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Cross-seeding of wild-type and hereditary variant-type amyloid beta-proteins in the presence of gangliosides.

Abstract：

:We investigated the molecular mechanism underlying the ganglioside-induced initiation of the assembly of wild and hereditary variant-type amyloid beta-proteins, including Arctic-, Dutch-, and Flemish-type amyloid beta-proteins. We monitored the assembly of amyloid beta-protein by thioflavin-T assay, western blotting and electron microscopy. We also examined how externally added amyloid beta-protein assembles in a cell culture. The assembly of wild-, Arctic-, Dutch-, and Flemish-type amyloid beta-proteins were accelerated in the presence of GM1, GM1, GM3 and GD3 gangliosides. Notably, all of these amyloid beta-proteins accelerated the assembly of different type of amyloid beta-protein, following prior binding to a specific ganglioside. A specific-ganglioside-bound form of variant-type amyloid beta-protein was recognized by the antibody (4396C) specific to the GM1-ganglioside-induced altered conformation of wild-type amyloid beta-protein. Moreover, the assembly of these amyloid beta-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 beta-proteins despite differences in their amino acid sequences.

journal_name

J Neurochem

journal_title

Journal of neurochemistry

authors

Yamamoto N,Matsuzaki K,Yanagisawa K

doi

10.1111/j.1471-4159.2005.03444.x

keywords:

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

1167-76

issue

4

eissn

0022-3042

issn

1471-4159

pii

JNC3444

journal_volume

95

pub_type

杂志文章

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