ReviewCurrent opinion in hematology2024
New insights of glycoprotein Ib-IX-V complex organization and glycoprotein Ibα in platelet biogenesis.
Review in Current opinion in hematology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Platelet glycoprotein V autoantibodies and complement C3 are associated with thrombosis in systemic lupus erythematosus.Haematologica · 2026Article
- Multi-Target Anticoagulant Regulation by Peptides from Medicinal Leeches: A Unique Natural Strategy against Thrombosis.Pharmaceutical research · 2026Review
- The relationship between ABO blood types and clopidogrel-related low on-treatment platelet reactivity in patients with coronary artery diseases and type 2 diabetes mellitus: a secondary analysis of a prospective cohort study.Diabetology & metabolic syndrome · 2025Article
- Platelet RNA-Seq Reveals Genes Associated with Carotid Intima-Media Thickness: A Cross-Sectional Study.TH open : companion journal to thrombosis and haemostasis · 2025Article
- NETs promote invasive behavior of fibroblast-like synoviocytes through GPIbα in rheumatoid arthritis.Frontiers in immunology · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
purpose of reviewGlycoprotein (GP) Ib-IX-V, a platelet surface receptor that plays a critical role in platelet adhesion and platelet-mediated immune responses, consists of GPIbα, GPIbβ, GPIX, and GPV in a stoichiometry of 2 : 4 : 2 : 1. Forming a complex is essential for GPIb-IX-V to function. GPIb-IX-V also plays an important role in platelet biogenesis by regulating the number and size of platelets. Yet how GPIb-IX-V regulates platelet biogenesis remains elusive. This review will summarize recent findings in the complex organization of GPIb-IX-V and its role in platelet biogenesis. RECENT
findingsProteomics studies suggest that GPIbα, GPIbβ, GPIX, and GPV form the complex in a ratio of 1 : 2 : 1 : 1, which is supported by analysis of molecular weight of GPIb-IX-V and GPIb-IX and the structure of entire GPIb-IX-V. To activate platelets, GPIbα requires binding of CLEC-2 to trigger signals. Furthermore, disrupting the GPIbα anchorage to filamin A causes defects in platelet budding away from proplatelets leading to giant platelets and a low platelet count. SUMMARY: New studies challenge the traditional model for the organization of GPIb-IX-V as a complex and indicate the role of GPIb-IX-V in platelet production. Those studies provide insights for GPIb-IX-V in the regulation of platelet activation and platelet biogenesis.
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