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Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains
Open accessAbstract
TDP-43 is the major component protein of ubiquitin-positive inclusions in brains of patients with frontotemporal lobar degeneration (FTLD-TDP) or amyotrophic lateral sclerosis (ALS). Here, we report the characterization of prion-like properties of aggregated TDP-43 prepared from diseased brains. When insoluble TDP-43 from ALS or FTLD-TDP brains was introduced as seeds into SH-SY5Y cells expressing TDP-43, phosphorylated and ubiquitinated TDP-43 was aggregated in a self-templating manner. Immunoblot analyses revealed that the C-terminal fragments of insoluble TDP-43 characteristic of each disease type acted as seeds, inducing seed-dependent aggregation of TDP-43 in these cells. The seeding ability of insoluble TDP-43 was unaffected by proteinase treatment but was abrogated by formic acid. One subtype of TDP-43 aggregate was resistant to boiling treatment. The insoluble fraction from cells harboring TDP-43 aggregates could also trigger intracellular TDP-43 aggregation. These results indicate that insoluble TDP-43 has prion-like properties that may play a role in the progression of TDP-43 proteinopathy.
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Metadata
- Authors
- Nonaka, T., Masuda-Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., Yoshida, M., Murayama, S., Mann, D. M. A., Akiyama, H., & Hasegawa, M.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 4
- Issue
- 1
- Pages
- 124-134
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2170087857
- Cited by
- 521
- References
- 45
- FWCI
- 23.37
- Type
- journal article
- Language
- en
- Open access
- gold
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