Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2005-4-27
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-10214087, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-10402068, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-10439115, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-10448860, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-10958771, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-11823641, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-12011456, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-15063745, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-15111306, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-1677357, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-2649795, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-3553738, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-3611954, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-3997836, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-51405, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-5701154, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-5812749, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-5954971, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-6693836, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-6823091, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-7885228, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-8123028, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-8376413, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-8459772, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-8589090, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-8692856, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-9182769, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-9192614, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-9482925, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-9488380, http://linkedlifedata.com/resource/pubmed/commentcorrection/15829582-9759504
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6098-102
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism.
pubmed:affiliation
Division of Pathology, Karolinska University Hospital, SE-141 86 Huddinge, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't