The principal pathogenic event in Parkinson’s disease is characterized by the conforma-tional change of α‐synuclein, which form pathological aggregates of misfolded proteins, and then accumulate in intraneuronal inclusions causing dopaminergic neuronal loss in specific brain re-gions. Over the last few years, a revolutionary theory has correlated Parkinson’s disease and other neurological disorders with a shared mechanism, which determines α‐synuclein aggregates and progresses in the host in a prion‐like manner. In this review, the main characteristics shared between α‐synuclein and prion protein are compared and the cofactors that influence the remodeling of native protein structures and pathogenetic mechanisms underlying neuro-degeneration are discussed.

Parkinson’s disease: A prionopathy?

Vascellari S.;Manzin A.
2021-01-01

Abstract

The principal pathogenic event in Parkinson’s disease is characterized by the conforma-tional change of α‐synuclein, which form pathological aggregates of misfolded proteins, and then accumulate in intraneuronal inclusions causing dopaminergic neuronal loss in specific brain re-gions. Over the last few years, a revolutionary theory has correlated Parkinson’s disease and other neurological disorders with a shared mechanism, which determines α‐synuclein aggregates and progresses in the host in a prion‐like manner. In this review, the main characteristics shared between α‐synuclein and prion protein are compared and the cofactors that influence the remodeling of native protein structures and pathogenetic mechanisms underlying neuro-degeneration are discussed.
2021
Gut microbiota; Parkinson’s disease; Prion‐like mechanism; Protein misfolding co-factors; α‐synuclein
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/316860
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