Further evidence of local ganglioside-dependent amyloid beta-protein assembly in brain

Neuroreport. 2006 Nov 6;17(16):1735-7. doi: 10.1097/01.wnr.0000239958.53072.14.

Abstract

We investigated the molecular mechanism underlying the region-specific deposition of amyloid beta-protein in brains affected with Alzheimer's disease or cerebral amyloid angiopathy. Here, we show that a hereditary variant-type ('Iowa') amyloid beta-protein, which predominantly deposits in the cerebral vessel wall similar to Dutch and Italian-type amyloid beta-proteins, preferably assembles in the presence of GM3 ganglioside. On the basis of our previous findings that first, cerebrovascular smooth muscle cells that provide favorable sites for these variant-type amyloid beta-proteins exclusively express GM3 ganglioside, and second, Dutch and Italian-type amyloid beta-proteins also require GM3 ganglioside for their assembly, our results provide further evidence that local gangliosides play a crucial role in the region-specific amyloid beta-protein deposition in the brain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism
  • Benzothiazoles
  • Brain / metabolism
  • Gangliosides / chemistry*
  • Humans
  • Indicators and Reagents
  • Microscopy, Electron
  • Mutation
  • Solutions
  • Thiazoles / chemistry

Substances

  • Amyloid beta-Peptides
  • Benzothiazoles
  • Gangliosides
  • Indicators and Reagents
  • Solutions
  • Thiazoles
  • thioflavin T