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Seeding and Cross-seeding in Amyloid Diseases

  • Per WestermarkEmail author
  • Gunilla T. Westermark
Chapter
Part of the Research and Perspectives in Alzheimer's Disease book series (ALZHEIMER)

Abstract

Seeding is a key phenomenon in all forms of amyloid and is most likely the mechanism by which amyloid deposits spread in a tissue and, in the case of systemic amyloidosis, from one organ to another. In experimental models of amyloid A (AA) amyloidosis, in which the fibril protein is derived from the acute phase reactant protein serum amyloid A (SAA), the disease can be transmitted from an amyloidotic animal to a susceptible recipient by a prion-like mechanism, and the transmitting agent has been identified as the amyloid fibril itself. AA amyloid fibrils from other species can also transfer the disease to mice, but with varying efficacy. In amyloid fibrils are protein monomers aggregated in a cross β-sheet conformation, and the molecular organization of amyloid fibrils is principally the same irrespective of biochemical type. However, fibril formation is specific, with subtle interactions between the β-strands making seeding specific, and even small amino acid sequence differences can block propagation. Nevertheless, cross-seeding does occur in vitro, and we have shown that fibrils of diverse nature, both natural and synthetic, can accelerate development of experimental AA amyloidosis. AA amyloidosis is common in many mammalian and avian species and can be present in the human food chain; such material can transfer amyloidosis experimentally to mice. Consequently, there are in our environment a number of components that may have the ability to induce amyloidosis in susceptible humans. It remains to be shown whether such mechanisms are limited to AA amyloidosis or can also operate in other protein aggregation disorders.

Keywords

Amyloid Deposit Amyloid Fibril Systemic Amyloidosis Islet Amyloid Polypeptide ATTR Amyloidosis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

Supported by the Swedish Research Council, the Swedish Diabetes Association and FAMY, FAMY Norrbotten and Amyl.

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Authors and Affiliations

  1. 1.Department of Immunology, Genetics and PathologyUppsala UniversityUppsalaSweden
  2. 2.Department of Medical Cell BiologyUppsala UniversityUppsalaSweden

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