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Vol. 8, No. 6, 2011
Issue release date: August 2011
Section title: Review
Neurodegenerative Dis 2011;8:397–412
(DOI:10.1159/000324514)

Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease

Hinault M.-P. · Farina-Henriquez-Cuendet A. · Goloubinoff P.
DBMV, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland

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Article / Publication Details

First-Page Preview
Abstract of Review

Received: 8/4/2010
Accepted: 1/21/2011
Published online: 3/16/2011
Issue release date: August 2011

Number of Print Pages: 16
Number of Figures: 3
Number of Tables: 0

ISSN: 1660-2854 (Print)
eISSN: 1660-2862 (Online)

For additional information: http://www.karger.com/NDD

Abstract

Parkinson’s disease (PD) is a slowly progressive neurodegenerative disorder marked by the loss of dopaminergic neurons (in particular in the substantia nigra) causing severe impairment of movement coordination and locomotion, associated with the accumulation of aggregated α-synuclein (α-Syn) into proteinaceous inclusions named Lewy bodies. Various early forms of misfolded α-Syn oligomers are cytotoxic. Their formation is favored by mutations and external factors, such as heavy metals, pesticides, trauma-related oxidative stress and heat shock. Here, we discuss the role of several complementing cellular defense mechanisms that may counteract PD pathogenesis, especially in youth, and whose effectiveness decreases with age. Particular emphasis is given to the ‘holdase’ and ‘unfoldase’ molecular chaperones that provide cells with potent means to neutralize and scavenge toxic protein conformers. Because chaperones can specifically recognize misfolded proteins, they are key specificity factors for other cellular defenses, such as proteolysis by the proteasome and autophagy. The efficiency of the cellular defenses decreases in stressed or aging neurons, leading to neuroinflammation, apoptosis and tissue loss. Thus, drugs that can upregulate the molecular chaperones, the ubiquitin-proteasome system and autophagy in brain tissues are promising avenues for therapies against PD and other mutation-, stress- or age-dependent protein-misfolding diseases.

© 2011 S. Karger AG, Basel


  

Author Contacts

Prof. Pierre Goloubinoff
Department of Plant Molecular Biology, Room 5427, Biology Building
University of Lausanne
CH–1015 Lausanne (Switzerland)
Tel. +41 21 692 4232, E-Mail Pierre.Goloubinoff@unil.ch

  

Article Information

Received: August 4, 2010
Accepted after revision: January 21, 2011
Published online: March 16, 2011
Number of Print Pages : 16
Number of Figures : 3, Number of Tables : 0, Number of References : 182

  

Publication Details

Neurodegenerative Diseases

Vol. 8, No. 6, Year 2011 (Cover Date: August 2011)

Journal Editor: Nitsch R.M. (Zürich), Hock C. (Zürich)
ISSN: 1660-2854 (Print), eISSN: 1660-2862 (Online)

For additional information: http://www.karger.com/NDD


Article / Publication Details

First-Page Preview
Abstract of Review

Received: 8/4/2010
Accepted: 1/21/2011
Published online: 3/16/2011
Issue release date: August 2011

Number of Print Pages: 16
Number of Figures: 3
Number of Tables: 0

ISSN: 1660-2854 (Print)
eISSN: 1660-2862 (Online)

For additional information: http://www.karger.com/NDD


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