General Neuroscience Parkinsonism Brain Parkinson Disease medicine.disease Immunohistochemistry Precipitin Tests Axons nervous system diseases Ubiquitin ligase Cell biology Oxidative Stress nervous system chemistry alpha-Synuclein biology.protein Lewy Bodies medicine.drug |
| Zdroj: | Neuroreport. 12:2839-2843 |
| ISSN: | 0959-4965 |
| Popis: | Parkin and alpha-synuclein are two proteins that are associated with the pathophysiology of Parkinson's disease (PD). Parkin is present in Lewy bodies and axonal spheroids in brains affected by PD, and mutations in parkin cause hereditary forms of Parkinsonism. Alpha-synuclein is a major component of Lewy bodies and is associated with rare cases of PD. We now show that parkin binds to alpha-synuclein, including conditions associated with alpha-synuclein aggregation. Parkin and alpha-synuclein complexes were observed in BE-M17 cells under basal conditions, in BE- M17 cells under oxidative conditions and in brains from control or PD donors. Double staining of PD brains shows parkin and alpha-synuclein co-localize to the same pathological structures (both Lewy bodies and axonal spheroids). These results suggest that parkin interacts with alpha-synuclein and could contribute to the pathophysiology of PD more generally than was previously considered. |
| Databáze: | OpenAIRE |
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