Ultrafiltrate of blood plasma modulates amyloid-β aggregation

J Alzheimers Dis. 2011;23(1):1-5. doi: 10.3233/JAD-2010-101137.

Abstract

Several neurodegenerative diseases, including Alzheimer's disease (AD), have etiology connected to abnormal protein self association. Copper-induced striking differences in amyloid-β40 aggregation, distinct from spontaneous self association, prompted us to study whether amyloid-β40 aggregation could be applied to differentiate between platelet poor plasma ultrafiltrates obtained from AD and control samples. We report, based on 20 AD and 18 age-matched controls, a significant difference in the concentration of short fibers induced by ultrafiltrated plasma from AD compared to control samples. The observed effect was independent of copper and other EDTA chelatable ions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Alzheimer Disease / blood*
  • Amyloid beta-Peptides / blood*
  • Case-Control Studies
  • Copper / metabolism
  • Female
  • Humans
  • Male
  • Peptide Fragments / blood*
  • Plasma / metabolism*
  • Spectrophotometry, Atomic / methods

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • Copper