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Author Notes:

Corresponding author: Renhao Li, Department of Pediatrics, Emory University School of Medicine, 2015 Upper gate Drive NE, Atlanta, GA 30322. Phone: 404-727-8217; Fax: 404-727-4859; renhao.li@emory.edu

Acknowledgements The authors thank Drs. Joel Bennett, Pete Lollar and Shannon Meeks for critical reading of the manuscript.

The authors declare no conflict of interest.

Subjects:

Research Funding:

The authors gratefully acknowledge support from National Institutes of Health (HL082808 and HL097226).

Keywords:

  • GPIb-IX-V complex
  • platelet glycoprotein
  • Bernard-Soulier syndrome
  • leucine-rich repeat domain
  • transmembrane domain

The Organizing Principle of Platelet Glycoprotein Ib-IX-V Complex

Tools:

Journal Title:

Journal of Thrombosis and Haemostasis

Volume:

Volume 11, Number 4

Publisher:

, Pages 605-614

Type of Work:

Article | Post-print: After Peer Review

Abstract:

The glycoprotein (GP)Ib-IX-V complex is the platelet receptor for von Willebrand factor and many other molecules critically involved in he most as is and thrombosis. The lack of functional GPIb-IX-V complexes on the platelet surface is the cause of Bernard-Soulier syndrome, a rare hereditary bleeding disorder also associated with macro thrombocytopenia. The GPIb-IX-V complex contains GPIbα, GPIbβ, GPIX and GPV subunits, all of which are type I trans membrane proteins containing leucine-rich repeat domains. Although all the subunits were identified decades ago, not until recently did the mechanism of complex assembly begin to emerge from a systematic characterization of inter-subunit interactions. This review summarizes forces driving the assembly of the GPIb-IX-V complex, discusses their implication on the pathogenesis of Bernard-Soulier syndrome, and identifies questions that remain about the structure and organization of GPIb-IX-V.

Copyright information:

© 2013 International Society on Thrombosis and Haemostasis

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