ReviewResearch and practice in thrombosis and haemostasis2019
Fibrinogen αC domain: Its importance in physiopathology.
Review in Research and practice in thrombosis and haemostasis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Concurrent fibrinogen Aα-chain amyloidosis and AA amyloidosis in a Humboldt penguin (Spheniscus humboldti).Veterinary research communications · 2026Article
- The fibrinogen αC region promotes arterial thrombosis in the context of hypofibrinogenemia.Blood · 2026Article
- Surface cues shape procoagulant properties of amyloidogenic microclots.Cell death & disease · 2026Review
- Multifaceted Role of Quercetin in Colorectal Cancer: An Integrative Review on Adipose Tissue Modulation and Direct Anti-tumor Mechanisms.Chinese journal of integrative medicine · 2026Review
- Exploiting the Molecular Properties of Fibrinogen to Control Bleeding Following Vascular Injury.International journal of molecular sciences · 2025Review
- Anion exchange chromatographic fractionation of urinary proteins followed by tandem mass spectrometry identifies potential natural inhibitors of calcium oxalate stone.Computational and structural biotechnology journal · 2025Article
- Fibrinogen αC-region acts as a functional safety latch: Implications for a fibrin biomechanical behaviour model.Acta biomaterialia · 2024Article
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- The Story of the Fibrin(ogen) αC-Domains: Evolution of Our View on Their Structure and Interactions.Thrombosis and haemostasis · 2022Review
- Article
- Potential Biomarkers of Acute Ischemic Stroke Etiology Revealed by Mass Spectrometry-Based Proteomic Characterization of Formalin-Fixed Paraffin-Embedded Blood Clots.Frontiers in neurology · 2022Article
- The protective effect of early dietary fat consumption on Alzheimer's disease-related pathology and cognitive function in mice.Alzheimer's & dementia (New York, N. Y.) · 2021Article
- Fibrin(ogen) in human disease: both friend and foe.Haematologica · 2020Review
- Fibrinogen alpha amyloidosis: insights from proteomics.Expert review of proteomics · 2019Review
- Fibrinogen αC domain: Its importance in physiopathology.Research and practice in thrombosis and haemostasis · 2019Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ABSTRACT: Fibrinogen, involved in coagulation, is a soluble protein composed of two sets of disulfide-bridged Aα, Bβ, and γ-chains. In this review, we present the clinical implications of the αC domain of the molecule in Alzheimer's disease, hereditary renal amyloidosis and a number of thrombotic and hemorrhagic disorders. In Alzheimer's disease, amyloid beta peptide (Aβ) is increased and binds to the αC domain of normal fibrinogen, triggering increased fibrin(ogen) deposition in patients' brain parenchyma. In hereditary renal amyloidosis, fibrinogen is abnormal, with mutations located in the fibrinogen αC domain. The mutant αC domain derived from fibrinogen degradation folds incorrectly so that, in time, aggregates form, leading to amyloid deposits in the kidneys. In these patients, no thrombotic tendency has been observed. Abnormal fibrinogens with either a point mutation in the αC domain or a frameshift mutation resulting in absence of a part of the αC domain are often associated with either thrombotic events or bleeding. Mutation of an amino acid into cysteine (as in fibrinogens Dusart and Caracas V) or a frameshift mutation yielding an unpaired cysteine in the αC domain is often responsible for thrombotic events. Covalent binding of albumin to the unpaired cysteine via a disulphide bridge leads to decreased accessibility to the fibrinolytic enzymes, hence formation of poorly degradable fibrin clots, which explains the high incidence of thrombosis. In contrast, anomalies due to a frameshift mutation in the αC connector of the molecule, provoking deletion of a great part of the αC domain, are associated with bleeding.
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