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Vol 53(2019) N 3 p. 335-341; DOI 10.1134/S002689331903018X Full Text

A.L. Schwarzman1, K.A. Senkevich1,2, A.K. Emelyanov1,2, S.N. Pchelina1,2*

Prion Properties of Alpha-Synuclein

1Konstantinov St. Petersburg Nuclear Physics Institute, National Research Center Kurchatov Institute, Gatchina, Leningrad oblast, 188300 Russia
2Pavlov First St. Petersburg State Medical University, St. Petersburg, 197022 Russia

*pchelina_sn@pnpi.nrcki.ru
Received - 2018-12-28; Revised - 2019-01-10; Accepted - 2019-01-10

The prion properties of alpha-synuclein, a key aggregating protein involved in the pathogenesis of so-called synucleinopathies, including Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and its various conformers are discussed. It is shown that alpha-synuclein may be transferred between cells by prion-like propagation. Similarly to other prions, alpha-synuclein aggregation develops from the initial lag-phase (nucleation) to the subsequent growth phase (elongation), and to the stationary phase where the aggregates and monomers exist in equilibrium. Similarly to prions, alpha-synuclein undergoes conformational changes from an alpha-helix to its beta-folded structure. However, there is currently no evidence that alpha-synuclein-dependent PD can be transmitted from person-to-person. This review describes the prion properties of alpha-synuclein, possible ways of its intercellular propagation, and novel approaches to PD diagnostics.

Parkinson's disease, alpha-synuclein, prions, alpha-synuclein transmission



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