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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Tabaton, M; Perry, G; Smith, M; Vitek, M; Angelini, G; Dapino, D; Garibaldi, S; Zaccheo, D; Odetti, P

Published Date

  • March 3, 1997

Published In

Volume / Issue

  • 8 / 4

Start / End Page

  • 907 - 909

PubMed ID

  • 9141062

Pubmed Central ID

  • 9141062

International Standard Serial Number (ISSN)

  • 0959-4965

Digital Object Identifier (DOI)

  • 10.1097/00001756-199703030-00018

Language

  • eng

Conference Location

  • England