Cited by 13Alzheimer's disease research and treatmentsComplement system in diseasesPrion Diseases and Protein Misfolding

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

Complement activation by the amyloid proteins Aβ peptide and β2-microglobulin

Abstract

Complement activation (CA) has been reported to play a role in the pathogenesis of Alzheimer's disease (AD). To investigate whether CA may contribute to amyloidogenesis in general, the CA potential of different amyloid fibril proteins was tested. CA induced by A beta preparations containing soluble protein, protofilaments and some fibrils or only fibrils in a solid phase system (ELISA) was modest with a slow kinetics compared to the positive delta IgG control. Soluble A beta induced no detectable CA in a liquid phase system (complement consumption assay) while fibrillar A beta caused CA at 200 mg/ml and higher concentrations. Soluble beta 2-microglobulin (beta 2M) purified from peritoneal dialysates was found to be as potent a complement activator as A beta in both solid and liquid phase systems while beta 2M purified from urine exhibited lower activity, a difference which may be explained by differences observed in SDS-resistant oligomers and isoforms. Soluble Amyloid A-protein caused no significant CA. A beta and beta 2M activated complement via the classical pathway. The modifying influence by amyloid-associated molecules on A beta-induced CA was also investigated, but neither serum amyloid P component nor heparan sulfate did significantly alter the A beta-induced CA. The results indicate that not only fibrillar A beta but also oligomers of, in particular, beta 2M from patients with dialysis-associated amyloidosis are capable of inducing CA at supra-physiological concentrations.

Overview

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Crossref · 10.3109/13506129909007338

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38 of 38 references verified0 citation errors · 0 not checkable

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Citations

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Research works printed but not linked: 4

  1. Coria F, 1988, Lab Invest, 58, 454
  2. Snow A S, 1987, Lab Invest, 56, 120
  3. Dhawan S, 1990, Biochim Biophys Acta, 171, 1284
  4. Björk L, 1984, Acra Pathol Microbiol Immunol Scand, 92, 19

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Metadata

Authors
Nybo, M., Nielsen, E. H., & Svehag, S.-E.
Affiliations
University of Southern Denmark (DK)
Corresponding author
Svehag, Sven-Erik
Venue
Amyloid
Published
1999-01
Volume
6
Issue
4
Pages
265-272
ISSN
  • 1350-6129 (ISSN-L)
  • 1744-2818
OpenAlex
W2043355674
Cited by
13
References
38
Citations by year
2022: 3 · 2017: 2
FWCI
0.95
Type
journal article
Language
en
Open access
closed
Locations
  • Amyloid (publishedVersion)
  • PubMed (publishedVersion)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords
complement activation, amyloid-beta, beta2-microglobulin, Alzheimer's disease, amyloid fibrils, classical complement pathway, dialysis-related amyloidosis, serum amyloid P component, heparan sulfate, amyloid oligomers, amyloidogenesis
MeSH terms
Serum Amyloid P-Component, Serum Amyloid A Protein, Amyloidosis, beta 2-Microglobulin, Complement Activation, Hemolysis, Heparitin Sulfate, Heparan Sulfate, Humans, Kinetics, Microscopy, Electron, Peptide Fragments, Solubility, Spectrometry, Fluorescence, Amyloid beta-Peptides

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