| Literature DB >> 11698390 |
Muhammad Abdul Alim1, Mosammat Shahanara Hossain, Kunimasa Arima, Kazuya Takeda, Yoko Izumiyama, Minako Nakamura, Hiroyuki Kaji, Tomotaka Shinoda, Shinichi Hisanaga, Kenji Ueda.
Abstract
Increasing evidence suggests that alpha-synuclein is a common pathogenic molecule in several neurodegenerative diseases, particularly in Parkinson's disease. To understand alpha-synuclein pathology, we investigated molecules that interact with alpha-synuclein in human and rat brains and identified tubulin as an alpha-synuclein binding/associated protein. Tubulin co-localized with alpha-synuclein in Lewy bodies and other alpha-synuclein-positive pathological structures. Tubulin initiated and promoted alpha-synuclein fibril formation under physiological conditions in vitro. These findings suggest that an interaction between tubulin and alpha-synuclein might accelerate alpha-synuclein aggregation in diseased brains, leading to the formation of Lewy bodies.Entities:
Mesh:
Substances:
Year: 2001 PMID: 11698390 DOI: 10.1074/jbc.M102981200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157