Cited by 385Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Rapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid

Vigo‐Pelfrey, Carmen, Lee, Doris, Keim, Pam, Lieberburg, Ivan, Schenk, Dale B.·1993·Journal of Neurochemistry

Abstract

Abstract: β‐Amyloid peptide (Aβ) is one of the main components of senile plaques in the brain tissue of Alzheimer's disease (AD) patients. Aβ is proteolytically cleaved from the amyloid precursor protein (APP), an integral membrane protein possessing a large extracellular N‐terminal domain followed by a single membrane‐spanning region and a short cytoplasmic C‐terminal tail. Aβ has been isolated from senile plaques and cerebral vascular tissue of AD brain and characterized as a heterogeneous peptide containing 28–43 amino acids whose sequence begins in the extracellular domain of APP and extends into the putative transmembrane sequence. It has long been speculated that Aβ may also be present in body fluids, such as CSF, that contact neurotic plaques. Recently using a specific enzyme‐linked immunosorbent assay we were able to quantify one form of Aβ in CSF. In this report, using one of these antibodies covalently bound as an affinity matrix, multiple complex forms of Aβ have been isolated and characterized from CSF derived from patients with either meningitis or other neurological disorders. Amino acid sequencing reveals Aβ species with N‐termini of Asp 1, Glu 3, His 6, Glu 11, and Val 12, although on a molar basis, Asp 1 represents the predominant amino‐terminus. Laser desorption mass spectrometry confirmed the presence in CSF of Aβ species containing 27, 28, 30, 34, 35, 40, 42, and 43 amino acids, all beginning at Asp 1; two stable trimmers, (Asp 1‐Met 35).) and (His 6‐Ala 42)3; and one stable dimer containing (Asp 1‐Val 40)2. Some of these fragments have yet to be identified in brain either because they are generated solely in the CSF used in this study or because current procedures used to isolate brain amyloid result in their loss.

Integrity signals

Registry

Crossref · 10.1111/j.1471-4159.1993.tb09841.x

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4 of 4 references verified0 citation errors · 0 not checkable

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  • Aβs ending at Aβ42(43) are a minor component of the Aβ in human cerebrospinal fluid and plasma.

    “These observations indicate that Aps ending at Ap42(43), which are a minor component of the Ap in human cerebrospinal fluid and”

    From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [8]

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Authors
Vigo‐Pelfrey, C., Lee, D., Keim, P., Lieberburg, I., & Schenk, D. B.
Corresponding author
Vigo‐Pelfrey, Carmen
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
1993-11
Volume
61
Issue
5
Pages
1965-1968
ISSN
  • 0022-3042 (ISSN-L)
  • 1471-4159
OpenAlex
W2082504479
Cited by
385
References
4
Citations by year
2026: 2 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 10 · 2021: 5 · 2020: 8 · 2019: 9 · 2018: 7 · 2017: 7 · 2016: 6 · 2015: 12 · 2014: 12 · 2013: 7 · 2012: 18
FWCI
11.11
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Neurochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
beta-amyloid peptide, cerebrospinal fluid, Alzheimer's disease, amyloid precursor protein, amyloid plaques, amyloid oligomers, affinity purification, meningitis
MeSH terms
Adult, Amino Acid Sequence, Antibodies, Monoclonal, Child, Chromatography, Affinity, Humans, Meningitis, Molecular Sequence Data, Molecular Weight, Nervous System Diseases, Peptide Fragments, Peptides, Amyloid beta-Peptides

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