Is amyloid beta-protein glycated in Alzheimer's disease?

Neuroreport. 1997 Mar 3;8(4):907-9. doi: 10.1097/00001756-199703030-00018.

Abstract

Recent data suggest that protein glycation is involved in the process of amyloid formation in Alzheimer's disease (AD). To further investigate this issue, we analyzed the presence of advanced glycation end products (AGE) in soluble and insoluble forms of amyloid beta-protein (A beta) as well as in apolipoprotein E (apoE), a protein bound to amyloid deposits. Both proteins were extracted from cerebral cortex obtained from patients with AD and probed by immunoblotting with two antibodies specific for different AGE, already known to immunocytochemically label amyloid plaques. All the AGE antibodies failed to recognize either A beta or apoE, whereas they reacted with synthetic A beta glycated in vitro. These findings indicate that other proteins associated with amyloid deposits are candidates to be modified with AGE in Alzheimer's cerebral tissue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism*
  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism*
  • Antibodies
  • Brain / metabolism*
  • Brain Chemistry
  • Cerebral Cortex / chemistry
  • Cerebral Cortex / metabolism*
  • Glycation End Products, Advanced / analysis
  • Glycosylation
  • Humans
  • Immunoblotting
  • Lipoproteins, LDL / chemistry
  • Lipoproteins, LDL / metabolism*

Substances

  • Amyloid beta-Peptides
  • Antibodies
  • Glycation End Products, Advanced
  • Lipoproteins, LDL
  • glycosylated lipoproteins, LDL