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From: TSS ()
Subject: Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism
Date: April 27, 2005 at 1:29 pm PST

-------- Original Message --------
Subject: Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism
Date: Wed, 27 Apr 2005 14:05:49 -0500
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@LISTS.UNI-KARLSRUHE.DE


##################### Bovine Spongiform Encephalopathy #####################

Protein fibrils in nature can enhance amyloid protein A amyloidosis in
mice: Cross-seeding as a disease mechanism

Katarzyna Lundmark *, Gunilla T. Westermark {dagger}, Arne Olsén
{ddagger} and Per Westermark §, ¶

*Division of Pathology, Karolinska University Hospital, SE-141 86
Huddinge, Sweden; {dagger}Division of Cell Biology, Linköping
University, SE-581 85 Linköping, Sweden; {ddagger}Department of Clinical
Immunology, Göteborg University, SE-413 46 Göteborg, Sweden; and
§Department of Genetics and Pathology, Uppsala University, SE-751 85
Uppsala, Sweden

Communicated by D. Carleton Gajdusek, Centre National de la Recherche
Scientifique, Gif-sur-Yvette, France, March 4, 2005 (received for review
December 15, 2004)

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.

http://www.pnas.org/cgi/content/abstract/0501814102v1

greetings,

does this article seem to possibly implicate CJD and Alzheimer's
as maybe being the same or very similar?

TSS

############ https://www.lists.uni-karlsruhe.de/warc/bse-l.html ############






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