AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
| Autor: | Bansal, Akanksha, Schmidt, Matthias, Rennegarbe, Matthies, Haupt, Christian, Liberta, Falk, Stecher, Sabrina, Puscalau-Girtu, Ioana, Biedermann, Alexander, Fändrich, Marcus |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Elektronenmikroskopie Amyloid Serum Amyloid A Protein Cryoelectronics Science Cryoelectron Microscopy Amyloidosis macromolecular substances Article Recombinant Proteins Mice Protein Aggregates DDC 570 / Life sciences ddc:570 mental disorders Animals Protein Conformation beta-Strand Protein aggregation |
| Zdroj: | Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021) Nature Communications |
| Popis: | Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher ��-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue. https://doi.org/10.1038/s41467-021-21129-z OPEN 1 publishedVersion |
| Databáze: | OpenAIRE |
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