ArticleThe Journal of biological chemistry2008
Complement factor H binds to denatured rather than to native pentameric C-reactive protein.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.
- Complement factor H genetic variant and age-related macular degeneration: effect size, modifiers and relationship to disease subtype.International journal of epidemiology · 2012Pooled it
- C-reactive protein dissociation drives choroidal neovascularization in age-related macular degeneration.Scientific reports · 2025Article
- The Complement System as a Part of Immunometabolic Post-Exercise Response in Adipose and Muscle Tissue.International journal of molecular sciences · 2024Review
- Complement factor H in molecular regulation of angiogenesis.Medical review (2021) · 2024Review
- Early detection of cardiovascular risk markers through non-invasive ultrasound methodologies in periodontitis patients.Open medicine (Warsaw, Poland) · 2024Review
- Natural Flavonoids Derived From Fruits Are Potential Agents Against Atherosclerosis.Frontiers in nutrition · 2022Review
- Interlink between Inflammation and Oxidative Stress in Age-Related Macular Degeneration: Role of Complement Factor H.Biomedicines · 2021Review
- Interaction of the Factor H Family Proteins FHR-1 and FHR-5 With DNA and Dead Cells: Implications for the Regulation of Complement Activation and Opsonization.Frontiers in immunology · 2020Article
- Regulation of the Complement System by Pentraxins.Frontiers in immunology · 2019Review
- Structure-Function Relationships of C-Reactive Protein in Bacterial Infection.Frontiers in immunology · 2019Review
- Review
- C-reactive protein and pentraxin-3 binding of factor H-like protein 1 differs from complement factor H: implications for retinal inflammation.Scientific reports · 2018Article
- C-Reactive Protein as a Therapeutic Target in Age-Related Macular Degeneration.Frontiers in immunology · 2018Review
- Complement factor H in AMD: Bridging genetic associations and pathobiology.Progress in retinal and eye research · 2018Review
- Pentraxins in Complement Activation and Regulation.Frontiers in immunology · 2018Review
- Self-Damage Caused by Dysregulation of the Complement Alternative Pathway: Relevance of the Factor H Protein Family.Frontiers in immunology · 2018Review
- C-Reactive Protein in Atherothrombosis and Angiogenesis.Frontiers in immunology · 2018Review
- Functional Transformation of C-reactive Protein by Hydrogen Peroxide.The Journal of biological chemistry · 2017Article
- Protection of host cells by complement regulators.Immunological reviews · 2016Review
- Complement factor H binding of monomeric C-reactive protein downregulates proinflammatory activity and is impaired with at risk polymorphic CFH variants.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Binding of the complement regulatory protein, factor H, to C-reactive protein has been reported and implicated as the biological basis for association of the H402 polymorphic variant of factor H with macular degeneration. Published studies utilize solid-phase or fluid-phase binding assays to show that the factor H Y402 variant binds C-reactive protein more strongly than H402. Diminished binding of H402 variant to C-reactive protein in retinal drusen is posited to permit increased complement activation, driving inflammation and pathology. We used well validated native human C-reactive protein and pure factor H Y402H variants to test interactions. When factor H variants were incubated with C-reactive protein in the fluid phase at physiological concentrations, no association occurred. When C-reactive protein was immobilized on plastic, either non-specifically by adsorption in the presence of Ca(2+) to maintain its native fold and pentameric subunit assembly or by specific Ca(2+)-dependent binding to immobilized natural ligands, no specific binding of either factor H variant from the fluid phase was observed. In contrast, both factor H variants reproducibly bound to C-reactive protein immobilized in the absence of Ca(2+), conditions that destabilize the native fold and pentameric assembly. Both factor H variants strongly bound C-reactive protein that was denatured by heat treatment before immobilization, confirming interaction with denatured but not native C-reactive protein. We conclude that the reported binding of factor H to C-reactive protein results from denaturation of the C-reactive protein during immobilization. Differential binding to C-reactive protein, thus, does not explain association of the Y402H polymorphism with macular degeneration.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.