Cited by 339Alzheimer's disease research and treatmentsComplement system in diseasesNeuroinflammation and Neurodegeneration Mechanisms

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beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain.

Jiang, H, Burdick, D, Glabe, C G, Cotman, C W, Tenner, A J·1994·The Journal of Immunology

DOI 10.4049/jimmunol.152.10.5050

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Abstract

beta-amyloid peptides that accumulate within the brain of individuals with Alzheimer's disease bind to C1q and activate the classical C pathway via a specific interaction with a site within the collagen-like domain of C1q (C1q-CLF). Synthetic analogues of beta-amyloid peptides, beta 1-42 and beta 1-40, bound to C1q and were strong activators of C as assessed by both total C consumption and C4 consumption. beta 1-42 was significantly more effective than beta 1-40 in binding to C1q and triggering C activation, whereas beta 1-28 demonstrated little or no binding or C activation. This C-activating capacity seems to be largely correlated with the assembly of the beta 1-42 into low speed sedimentable aggregates and/or macromolecular fibrils. Radiolabeled C1q and C1q-CLF bind specifically to these aggregates or amyloid fibrils. In addition, using synthetic C1q peptides in a solid phase binding assay, the major binding site of beta 1-42 to C1q was localized to the C1q A chain collagen-like residues 14-26, a region previously described as a novel interaction site for Ab-independent activators of C1. C1q A chain peptide 14-26 blocked the ability of beta-amyloid peptides to activate the classical C pathway, providing evidence that this relatively unrecognized mechanism of C activation (via binding to the C1q-CLF) may have crucial physiologic consequences. Finally, these observations provide further support for the hypothesis that C activation and inflammation may be a component in the pathogenesis of AD and suggest possibilities for modulating the progression of AD.

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Authors: Jiang, H., Burdick, D., Glabe, C. G., Cotman, C. W., & Tenner, A. J.
Affiliations: University of California, Irvine (US)
ORCID: Jiang, H
Glabe, C G
Cotman, C W
Tenner, A J
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 1994-05
Volume: 152
Issue: 10
Pages: 5050-5059
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.152.10.5050
OpenAlex: W1549447146
Cited by: 330
References: 0
Citations by year: 2026: 3 · 2025: 8 · 2024: 9 · 2023: 9 · 2022: 6 · 2021: 4 · 2020: 13 · 2019: 11 · 2018: 4 · 2017: 8 · 2016: 6 · 2015: 4 · 2014: 8 · 2013: 5 · 2012: 9
FWCI: 10.41
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (5T32 CA 09054, T32CA009054)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, C1q, classical complement pathway, complement activation, collagen-like domain, amyloid fibrils, Alzheimer's disease
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Binding Sites, Collagen, Complement Activation, Humans, Molecular Sequence Data, Complement C1q, Amyloid beta-Peptides

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beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain.

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