Propagation of protein aggregation in neurodegenerative diseases

Jaime Vaquer-Alicea, Marc I. Diamond

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Most common neurodegenerative diseases feature deposition of protein amyloids and degeneration of brain networks. Amyloids are ordered protein assemblies that can act as templates for their own replication through monomer addition. Evidence suggests that this characteristic may underlie the progression of pathology in neurodegenerative diseases. Many different amyloid proteins, including Aβ, tau, and α-synuclein, exhibit properties similar to those of infectious prion protein in experimental systems: discrete and self-replicating amyloid structures, transcellular propagation of aggregation, and transmissible neuropathology. This review discusses the contribution of prion phenomena and transcellular propagation to the progression of pathology in common neurodegenerative diseases such as Alzheimer's and Parkinson's. It reviews fundamental events such as cell entry, amplification, and transcellular movement. It also discusses amyloid strains, which produce distinct patterns of neuropathology and spread through the nervous system. These concepts may impact the development of new diagnostic and therapeutic strategies.

Original languageEnglish (US)
Pages (from-to)785-810
Number of pages26
JournalAnnual Review of Biochemistry
Volume88
DOIs
StatePublished - Jun 20 2019

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Keywords

  • aggregation
  • amyloid
  • prion
  • propagation
  • strain
  • tau

ASJC Scopus subject areas

  • Biochemistry

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