Biochemical evidence for the long-tail form (Aβ1-42/43) of amyloid β protein as a seed molecule in cerebral deposits of alzheimer′s disease

A. Tamaoka*, T. Kondo, A. Odaka, N. Sahara, N. Sawamura, K. Ozawa, N. Suzuki, S. Shoji, H. Mori

*この研究の対応する著者

研究成果: Article査読

106 被引用数 (Scopus)

抄録

We measured the amounts of total Aβ, Aβ1-40, and Aβ1-42/43 in brain tissues using a newly developed ELISA assay and found that the amounts of insoluble Aβ1-42/43 and insoluble Aβ1-40) were linearly related to the amount of Aβ deposits or total insoluble Aβ at their lower and higher concentrations, respectively. In an experiment to characterize the Aβ species in brain homogenates with buffered saline, we unexpectedly detected soluble Aβ which was derived from the insoluble amyloid deposits in brain tissue, indicating reversible depolymerisation of Aβ from insoluble amyloid deposits. To confirm this finding, we performed 5 consecutive washes of insoluble precipitates of AD brains with buffered saline. Both species of Aβ were found in all 5 supernatant fractions and their amounts were gradually decreased. The ratio of Aβ1-42/43/43 to Aβ1-40 was increased with the numbers of washes, indicating that Aβ1-40 existed in an exposed manner as compared to Aβ1-42/43. Thus the present finding is the first biochemical evidence that Aβ1-40 was the predominant species involved in the reversible exchanging reaction on seeding Aβ1-42/43 between the soluble and the insoluble forms (amyloid fibrils).

本文言語English
ページ(範囲)834-842
ページ数9
ジャーナルBiochemical and Biophysical Research Communications
205
1
DOI
出版ステータスPublished - 1994 11 30
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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