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

Cold Spring Harb Perspect Med. 2018 Jan 2;8(1):a024323. doi: 10.1101/cshperspect.a024323.

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).

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloidosis / etiology*
  • Amyloidosis / metabolism
  • Amyloidosis / pathology
  • Animals
  • Humans
  • Islet Amyloid Polypeptide / metabolism*
  • Islets of Langerhans / metabolism
  • Islets of Langerhans / pathology
  • Liver / pathology
  • Plaque, Amyloid / metabolism
  • Prealbumin / metabolism*
  • Protein Folding
  • Serum Amyloid A Protein / metabolism*

Substances

  • Islet Amyloid Polypeptide
  • Prealbumin
  • Serum Amyloid A Protein