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Small heat shock proteins inhibit in vitro Aβ 1–42 amyloidogenesis
Author(s) -
Kudva Yogish C,
Hiddinga Henry J,
Butler Peter C,
Mueske Cheryl S,
Eberhardt Norman L
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01180-0
Subject(s) - in vitro , chemistry , chaperone (clinical) , amyloid (mycology) , pathogenesis , heat shock protein , fibril , protein aggregation , biochemistry , biophysics , microbiology and biotechnology , biology , medicine , pathology , immunology , inorganic chemistry , gene
We demonstrate that small heat shock proteins (sHsp) inhibit in vitro amyloid formation by the Alzheimer's Aβ 1–42 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 Aβ 1–42 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 be 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.