Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins

Craig S. Atwood*, Ralph N. Martins, Mark A. Smith, George Perry

*Corresponding author for this work

Research output: Contribution to journalArticle

104 Citations (Scopus)

Abstract

Amyloid deposits are primarily composed of the amyloid-β protein, although other proteins (and metal ions) also have been colocalized to these lesions. The pattern of oxidative modifications in amyloid plaques is very different to that associated with neurofibrillary tangles and neuronal cell bodies, likely reflecting the different composition of these structures, accessibility of oxidants, the generation of oxidants in and around these structures and the intrinsic antioxidant defense systems to protect these structures. Future studies directed at understanding Aβ interactions with other amyloid components, the role of oxidative modifications in stabilizing amyloid deposits and the determination of protease cleavage sites on Aβ may provide mechanistic insights regarding both amyloid formation and removal.

Original languageEnglish
Pages (from-to)1343-1350
Number of pages8
JournalPeptides
Volume23
Issue number7
DOIs
Publication statusPublished - 2002
Externally publishedYes

Keywords

  • Alzheimer disease
  • Amyloid
  • Composition
  • Down syndrome
  • Inflammation
  • Metal ions
  • Microglial activation
  • Oxidants
  • Oxidative stress
  • Posttranslational modification
  • Protein crosslinks

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