ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
We investigated the molecular mechanism underlying the ganglioside-induced initiation of the assembly of wild and hereditary variant-type amyloid β-proteins, including Arctic-, Dutch-, and Flemish-type amyloid β-proteins. We monitored the assembly of amyloid β-protein by thioflavin-T assay, western blotting and electron microscopy. We also examined how externally added amyloid β-protein assembles in a cell culture. The assembly of wild-, Arctic-, Dutch-, and Flemish-type amyloid β-proteins were accelerated in the presence of GM1, GM1, GM3 and GD3 gangliosides. Notably, all of these amyloid β-proteins accelerated the assembly of different type of amyloid β-protein, following prior binding to a specific ganglioside. A specific-ganglioside-bound form of variant-type amyloid β-protein was recognized by the antibody (4396C) specific to the GM1-ganglioside-induced altered conformation of wild-type amyloid β-protein. Moreover, the assembly of these amyloid β-proteins in the presence of a specific ganglioside was markedly suppressed by coincubation with 4396C. This study suggests that cross-seeding can occur between wild and hereditary variant-type amyloid β-proteins despite differences in their amino acid sequences.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.2005.03444.x
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