ArticleThe Journal of biological chemistry2013
Zn2+ mediates high affinity binding of heparin to the αC domain of fibrinogen.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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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.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Binding properties of marine sulfated glycans to coagulation (co)-factors using surface plasmon resonance spectroscopy.Scientific reports · 2026Article
- Investigating the conformational landscape of human histidine-rich glycoprotein using amide HDX-MS.The Biochemical journal · 2025Article
- Fibrinogen based resuscitation mitigates lung injury in mice with bacterial pneumonia after hemorrhagic shock.Biochemistry and biophysics reports · 2025Article
- Contributing factors to heparin resistance during cardiopulmonary bypass.Journal of artificial organs : the official journal of the Japanese Society for Artificial Organs · 2024Article
- Association of Metal Cations with the Anti-PF4/Heparin Antibody Response in Heparin-Induced Thrombocytopenia.Cardiovascular toxicology · 2024Article
- Association of Metal Cations with the Anti-PF4/Heparin Antibody Response in Heparin-Induced Thrombocytopenia.Research square · 2024Article
- ZnInternational journal of molecular sciences · 2023Article
- Crosstalk between Circulating Tumor Cells and Plasma Proteins-Impact on Coagulation and Anticoagulation.Cancers · 2023Review
- Strategies for Therapeutic Amelioration of Aberrant Plasma ZnInternational journal of molecular sciences · 2022Review
- The Interplay between Non-Esterified Fatty Acids and Plasma Zinc and Its Influence on Thrombotic Risk in Obesity and Type 2 Diabetes.International journal of molecular sciences · 2021Review
- Elucidation of Cellular Contributions to Heparin-Induced Thrombocytopenia Using Omic Approaches.Frontiers in pharmacology · 2021Review
- Zinc Therapy in Early Alzheimer's Disease: Safety and Potential Therapeutic Efficacy.Biomolecules · 2020Review
- Crosstalk between zinc and free fatty acids in plasma.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
- Influence of zinc on glycosaminoglycan neutralisation during coagulation.Metallomics : integrated biometal science · 2018Review
- Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein.Scientific reports · 2018Article
- Microparticle-mediated sequestration of cell-secreted proteins to modulate chondrocytic differentiation.Acta biomaterialia · 2018Article
- Heparin/Heparan sulfate proteoglycans glycomic interactome in angiogenesis: biological implications and therapeutical use.Molecules (Basel, Switzerland) · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin. In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin from inhibition by the heparin-antithrombin complex. Previous studies have shown that heparin binds the E domain of fibrinogen. The current investigation examines the role of Zn(2+) in this interaction because Zn(2+) is released locally by platelets and both heparin and fibrinogen bind the cation, resulting in greater protection from inhibition by antithrombin. Zn(2+) promotes heparin binding to fibrinogen, as determined by chromatography, fluorescence, and surface plasmon resonance. Compared with intact fibrinogen, there is reduced heparin binding to fragment X, a clottable plasmin degradation product of fibrinogen. A monoclonal antibody directed against a portion of the fibrinogen αC domain removed by plasmin attenuates binding of heparin to fibrinogen and a peptide analog of this region binds heparin in a Zn(2+)-dependent fashion. These results indicate that the αC domain of fibrinogen harbors a Zn(2+)-dependent heparin binding site. As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present. These results reveal the mechanism by which Zn(2+) augments the capacity of fibrinogen to impair the anticoagulant activity of heparin.
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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.