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Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies.
- Source :
- Amyloid; Dec 2021, Vol. 28 Issue 4, p243-251, 9p
- Publication Year :
- 2021
-
Abstract
- Several studies recently showed that ex vivo fibrils from patient or animal tissue were structurally different from in vitro formed fibrils from the same polypeptide chain. Analysis of serum amyloid A (SAA) and Aβ-derived amyloid fibrils additionally revealed that ex vivo fibrils were more protease stable than in vitro fibrils. These observations gave rise to the proteolytic selection hypothesis that suggested that disease-associated amyloid fibrils were selected inside the body by their ability to resist endogenous clearance mechanisms. We here show, for more than twenty different fibril samples, that ex vivo fibrils are more protease stable than in vitro fibrils. These data support the idea of a proteolytic selection of pathogenic amyloid fibril morphologies and help to explain why only few amino acid sequences lead to amyloid diseases, although many, if not all, polypeptide chains can form amyloid fibrils in vitro. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMYLOID
AMINO acid sequence
IMMUNOGLOBULIN light chains
BLOOD serum analysis
Subjects
Details
- Language :
- English
- ISSN :
- 13506129
- Volume :
- 28
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Amyloid
- Publication Type :
- Academic Journal
- Accession number :
- 154441768
- Full Text :
- https://doi.org/10.1080/13506129.2021.1960501