The amino-terminus of the amyloid-beta protein is critical for the cellular binding and consequent activation of the respiratory burst of human macrophages

J Neuroimmunol. 1999 Apr 1;96(1):121-30. doi: 10.1016/s0165-5728(99)00019-3.

Abstract

Here, we show that amyloid-beta (Abeta) is capable to prime and activate the respiratory burst of human macrophages. Previously, the N-terminus of Abeta(1-42) has been shown to contain a cell binding domain that is implicated in eliciting neuropathogenic microglia in vitro. To evaluate the role of this domain in the Abeta(1-42)-induced respiratory burst activity, the effect of Abeta subfragments on the Abeta(1-42)-induced superoxide release were studied. On the basis of the antagonistic properties of Abeta(1-16), it is concluded that the N-terminal region of Abeta is critical for the cellular binding and consequent activation of the respiratory burst of human phagocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / immunology
  • Alzheimer Disease / metabolism
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Peptides / pharmacology*
  • Binding, Competitive / drug effects
  • Binding, Competitive / immunology
  • Brain Chemistry / immunology
  • Flow Cytometry
  • Fluorescein-5-isothiocyanate
  • Fluorescent Dyes
  • Humans
  • Luminescent Measurements
  • Macrophages / chemistry
  • Macrophages / immunology*
  • Macrophages / metabolism*
  • Monocytes / chemistry
  • Monocytes / immunology
  • Monocytes / metabolism
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology*
  • Protein Binding / immunology
  • Respiratory Burst / drug effects
  • Respiratory Burst / immunology*
  • Superoxides / metabolism

Substances

  • Amyloid beta-Peptides
  • Fluorescent Dyes
  • Peptide Fragments
  • amyloid beta-protein (1-11)
  • amyloid beta-protein (1-42)
  • amyloid beta-protein (25-35)
  • Superoxides
  • Fluorescein-5-isothiocyanate