Format

Send to:

Choose Destination
See comment in PubMed Commons below
ScientificWorldJournal. 2011;11:1893-907. doi: 10.1100/2011/371893. Epub 2011 Oct 24.

Interaction between α-synuclein and other proteins in neurodegenerative disorders.

Author information

  • 1Institute of Clinical Neurobiology, Kenyongasse 18, A-1070 Vienna, Austria. kurt.jellinger@univie.ac.at

Abstract

Protein aggregation is a common characteristic of many neurodegenerative disorders, and the interaction between pathological/toxic proteins to cause neurodegeneration is a hot topic of current neuroscience research. Despite clinical, genetic, and experimental differences, evidence increasingly indicates considerable overlap between synucleinopathies and tauopathies or other protein-misfolding diseases. Inclusions, characteristics of these disorders, also occurring in other neurodegenerative diseases, suggest interactions of pathological proteins engaging common downstream pathways. Novel findings that have shifted our understanding in the role of pathologic proteins in the pathogenesis of Parkinson and Alzheimer diseases have confirmed correlations/overlaps between these and other neurodegenerative disorders. The synergistic effects of α-synuclein, hyperphosphorylated tau, amyloid-β, and other pathologic proteins, and the underlying molecular pathogenic mechanisms, including induction and spread of protein aggregates, are critically reviewed, suggesting a dualism or triad of neurodegeneration in protein-misfolding disorders, although the etiology of most of these processes is still mysterious.

PMID:
22125446
[PubMed - indexed for MEDLINE]
PMCID:
PMC3217595
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Hindawi Publishing Corporation Icon for PubMed Central
    Loading ...
    Write to the Help Desk