Abstract
We demonstrate that small heat shock proteins (sHsp) inhibit in vitro amyloid formation by the Alzheimer's Aβ1-42 polypeptide as detected by a thioflavine T fluorescence assay and electron microscopy. Human sHsp27 (0.50-3.0 μM) inhibited amyloid formation from 20 μM Aβ1-42 by 23-75% in 24 h. In contrast, treatment of pre-formed amyloid with 0.5-3.0 μM sHsp27 only reduced the fluorescence signal by 6-36%. The data suggest that ordered fibril formation may represent a form of off-pathway aggregation that can he prevented by chaperone action. The data raise the possibility that age-related changes in chaperone function could contribute toward the pathogenesis of Alzheimer's and other amyloid-associated diseases.
Original language | English (US) |
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Pages (from-to) | 117-121 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 416 |
Issue number | 1 |
DOIs | |
State | Published - Oct 13 1997 |
Keywords
- Alzheimer's disease
- Amyloidogenesis
- Chaperone
- Heat shock protein
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology