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Membrane-bound α-Synuclein Has a High Aggregation Propensity and the Ability to Seed the Aggregation of the Cytosolic Form
Open accessAbstract
Alpha-synuclein exists as at least two structural isoforms: a helix-rich, membrane-bound form and a disordered, cytosolic form. Here, we investigated the role of membrane-bound alpha-synuclein in the aggregation process. In a cell-free system consisting of isolated brain fractions, spontaneous and progressive aggregation of alpha-synuclein was observed in membranes starting at day 1, whereas no aggregation was observed in the cytosolic fraction in a 3-day period. The addition of antioxidants reduced the aggregation in the membrane fraction, implicating the role of oxidative modifications. When excess cytosolic alpha-synuclein was added to brain membranes, the rate of aggregation was increased, while the lag time was unaffected. Incorporation of cytosolic alpha-synuclein into membrane-associated aggregates was demonstrated by fractionation and co-immunoprecipitation experiments. In our recent study, we showed that mitochondrial inhibitors such as rotenone, induced alpha-synuclein aggregation in cells. In the present study using rotenone-treated cells, the earliest appearance of alpha-synuclein oligomeric species was observed in membranous compartments. Furthermore, alpha-synuclein-positive inclusions were co-stained with DiI, a membrane-partitioning fluorescent dye, confirming the presence of lipid components in alpha-synuclein aggregates. These results suggest that membrane-bound alpha-synuclein can generate nuclei that seed the aggregation of the more abundant cytosolic form.
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Metadata
- Authors
- Lee, H.-J., Choi, C., & Lee, S.-J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 277
- Issue
- 1
- Pages
- 671-678
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2136012285
- Cited by
- 450
- References
- 13
- FWCI
- 10.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 6854 d)
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