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Carboxy-terminal truncations of mouse α-synuclein alter aggregation and prion-like seeding.
- Source :
-
FEBS letters [FEBS Lett] 2020 Apr; Vol. 594 (8), pp. 1271-1283. Date of Electronic Publication: 2020 Jan 24. - Publication Year :
- 2020
-
Abstract
- α-synuclein (αsyn) forms pathologic inclusions in several neurodegenerative diseases termed synucleinopathies. The inclusions are comprised of αsyn fibrils harboring prion-like properties. Prion-like activity of αsyn has been studied by intracerebral injection of fibrils into mice, where the presence of a species barrier requires the use of mouse αsyn. Post-translational modifications to αsyn such as carboxy (C)-terminal truncation occur in synucleinopathies, and their implications for prion-like aggregation and seeding are under investigation. Herein, C-truncated forms of αsyn found in human disease are recapitulated in mouse αsyn to study their seeding activity in vitro, in HEK293T cells, in neuronal-glial culture, and in nontransgenic mice. The results show that C-truncation of mouse αsyn accelerates aggregation of αsyn but alters prion-like seeding of inclusion formation.<br /> (© 2020 Federation of European Biochemical Societies.)
- Subjects :
- Amyloid metabolism
Animals
Cells, Cultured
HEK293 Cells
Hippocampus metabolism
Hippocampus pathology
Humans
Injections
Mice, Inbred Strains
Neuroglia cytology
Neuroglia metabolism
Neurons pathology
Prions metabolism
alpha-Synuclein administration & dosage
alpha-Synuclein genetics
Neurons metabolism
alpha-Synuclein metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 594
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 31912891
- Full Text :
- https://doi.org/10.1002/1873-3468.13728