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, Naoya Sawamura, K. Ozawa, N. Suzuki, S. Shoji, H. Mori

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

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).

Original languageEnglish
Pages (from-to)834-842
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume205
Issue number1
DOIs
Publication statusPublished - 1994 Nov 30
Externally publishedYes

Fingerprint

Amyloidogenic Proteins
Seed
Brain
Seeds
Alzheimer Disease
Deposits
Amyloid
Molecules
Amyloid Plaques
Tissue
Depolymerization
Precipitates
Assays
Enzyme-Linked Immunosorbent Assay
Experiments

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

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

In: Biochemical and Biophysical Research Communications, Vol. 205, No. 1, 30.11.1994, p. 834-842.

Research output: Contribution to journalArticle

Tamaoka, A. ; Kondo, T. ; Odaka, A. ; Sahara, N. ; Sawamura, Naoya ; Ozawa, K. ; Suzuki, N. ; Shoji, S. ; Mori, H. / 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. In: Biochemical and Biophysical Research Communications. 1994 ; Vol. 205, No. 1. pp. 834-842.
@article{35c5770d1f134f979fae774892690641,
title = "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",
abstract = "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).",
author = "A. Tamaoka and T. Kondo and A. Odaka and N. Sahara and Naoya Sawamura and K. Ozawa and N. Suzuki and S. Shoji and H. Mori",
year = "1994",
month = "11",
day = "30",
doi = "10.1006/bbrc.1994.2740",
language = "English",
volume = "205",
pages = "834--842",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - 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

AU - Tamaoka, A.

AU - Kondo, T.

AU - Odaka, A.

AU - Sahara, N.

AU - Sawamura, Naoya

AU - Ozawa, K.

AU - Suzuki, N.

AU - Shoji, S.

AU - Mori, H.

PY - 1994/11/30

Y1 - 1994/11/30

N2 - 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).

AB - 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).

UR - http://www.scopus.com/inward/record.url?scp=0028096692&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028096692&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1994.2740

DO - 10.1006/bbrc.1994.2740

M3 - Article

C2 - 7999120

AN - SCOPUS:0028096692

VL - 205

SP - 834

EP - 842

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -