Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism.
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.
Lundmark
Katarzyna
K
Division of Pathology, Karolinska University Hospital, SE-141 86 Huddinge, Sweden.
Westermark
Gunilla T
GT
Olsén
Arne
A
Westermark
Per
P
D000199:Actins / Q000378:metabolism; D000686:Amyloidosis / Q000473:pathology*; D000818:Animals; D012831:Bombyx; D004926:Escherichia coli; D005260:Female; D007249:Inflammation; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D000685:Serum Amyloid A Protein / Q000378:metabolism*; D012835:Silver Nitrate / Q000494:pharmacology
D000199:Actins; D000685:Serum Amyloid A Protein; D012835:Silver Nitrate