beta-Amyloid Protein Induces Platelet Aggregation and Supports Platelet Adhesion

Biochem Biophys Res Commun. 1994 Dec 30;205(3):1829-35. doi: 10.1006/bbrc.1994.2883.

Abstract

The amyloid precursor protein (APP) is found in many cells including neurons, endothelial cells and blood platelets. Beta-amyloid protein (beta AP) is derived from APP and is deposited in brain and in cerebral microvasculature of individuals with Alzheimer's disease. In this study we demonstrate that beta AP interacts with human blood platelets. We found that human beta AP peptide (1-40) fibrils aggregate platelets and support their adhesion, and these interactions are mediated through platelet membrane integrin receptors.

Publication types

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

MeSH terms

  • Alzheimer Disease / etiology
  • Amino Acid Sequence
  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / pharmacology*
  • Amyloid beta-Peptides / physiology
  • Binding Sites
  • Fibrinogen / metabolism
  • Humans
  • In Vitro Techniques
  • Macromolecular Substances
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology
  • Platelet Adhesiveness / drug effects*
  • Platelet Adhesiveness / physiology
  • Platelet Aggregation / drug effects*
  • Platelet Aggregation / physiology
  • Platelet Membrane Glycoproteins / metabolism
  • Protein Binding
  • Thrombosis / etiology
  • Thrombospondins

Substances

  • Amyloid beta-Peptides
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Oligopeptides
  • Peptide Fragments
  • Platelet Membrane Glycoproteins
  • Thrombospondins
  • amyloid beta-protein (1-28)
  • amyloid beta-protein (1-40)
  • arginyl-glycyl-aspartic acid
  • Fibrinogen