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Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission
Department of Medical Cell Biology, Uppsala University, Uppsala, Sweden.
Institute of Protein Biochemistry, Ulm University, Ulm, Germany.
Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Medicine and Health Sciences. Region Östergötland, Center for Diagnostics, Department of Clinical Pathology and Clinical Genetics.
Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden.
2018 (English)In: Cold Spring Harbor Perspectives in Medicine, ISSN 0103-3247, E-ISSN 2157-1422, Vol. 8, no 1, article id a024323Article, review/survey (Refereed) Published
Abstract [en]

More than 30 proteins form amyloid in humans, most of them outside of the brain. Deposition of amyloid in extracerebral tissues is very common and seems inevitable for an aging person. Most deposits are localized, small, and probably without consequence, but in some instances, they are associated with diseases such as type 2 diabetes. Other extracerebral amyloidoses are systemic, with life-threatening effects on the heart, kidneys, and other organs. Here, we review how amyloid may spread through seeding and whether transmission of amyloid diseases may occur between humans. We also discuss whether cross-seeding is important in the development of amyloidosis, focusing specifically on the amyloid proteins AA, transthyretin, and islet amyloid polypeptide (IAPP).

Place, publisher, year, edition, pages
Cold Spring Harbor Laboratory Press (CSHL), 2018. Vol. 8, no 1, article id a024323
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-134871DOI: 10.1101/cshperspect.a024323ISI: 000429143200001PubMedID: 28108533Scopus ID: 2-s2.0-85039992624OAI: oai:DiVA.org:liu-134871DiVA, id: diva2:1077540
Available from: 2017-02-28 Created: 2017-02-28 Last updated: 2018-05-16Bibliographically approved

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Lundmark, Katarzyna
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CiteExportLink to record
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