alpha-1-antichymotrypsin interaction with A beta (1-40) inhibits fibril formation but does not affect the peptide toxicity

Neurosci Lett. 1996 Jun 14;211(1):45-8. doi: 10.1016/0304-3940(96)12717-8.

Abstract

Recent studies have shown that senile plaque-associated or glial-derived proteins can prevent fibril formation of beta-amyloid peptide (A beta), while increasing the neurotoxicity of the latter (in the case of glutamine synthetase, apolipoprotein J or thrombin). alpha-1-Antichymotrypsin (ACT) is a glial-derived protein associated with senile plaques in the Alzheimer's brain. In this report we show that ACT, a minor protein component of beta-amyloid deposits, is able to inhibit A beta (1-40) aggregation into fibrils, but unable to modulate the toxicity of A beta (1-40) in primary rat hippocampal cell cultures. These results are discussed in terms of the potential role of glial-derived proteins on A beta aggregation and neurotoxicity.

Publication types

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

MeSH terms

  • Amyloid beta-Peptides / pharmacology*
  • Animals
  • Cells, Cultured
  • Hippocampus / cytology
  • Hippocampus / metabolism
  • Neurofibrillary Tangles / pathology*
  • Peptide Fragments / pharmacology*
  • Rats
  • Serine Proteinase Inhibitors / pharmacology*
  • alpha 1-Antichymotrypsin / pharmacology*

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Serine Proteinase Inhibitors
  • alpha 1-Antichymotrypsin
  • amyloid beta-protein (1-40)