2005/04/13 by Katarzyna Lundmark, Gunilla T. Westermark, Arne Olsén +1 · 3 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Chemistry · #Prion Diseases and Protein Misfolding #Amyloidosis: Diagnosis, Treatment, Outcomes #Alzheimer's disease research and treatments #Fibril #Amyloidosis #Amyloid (mycology) #Amyloid disease #Chemistry #Amyloid fibril #In vitro #Biochemistry #AA amyloidosis #Biophysics #Biology #Pathology #Medicine #Amyloid β #Disease
paper · doi:10.1073/pnas.0501814102
openalex publication_date 2005/04/13 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26
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 beta-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.