Journal
PROTEIN SCIENCE
Volume 19, Issue 4, Pages 836-846Publisher
WILEY
DOI: 10.1002/pro.363
Keywords
amyloid disassembly; amyloid depolymerization; amyloid fragmentation; amyloid dissociation; Alzheimer's disease; aggregation; gelsolin; Abeta
Categories
Funding
- NIH [AG031097]
- Proteostasis Therapeutics, Inc.
- Skaggs Institute for Chemical Biology
- Lita Annenberg Hazen Foundation
- Bruce Ford and Anne Smith Bundy Foundation
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The formation of amyloid, a cross-beta-sheet fibrillar aggregate, is associated with a variety of aging-associated degenerative diseases. Herein, we report the existence of a mammalian amyloid disaggregase activity that is present in all tissues and cell types tested. Homogenates from mammalian tissues and cell lines are able to disaggregate amyloid fibrils composed of amyloid beta (A beta)(1-40) or the 8 kDa plasma gelsolin fragment. The mammalian disaggregase activity is sensitive to proteinase K digestion and can be uncoupled from proteolysis activity using a protease inhibitor cocktail. Amyloid disaggregation and proteolysis activities are remarkably resistant to changes in temperature and pH. Identification and manipulation of the proteins responsible for the amyloid disaggregation/degradation activities offers the possibility of ameliorating aggregation-associated diseases.
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