Human anti-beta-amyloid antibodies block beta-amyloid fibril formation and prevent beta-amyloid-induced neurotoxicity

Brain. 2003 Sep;126(Pt 9):1935-9. doi: 10.1093/brain/awg191. Epub 2003 Jun 23.

Abstract

The accumulation of beta-amyloid (A beta) in neuritic plaques is thought to be causative for the progression of Alzheimer's disease (AD). Recently, both active immunization and passive administration of A beta antibodies dramatically attenuated amyloid plaque deposition, neuritic dystrophy, astrogliosis and behaviour deficits in transgenic animals. In addition, we and others have found that titres of naturally occurring anti-A beta antibodies in the CSF of AD patients are significantly lower than those in age-matched controls. Treatment with intravenous immunoglobulins (a preparation that contained anti-A beta antibodies) significantly lowered CSF levels of A beta in non-demented patients. In this study, anti-A beta antibodies were isolated from immunoglobulin preparations and these anti-A beta antibodies strongly block fibril formation or disrupt formation of fibrilar structures. Furthermore, these antibodies almost completely prevented neurotoxicity of A beta. In contrast, immunoglobulins depleted of anti-A beta antibodies had little effect on A beta fibril formation or protection of neuronal cells. This study supports the findings that human anti-A beta antibodies may interfere with the pathogenesis of AD by more than one mechanism, and administration of polyclonal human anti-A beta antibodies isolated from plasma is a potential therapeutic agent to prevent or slow down disease progression.

MeSH terms

  • Amyloid beta-Peptides / immunology*
  • Amyloid beta-Peptides / toxicity
  • Animals
  • Cell Survival
  • Cells, Cultured
  • Enzyme-Linked Immunosorbent Assay / methods
  • Hippocampus / pathology
  • Humans
  • Immunoglobulin G / immunology
  • Neurons / pathology
  • Plaque, Amyloid / metabolism
  • Plaque, Amyloid / pathology*
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Amyloid beta-Peptides
  • Immunoglobulin G