CoChat
Sign Up
Cited by 510Alzheimer's disease research and treatmentsMass Spectrometry Techniques and ApplicationsDementia and Cognitive Impairment Research

Peptide Compositions of the Cerebrovascular and Senile Plaque Core Amyloid Deposits of Alzheimer′s Disease

Miller, D.L., Papayannopoulos, I.A., Styles, J., Bobin, S.A., Lin, Y.Y., Biemann, K., Iqbal, K.·1993·Archives of Biochemistry and Biophysics
DOI 10.1006/abbi.1993.1112
Open this paper in CoChat — free account

Abstract

The pathological findings of Alzheimer's disease include amyloid deposition in cerebral blood vessels and in senile plaques. Both deposits are known to include peptides that contain a common sequence. Both forms of amyloid were isolated and their peptide compositions were determined. The peptides were resolved by size-exclusion chromatography in 70% formic acid, and reverse-phase chromatography in 60% formic acid, 0-40% acetonitrile. Senile plaque amyloid cores contain about 25% protein, about 70% of which is composed of peptides containing the beta-amyloid sequence. Amino-terminal sequencing of the core amyloid peptides (CAPs) revealed extensive amino-terminal heterogeneity, with variable amounts of blocked amino termini. Matrix-assisted, laser-desorption-time-of-flight mass spectrometry of the CAP mixture revealed an array of peptides the molecular weights of which corresponded to peptides beginning with each of the first 11 amino acids of the beta-peptide sequence and ending with Ala-42 of that sequence. The carboxyl-terminal residues were identified by tandem mass spectrometry of chymotrypsin digests. CAP possessed a minor degree of carboxyl-terminal heterogeneity. Cerebrovascular amyloid peptides (CVAPs) possessed minor degrees of both amino- and carboxyl-terminal heterogeneity. The major CVAP commenced at Asp-1 and ended at Val-40. Minor components of CAP possessed masses of 8000-9000 Da and the same amino-terminal residues as the major components of CAP. They may be pr…

Integrity signals

Registry

Crossref · 10.1006/abbi.1993.1112

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • This finding is consistent with previous reports that most of the Aβ in AD brains is amino-terminally truncated or modified.

    “Th is finding is consistent with pr evious re ports (15,17,18) that most of the A{3 in AD brains is amino-ter mi na lly trunca te d or modifi ed.”

    From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [17]

  • The increased amount of Aβ detected with 4G8 suggests that there may be considerable amino-terminally truncated Aβ in AD brain.

    “The increased amount of A{3 detected with 4G8 suggests that there may be considerable amino-terminally truncated A{3 in AD brain, consistent with the results of others who have examined the SDSinsoluble A{3 in AD brain (1S, 17,18).”

    From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [17]

  • SDS-insoluble amyloid in senile plaque cores is primarily Aβ1-42.

    “Recent reports using this approach, particularly those of Roher and his colleagues, indicate that the SDS-insoluble amyloid in senile plaque cores is primarily A(31-42 (15,17)”

    From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [17]

Cited by

Sorted by citations

Authors
Miller, D. L., Papayannopoulos, I. A., Styles, J., Bobin, S. A., Lin, Y. Y., Biemann, K., & Iqbal, K.
ORCID
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
1993-02
Volume
301
Issue
1
Pages
41-52
ISSN
0003-9861 (ISSN-L)
DOI
10.1006/abbi.1993.1112
OpenAlex
W2067811915
Cited by
510
References
0
Citations by year
2026: 10 · 2025: 13 · 2024: 22 · 2023: 25 · 2022: 16 · 2021: 13 · 2020: 17 · 2019: 15 · 2018: 20 · 2017: 15 · 2016: 12 · 2015: 12 · 2014: 16 · 2013: 14 · 2012: 14
FWCI
15.77
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (1r01ns025231-01, 5r01ag005892-16, 5p01ag004220-12)
  • National Institute on Aging (AG04220, AG-05892)
  • National Institute of Neurological Disorders and Stroke (NS25231)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
Alzheimer's disease, amyloid deposits, amyloid plaques, cerebrovascular amyloid, beta-amyloid peptide, peptide composition, proteolytic processing
MeSH terms
Alzheimer Disease, Amino Acid Sequence, Amino Acids, Amyloid, Capillaries, Cerebral Cortex, Chromatography, High Pressure Liquid, Chymotrypsin, Humans, Molecular Sequence Data, Peptide Fragments, Peptides, Mass Spectrometry, Spectrometry, Mass, Fast Atom Bombardment, Neurofibrillary Tangles

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review