In vivo reversal of amyloid-beta lesions in rat brain

J Neuropathol Exp Neurol. 2000 Jan;59(1):11-7. doi: 10.1093/jnen/59.1.11.

Abstract

Cerebral amyloid-beta (Abeta) deposition is central to the neuropathological definition of Alzheimer disease (AD) with Abeta related toxicity being linked to its beta-sheet conformation and/or aggregation. We show that a beta-sheet breaker peptide (iAbeta5) dose-dependently and reproducibly induced in vivo disassembly of fibrillar amyloid deposits, with control peptides having no effect. The iAbeta5-induced disassembly prevented and/or reversed neuronal shrinkage caused by Abeta and reduced the extent of interleukin-1beta positive microglia-like cells that surround the Abeta deposits. These findings suggest that beta-sheet breakers, such as iAbeta5 or similar peptidomimetic compounds, may be useful for reducing the size and/or number of cerebral amyloid plaques in AD, and subsequently diminishing Abeta-related histopathology.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alzheimer Disease / chemically induced
  • Alzheimer Disease / drug therapy*
  • Alzheimer Disease / pathology*
  • Amygdala / pathology*
  • Amyloid beta-Peptides / pharmacology*
  • Animals
  • Male
  • Microglia / metabolism
  • Neurofibrillary Tangles / chemistry
  • Neurofibrillary Tangles / metabolism
  • Neurofibrillary Tangles / pathology
  • Neurons / metabolism
  • Neurons / pathology
  • Peptide Fragments / pharmacology*
  • Protein Structure, Secondary
  • Rats
  • Rats, Inbred F344
  • Reproducibility of Results
  • Sensitivity and Specificity

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-42)