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