Abstract
Secondary, or amyloid protein A (AA), amyloidosis is a complication of chronic inflammatory diseases, both infectious and noninfectious. AA constitutes the insoluble fibrils, which are deposited in different organs, and is a major N-terminal part of the acute phase protein serum AA. It is not known why only some patients with chronic inflammation develop AA amyloidosis. Nucleation is a widely accepted mechanism in amyloidogenesis. Preformed amyloid-like fibrils act as nuclei in amyloid fibril formation in vitro , and AA amyloid fibrils and synthetic amyloid-like fibrils also may serve as seed for fibril formation in vivo . In addition to amyloid fibrils, there is a variety of similar nonmammalian protein fibrils with β-pleated structure in nature. We studied three such naturally occurring protein fibrils: silk from Bombyx mori , Sup35 from Saccharomyces cerevisiae , and curli from Escherichia coli . Our results show that these protein fibrils exert amyloid-accelerating properties in the murine experimental AA amyloidosis, suggesting that such environment factors may be important risk factors in amyloidogenesis.
Keywords
FibrilAmyloidosisAmyloid (mycology)Amyloid diseaseChemistryAmyloid fibrilIn vitroBiochemistryAA amyloidosisBiophysicsBiologyPathologyMedicineAmyloid βDisease
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Publication Info
- Year
- 2005
- Type
- article
- Volume
- 102
- Issue
- 17
- Pages
- 6098-6102
- Citations
- 302
- Access
- Closed
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Cite This
Katarzyna Lundmark,
Gunilla T. Westermark,
Arne Olsén
et al.
(2005).
Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism.
Proceedings of the National Academy of Sciences
, 102
(17)
, 6098-6102.
https://doi.org/10.1073/pnas.0501814102
Identifiers
- DOI
- 10.1073/pnas.0501814102