ArticleThe American journal of pathology2007
Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils.
Article in The American journal of pathology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 52 citations in OpenAlex.
- AA amyloid in human food chain is a possible biohazard.Scientific reports · 2021Article
- Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases.Nature neuroscience · 2018Review
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Amyloidosis-inducing activity of blood cells in mouse AApoAII amyloidosis.Experimental animals · 2018Article
- Apolipoprotein A-II induces acute-phase response associated AA amyloidosis in mice through conformational changes of plasma lipoprotein structure.Scientific reports · 2018Article
- Molecular interaction between type 2 diabetes and Alzheimer's disease through cross-seeding of protein misfolding.Molecular psychiatry · 2017Article
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
- The amyloid interactome: Exploring protein aggregation.PloS one · 2017Article
- Article
- C-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Extracellular environment modulates the formation and propagation of particular amyloid structures.Molecular microbiology · 2014Article
- Review
- Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases.PLoS pathogens · 2013Review
- Review
- Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease.PLoS pathogens · 2011Article
- Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy.The American journal of pathology · 2010Article
- Animal models of human amyloidoses: are transgenic mice worth the time and trouble?FEBS letters · 2009Review
- Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification.FEBS letters · 2009Review
- Conformational switching within individual amyloid fibrils.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Murine senile [apolipoprotein A-II amyloid (AApoAII)] and reactive [protein A amyloid (AA)] amyloidosis are reported to be transmissible diseases via a seeding mechanism similar to that observed in the prion-associated disorders, although de novo amyloidogenesis and the progression of AApoAII or AA amyloidosis remain unclear. We examined the effect of co-injection of AApoAII and AA fibrils and multiple inflammatory stimuli in R1.P1-Apoa2(c) mice with the amyloidogenic Apoa2(c) allele. Both AApoAII and AA amyloidosis could be induced in this system, but the two types of amyloid fibrils preferentially promote the formation of the same type of fibrils while inhibiting the formation of the other. Furthermore, we demonstrate that AA or AApoAII amyloidosis could be cross-seeded by predeposited AApoAII or AA fibrils and that the predeposited amyloid fibrils were degraded when the fibril formation was reduced or stopped. In addition, a large proportion of the two amyloid fibrils colocalized during the formation of new fibrils in the spleen and liver. Thus, we propose that AApoAII and AA can both cross-seed and cross-compete with regard to amyloid formation, depending on the stage of amyloidogenesis. These results will aid in the clarification of the mechanisms of pathogenesis and progression of amyloid disorders.
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