Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
Identifieur interne : 000301 ( Main/Exploration ); précédent : 000300; suivant : 000302Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
Auteurs : Daniel W. Neef [États-Unis] ; Alex M. Jaeger [États-Unis] ; Dennis J. Thiele [États-Unis]Source :
- Nature Reviews Drug Discovery [ 1474-1776 ] ; 2011-12.
Abstract
Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis and prion-based neurodegeneration are associated with the accumulation of misfolded proteins, resulting in neuronal dysfunction and cell death. However, current treatments for these diseases predominantly address disease symptoms, rather than the underlying protein misfolding and cell death, and are not able to halt or reverse the degenerative process. Studies in cell culture, fruitfly, worm and mouse models of protein misfolding-based neurodegenerative diseases indicate that enhancing the protein-folding capacity of cells, via elevated expression of chaperone proteins, has therapeutic potential. Here, we review advances in strategies to harness the power of the natural cellular protein-folding machinery through pharmacological activation of heat shock transcription factor 1 — the master activator of chaperone protein gene expression — to treat neurodegenerative diseases.
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DOI: 10.1038/nrd3453
Affiliations:
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All Rights Reserved.</publisher><date type="published" when="2011-12">2011-12</date><biblScope unit="volume">10</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="930">930</biblScope><biblScope unit="page" to="944">944</biblScope></imprint><idno type="ISSN">1474-1776</idno></series><idno type="istex">75D296ED88F1203C7C2C2BAE191D092DCC6A21DE</idno><idno type="DOI">10.1038/nrd3453</idno><idno type="ArticleID">nrd3453</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1474-1776</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="eng">Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis and prion-based neurodegeneration are associated with the accumulation of misfolded proteins, resulting in neuronal dysfunction and cell death. However, current treatments for these diseases predominantly address disease symptoms, rather than the underlying protein misfolding and cell death, and are not able to halt or reverse the degenerative process. Studies in cell culture, fruitfly, worm and mouse models of protein misfolding-based neurodegenerative diseases indicate that enhancing the protein-folding capacity of cells, via elevated expression of chaperone proteins, has therapeutic potential. Here, we review advances in strategies to harness the power of the natural cellular protein-folding machinery through pharmacological activation of heat shock transcription factor 1 — the master activator of chaperone protein gene expression — to treat neurodegenerative diseases.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Neef, Daniel W" sort="Neef, Daniel W" uniqKey="Neef D" first="Daniel W." last="Neef">Daniel W. Neef</name></noRegion><name sortKey="Jaeger, Alex M" sort="Jaeger, Alex M" uniqKey="Jaeger A" first="Alex M." last="Jaeger">Alex M. Jaeger</name><name sortKey="Thiele, Dennis J" sort="Thiele, Dennis J" uniqKey="Thiele D" first="Dennis J." last="Thiele">Dennis J. Thiele</name><name sortKey="Thiele, Dennis J" sort="Thiele, Dennis J" uniqKey="Thiele D" first="Dennis J." last="Thiele">Dennis J. Thiele</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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