Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission

Overview

Journal Cold Spring Harb Perspect Med

Specialty General Medicine

Date 2017 Jan 22

PMID 28108533

Citations 17

Authors

Gunilla T Westermark

Marcus Fandrich

Katarzyna Lundmark

Per Westermark

Affiliations

Soon will be listed here.

Abstract

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).

Citing Articles

Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.

Kell D, Pretorius E Int J Mol Sci. 2024; 25(19).

PMID: 39409138 PMC: 11476703. DOI: 10.3390/ijms251910809.

DES-Amyloidoses "Amyloidoses through the looking-glass": A knowledgebase developed for exploring and linking information related to human amyloid-related diseases.

Bajic V, Salhi A, Lakota K, Radovanovic A, Razali R, Zivkovic L PLoS One. 2022; 17(7):e0271737.

PMID: 35877764 PMC: 9312389. DOI: 10.1371/journal.pone.0271737.

High-avidity binding drives nucleation of amyloidogenic transthyretin monomer.

Gao L, Xie X, Liu P, Jin J JCI Insight. 2022; 7(7).

PMID: 35393947 PMC: 9057628. DOI: 10.1172/jci.insight.150131.

Amyloid fibril composition type is consistent over time in patients with Val30Met (p.Val50Met) transthyretin amyloidosis.

Anan I, Suhr O, Liszewska K, Mejia Baranda J, Pilebro B, Wixner J PLoS One. 2022; 17(3):e0266092.

PMID: 35358243 PMC: 8970372. DOI: 10.1371/journal.pone.0266092.

Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.

Lewkowicz E, Gursky O Biophys Chem. 2021; 280:106699.

PMID: 34773861 PMC: 9416430. DOI: 10.1016/j.bpc.2021.106699.

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