Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.

Details

Ressource 1Download: serval:BIB_EC859331588D.P001 (1024.74 [Ko])
State: Public
Version: author
License: Not specified
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
Serval ID
serval:BIB_EC859331588D
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.
Journal
Journal of Molecular Neuroscience
Author(s)
Hinault M.P., Ben-Zvi A., Goloubinoff P.
ISSN
0895-8696 (Print)
ISSN-L
0895-8696
Publication state
Published
Issued date
2006
Volume
30
Number
3
Pages
249-265
Language
english
Abstract
The formation of toxic protein aggregates is a common denominator to many neurodegenerative diseases and aging. Accumulation of toxic, possibly infectious protein aggregates induces a cascade of events, such as excessive inflammation, the production of reactive oxygen species, apoptosis and neuronal loss. A network of highly conserved molecular chaperones and of chaperone-related proteases controls the fold-quality of proteins in the cell. Most molecular chaperones can passively prevent protein aggregation by binding misfolding intermediates. Some molecular chaperones and chaperone-related proteases, such as the proteasome, can also hydrolyse ATP to forcefully convert stable harmful protein aggregates into harmless natively refoldable, or protease-degradable, polypeptides. Molecular chaperones and chaperone-related proteases thus control the delicate balance between natively folded functional proteins and aggregation-prone misfolded proteins, which may form during the lifetime and lead to cell death. Abundant data now point at the molecular chaperones and the proteases as major clearance mechanisms to remove toxic protein aggregates from cells, delaying the onset and the outcome of protein-misfolding diseases. Therapeutic approaches include treatments and drugs that can specifically induce and sustain a strong chaperone and protease activity in cells and tissues prone to toxic protein aggregations.
Keywords
Aging/physiology, Alzheimer Disease/drug therapy, Alzheimer Disease/enzymology, Animals, Anti-Inflammatory Agents/therapeutic use, Heat-Shock Proteins/physiology, Humans, Molecular Chaperones/chemistry, Molecular Chaperones/physiology, Neurodegenerative Diseases/drug therapy, Neurodegenerative Diseases/enzymology, Peptide Hydrolases/chemistry, Peptide Hydrolases/metabolism, Proteasome Endopeptidase Complex/metabolism, Protein Conformation, Protein Folding
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 21:02
Last modification date
01/10/2019 7:20
Usage data