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.
| File | Dimensione | Formato | |
|---|---|---|---|
|
ijms-22-08022-v2.pdf
accesso aperto
Tipologia:
versione editoriale (VoR)
Dimensione
336 kB
Formato
Adobe PDF
|
336 kB | Adobe PDF | Visualizza/Apri |
I metadati presenti in IRIS UNICA sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono protetti da diritto d'autore, salvo diversa indicazione.
