ReviewFrontiers in immunology2014
Molecular Interactions between Complement Factor H and Its Heparin and Heparan Sulfate Ligands.
Review in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 63 citations in OpenAlex.
- Engineering Host-Guest Interactions for Next-Generation Heparin Biosensors.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Interactions of dual antiplatelet and anticoagulant with C1q and FH regulate complement activation by injured cells.Blood vessels, thrombosis & hemostasis · 2026Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Endothelial Glycocalyx: The Missing Link Between Angiogenic Imbalance in Preeclampsia and Systemic Inflammation in HELLP Syndrome.Comprehensive Physiology · 2025Review
- Association between circulatory complement activation and hypertensive renal damage: a case-control study.Renal failure · 2024Article
- Complement factor H in molecular regulation of angiogenesis.Medical review (2021) · 2024Review
- Complement, Coagulation, and Fibrinolysis: The Role of the Endothelium and Its Glycocalyx Layer in Xenotransplantation.Transplant international : official journal of the European Society for Organ Transplantation · 2024Review
- Factor H related proteins modulate complement activation on kidney cells.Kidney international · 2022Article
- The Exploration of Complement-Resistance Mechanisms of Pathogenic Gram-Negative Bacteria to Support the Development of Novel Therapeutics.Pathogens (Basel, Switzerland) · 2022Review
- Review
- Article
- The potential role of complement alternative pathway activation in hypertensive renal damage.Experimental biology and medicine (Maywood, N.J.) · 2022Article
- Complement dysregulation is associated with severe COVID-19 illness.Haematologica · 2022Article
- The Complement System in Metabolic-Associated Kidney Diseases.Frontiers in immunology · 2022Review
- Evidence of a putative glycosaminoglycan binding site on the glycosylated SARS-CoV-2 spike protein N-terminal domain.Computational and structural biotechnology journal · 2021Article
- Use of low-molecular-weight heparin in severe paraquat poisoning: a case report.Journal of medical case reports · 2020Article
- Article
- A genome-wide association study identifies key modulators of complement factor H binding to malondialdehyde-epitopes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Large-scale Identification of N-linked Intact Glycopeptides in Human Serum using HILIC Enrichment and Spectral Library Search.Molecular & cellular proteomics : MCP · 2020Article
- Mechanisms of FH Protection Against Neovascular AMD.Frontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Complement factor H (CFH) is the major regulator of the central complement protein C3b in the alternative pathway of complement activation. A molecular view of the CFH interaction with native heparan sulfate (HS) is central for understanding the mechanism of how surface-bound CFH interacts with C3b bound to host cell surfaces. HS is composed of sulfated heparin-like S-regions that alternate with desulfated NA-regions. Solution structural studies of heparin (equivalent to the S-regions) and desulfated HS (the NA-regions) by scattering and ultracentrifugation showed that each structure was mostly extended and partially bent, but with greater bending and flexibility in the NA-regions compared to the S-regions. Their solution structures have been deposited in the Protein Data Bank. The largest HS oligosaccharides showed more bent and flexible structures than those for heparin. A folded-back domain structure for the solution structure of the 20 domains in CFH was determined likewise. CFH binds to the S-regions but less so to the NA-regions of HS. The bivalent interaction of CFH-heparin was observed by ultracentrifugation, and binding studies of CFH fragments with heparin-coated sensor chips. In common with other CFH interactions with its physiological and pathophysiological ligands, the CFH-heparin and CFH-C3b interactions have moderate micromolar dissociation constants K D, meaning that these complexes do not fully form in vivo. The combination of the solution structures and binding studies indicated a two-site interaction model of CFH with heparin at cell surfaces. By this, the bivalent binding of CFH to a cell surface is co-operative. Defective interactions at either of the two independent CFH-heparin sites reduce the CFH interaction with surface-bound C3b and lead to immune disorders.
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