ArticlePloS one2014
α2β1 integrin, GPVI receptor, and common FcRγ chain on mouse platelets mediate distinct responses to collagen in models of thrombosis.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Characterization of Novel Variants inBiomolecules · 2025Article
- A Perspective on How Fibrinaloid Microclots and Platelet Pathology May be Applied in Clinical Investigations.Seminars in thrombosis and hemostasis · 2024Review
- Platelet procoagulant membrane dynamics: a key distinction between thrombosis and hemostasis?Blood advances · 2023Article
- Adenosine 2A Receptor Activation Amplifies Ibrutinib Antiplatelet Effect; Implications in Chronic Lymphocytic Leukemia.Cancers · 2022Article
- Reversible Platelet Integrin αIIbβ3 Activation and Thrombus Instability.International journal of molecular sciences · 2022Review
- Modulation of Glycoprotein VI and Its Downstream Signaling Pathways as an Antiplatelet Target.International journal of molecular sciences · 2022Review
- Platelet Membrane: An Outstanding Factor in Cancer Metastasis.Membranes · 2022Review
- Role of Neutrophils and NETs in Animal Models of Thrombosis.International journal of molecular sciences · 2022Review
- Platelets, Constant and Cooperative Companions of Sessile and Disseminating Tumor Cells, Crucially Contribute to the Tumor Microenvironment.Frontiers in cell and developmental biology · 2021Review
- Cryptic collagen elements as signaling hubs in the regulation of tumor growth and metastasis.Journal of cellular physiology · 2020Review
- Engineering small-caliber vascular grafts from collagen filaments and nanofibers with comparable mechanical properties to native vessels.Biofabrication · 2019Article
- Structurally Robust and Functionally Highly Versatile-C-Type Lectin (-Related) Proteins in Snake Venoms.Toxins · 2019Review
- Impact of Itga2-Gp6-double collagen receptor deficient mice for bone marrow megakaryocytes and platelets.PloS one · 2019Article
- Dramatic and concerted conformational changes enable rhodocetin to block α2β1 integrin selectively.PLoS biology · 2017Article
- Characterization of the platelet transcriptome by RNA sequencing in patients with acute myocardial infarction.Platelets · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
objectivePlatelets express the α2β1 integrin and the glycoprotein VI (GPVI)/FcRγ complex, both collagen receptors. Understanding platelet-collagen receptor function has been enhanced through use of genetically modified mouse models. Previous studies of GPVI/FcRγ-mediated collagen-induced platelet activation were perfomed with mice in which the FcRγ subunit was genetically deleted (FcRγ-/-) or the complex was depleted. The development of α2β1-/- and GPVI-/- mice permits side-by-side comparison to address contributions of these collagen receptors in vivo and in vitro. APPROACH AND
resultsTo understand the different roles played by the α2β1 integrin, the GPVI receptor or FcRγ subunit in collagen-stimulated hemostasis and thrombosis, we compared α2β1-/-, FcRγ-/-, and GPVI-/- mice in models of endothelial injury and intravascular thrombosis in vivo and their platelets in collagen-stimulated activation in vitro. We demonstrate that both the α2β1 integrin and the GPVI receptor, but not the FcRγ subunit influence carotid artery occlusion in vivo. In contrast, the GPVI receptor and the FcRγ chain, but not the α2β1 integrin, play similar roles in intravascular thrombosis in response to soluble Type I collagen. FcRγ-/- platelets showed less attenuation of tyrosine phosphorylation of several proteins including RhoGDI when compared to GPVI-/- and wild type platelets. The difference between FcRγ-/- and GPVI-/- platelet phosphotyrosine levels correlated with the in vivo thrombosis findings.
conclusionOur data demonstrate that genetic deletion of GPVI receptor, FcRγ chain, or the α2β1 integrin changes the thrombotic potentials of these platelets to collagen dependent on the stimulus mechanism. The data suggest that the FcRγ chain may provide a dominant negative effect through modulating signaling pathways in platelets involving several tyrosine phosphorylated proteins such as RhoGDI. In addition, these findings suggest a more complex signaling network downstream of the platelet collagen receptors than previously appreciated.
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