ArticleThe Journal of biological chemistry2013
Procoagulant platelets form an α-granule protein-covered "cap" on their surface that promotes their attachment to aggregates.
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 35 papers.
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Who cites it
35 citing papers in PubMed, 93 citations in OpenAlex.
- Bleeding tendency and platelet function during treatment with romiplostim in children with severe immune thrombocytopenic purpura.International journal of hematology · 2017Trial
- Procoagulant platelets: linking coagulation and thromboinflammation in cardiovascular disease.Nature reviews. Cardiology · 2026Review
- Platelet-Prostate cancer crosstalk driving disparities and therapeutic vulnerabilities.Discover oncology · 2026Review
- Murine thrombus organization limits access to high platelet activation states while supporting platelet recruitment.Blood vessels, thrombosis & hemostasis · 2026Article
- Continuum and discrete modeling of binding-site distribution-mediated reactions on lipid surfaces.Biophysical journal · 2026Article
- Beyond Direct Fibrinolysis: Novel Approaches to Thrombolysis.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Fibrin as the mediator of tumor cell interaction with platelets.Journal of molecular medicine (Berlin, Germany) · 2025Article
- The Ways of the Virus: Interactions of Platelets and Red Blood Cells with SARS-CoV-2, and Their Potential Pathophysiological Significance in COVID-19.International journal of molecular sciences · 2023Review
- A thrombus is formed by a gradient of platelet activation and procoagulant endothelium.Research and practice in thrombosis and haemostasis · 2023Article
- Platelet procoagulant membrane dynamics: a key distinction between thrombosis and hemostasis?Blood advances · 2023Article
- Study on Doxorubicin Loading on Differently Functionalized Iron Oxide Nanoparticles: Implications for Controlled Drug-Delivery Application.International journal of molecular sciences · 2023Article
- Activation mechanism dependent surface exposure of cellular factor XIII on activated platelets and platelet microparticles.Journal of thrombosis and haemostasis : JTH · 2022Article
- Location, location, location: Fibrin, cells, and fibrinolytic factors in thrombi.Frontiers in cardiovascular medicine · 2022Review
- Factor XIII-A: An Indispensable "Factor" in Haemostasis and Wound Healing.International journal of molecular sciences · 2021Review
- Thrombocytopathies: Not Just Aggregation Defects-The Clinical Relevance of Procoagulant Platelets.Journal of clinical medicine · 2021Review
- Exposure of plasminogen and a novel plasminogen receptor, Plg-RKT, on activated human and murine platelets.Blood · 2021Article
- Characterization of Procoagulant COAT Platelets in Patients with Glanzmann Thrombasthenia.International journal of molecular sciences · 2020Article
- Single platelet variability governs population sensitivity and initiates intrinsic heterotypic responses.Communications biology · 2020Article
- Article
- Procoagulant Phosphatidylserine-Exposing PlateletsFrontiers in cardiovascular medicine · 2020Review
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Strongly activated "coated" platelets are characterized by increased phosphatidylserine (PS) surface expression, α-granule protein retention, and lack of active integrin αIIbβ3. To study how they are incorporated into thrombi despite a lack of free activated integrin, we investigated the structure, function, and formation of the α-granule protein "coat." Confocal microscopy revealed that fibrin(ogen) and thrombospondin colocalized as "cap," a single patch on the PS-positive platelet surface. In aggregates, the cap was located at the point of attachment of the PS-positive platelets. Without fibrin(ogen) retention, their ability to be incorporated in aggregates was drastically reduced. The surface fibrin(ogen) was strongly decreased in the presence of a fibrin polymerization inhibitor GPRP and also in platelets from a patient with dysfibrinogenemia and a fibrinogen polymerization defect. In contrast, a fibrinogen-clotting protease ancistron increased the amount of fibrin(ogen) and thrombospondin on the surface of the PS-positive platelets stimulated with collagen-related peptide. Transglutaminases are also involved in fibrin(ogen) retention. However, platelets from patients with factor XIII deficiency had normal retention, and a pan-transglutaminase inhibitor T101 had only a modest inhibitory effect. Fibrin(ogen) retention was normal in Bernard-Soulier syndrome and kindlin-3 deficiency, but not in Glanzmann thrombasthenia lacking the platelet pool of fibrinogen and αIIbβ3. These data show that the fibrin(ogen)-covered cap, predominantly formed as a result of fibrin polymerization, is a critical mechanism that allows coated (or rather "capped") platelets to become incorporated into thrombi despite their lack of active integrins.
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