Work

Carboxy‐terminal truncations of mouse α‐synuclein alter aggregation and prion‐like seeding

Year: 2020

Type: article

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.

Source: FEBS Letters

DOI: 10.1002/1873-3468.13728

Authors: Zachary A. Sorrentino, Yuxing Xia, Kimberly‐Marie Gorion, Ethan Hass, Benoit I. Giasson

Institutions: University of Florida Health, University of Florida

Language: English

Topic: Parkinson's Disease Mechanisms and Treatments

Subfield: Neurology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: University of Florida, National Institutes of Health, National Institute on Aging, National Institute of Neurological Disorders and Stroke