The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
In vitro demonstration of a particular affinity of glomerular basement membrane and collagen for DNA. A possible basis for a local formation of DNA-anti-DNA complexes in systemic lupus erythematosus.
Open accessAbstract
In vitro, collagen and collagen-like material in GBM, were demonstrated to have a particular high affinity for any DNA tested (mammalian, bacterial, viral, and plant). GBM fixed DNA 40-80 times more than HGG and BSA and 10-40 times more than bacterial LPS. GBM has a higher affinity for SSDNA than for DSDNA. This binding was inhibited at low pH, low ionic strength, and in the presence of anionic detergents, indicating that the highly negatively charged DNA may interact with the basic site on collagen or GBM by electrostatic forces. This interaction was competitively interfered with by DNA-binding proteins such as Clq. Complexes formed of DNA and anti-DNA antibodies did not exhibit the same binding property as free DNA. However, DNA which was already bound to GBM or to collagen could very efficiently bind anti-DNA antibodies and form immune complexes which would remain on these structures. The biological significance of the binding of DNA to GBM or to collagen should be particularly considered in relation to the pathogenesis of SLE. It is possible that DNA released from disrupted or degenerating cells would bind to surrounding collagen fibers or to basement membranes and then act as an immunoabsorbant for circulating anti-DNA antibodies. Some evidence for an in vivo binding of SSDNA to renal structures was obtained in mice treated with bacterial LPS 2 days before the injection of SSDNA.
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“However, DNA is a stable polymer with a negative charge that has affinity for positively charged molecules such as side chains of collagen fibrils [180].”
From Immune Response to Extracellular Matrix Bioscaffolds: A Comprehensive Review (2025) · cites this paper as [180]
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Metadata
- Authors
- Izui, S., Lambert, P. H., & Miescher, P. A.
- Affiliations
- World Health Organization (CH)
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1976-08-01
- Volume
- 144
- Issue
- 2
- Pages
- 428-443
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2190380
- OpenAlex
- W2085459553
- Cited by
- 313
- References
- 43
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2021: 1 · 2020: 2 · 2019: 2 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 2
- FWCI
- 19.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion)
- Funders
- World Health Organization
- National Research Foundation
- Topics
- Health Sciences › Medicine › Rheumatology › Systemic Lupus Erythematosus Research
- Health Sciences › Medicine › Nephrology › Renal Diseases and Glomerulopathies
- Health Sciences › Medicine › Rheumatology › Vasculitis and related conditions
- Keywords
- glomerular basement membrane, collagen, DNA binding, anti-DNA antibodies, immune complexes, systemic lupus erythematosus, single-stranded DNA, electrostatic binding, C1q, lipopolysaccharide, lupus pathogenesis
- MeSH terms
- Animals, Antigen-Antibody Complex, Basement Membrane, Binding Sites, Collagen, Complement C1, DNA, DNA, Single-Stranded, Humans, Hydrogen-Ion Concentration, Kidney Glomerulus, Lupus Erythematosus, Systemic, Osmolar Concentration, Protein Binding, Solubility, Temperature, Mice
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