Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies
العنوان: | Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies |
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المؤلفون: | Bouke P. C. Hazenberg, Stefan Schoenland, Bernd Reif, Tejaswini Pradhan, Christian Haupt, M. Faendrich, J. Schoenfelder, Johan Bijzet, Ute Hegenbart, P. B. Pfeiffer |
المساهمون: | Translational Immunology Groningen (TRIGR) |
المصدر: | Amyloid, 28(4), 243-251. Taylor & Francis Ltd |
بيانات النشر: | Taylor & Francis Ltd, 2021. |
سنة النشر: | 2021 |
مصطلحات موضوعية: | PROTEINS, medicine.medical_treatment, proteolytic stability, macromolecular substances, Fibril, prion, Amyloid disease, Internal Medicine, medicine, Serum amyloid A, protein misfolding, immunoglobulin light chain, GLYCOSAMINOGLYCANS, chemistry.chemical_classification, Protease, biology, Chemistry, serum amyloid A, Amyloid fibril, TRANSTHYRETIN, In vitro, POLYMORPHISM, Amino acid, Transthyretin, Amyloid structure, biology.protein, Biophysics, Protein folding, Ex vivo |
الوصف: | Several studies recently showed that ex vivo fibrils from patient or animal tissue were structurally different from in vitro formed fibrils from the same polypeptide chain. Analysis of serum amyloid A (SAA) and Aβ-derived amyloid fibrils additionally revealed that ex vivo fibrils were more protease stable than in vitro fibrils. These observations gave rise to the proteolytic selection hypothesis that suggested that disease-associated amyloid fibrils were selected inside the body by their ability to resist endogenous clearance mechanisms. We here show, for more than twenty different fibril samples, that ex vivo fibrils are more protease stable than in vitro fibrils. These data support the idea of a proteolytic selection of pathogenic amyloid fibril morphologies and help to explain why only few amino acid sequences lead to amyloid diseases, although many, if not all, polypeptide chains can form amyloid fibrils in vitro. |
وصف الملف: | application/pdf |
اللغة: | English |
تدمد: | 1744-2818 1350-6129 |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e229dee1268b3cc10a97beb6344d5b95Test https://doi.org/10.1080/13506129.2021.1960501Test |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....e229dee1268b3cc10a97beb6344d5b95 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 17442818 13506129 |
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