Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Platelet GPIb-V-IX complex. Structure, function, physiology, and pathology

K J Clemetson1, J M Clemetson

  • 1Theodor Kocher Institute, University of Berne, Switzerland.

Seminars in Thrombosis and Hemostasis
|January 1, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Distinct effects of Re- and S-forms of LPS on modulating platelet activation.

Journal of thrombosis and haemostasis : JTH·2013
Same author

Potential therapeutic targeting of platelet-mediated cellular interactions in atherosclerosis and inflammation.

Current medicinal chemistry·2011
Same author

The role of platelets in defence against pathogens.

Hamostaseologie·2011
Same author

Classification and nomenclature of snake venom C-type lectins and related proteins.

Toxicon : official journal of the International Society on Toxinology·2009
Same author

Scientific and standardization committee communications: classification and nomenclature of snake venom C-type lectins and related proteins.

Journal of thrombosis and haemostasis : JTH·2008
Same author

Snake venom C-type lectins as tools in platelet research.

Platelets·2006
Same journal

Bridging the Gap in Laboratory Monitoring of Extended Half-Life Factor VIII and IX: Can Thrombin Generation Assays Overcome Assay Discrepancies?

Seminars in thrombosis and hemostasis·2026
Same journal

External Quality Assessment for Low Molecular Weight Heparin Monitoring in the Australasia/Asia-Pacific Region.

Seminars in thrombosis and hemostasis·2026
Same journal

Human evolution: between hemorrhage and thrombosis.

Seminars in thrombosis and hemostasis·2026
Same journal

Full- vs Reduced-Dose Direct Oral Anticoagulants for Extended Treatment of Cancer-Associated Thrombosis: A Multicenter Retrospective Cohort Study.

Seminars in thrombosis and hemostasis·2026
Same journal

Too Old for PESI?: Risk Stratification of Octogenarians with Pulmonary Embolism in the Emergency Department.

Seminars in thrombosis and hemostasis·2026
Same journal

Acute Management and Bleeding Outcomes in Pediatric Pulmonary Embolism: A Large Single-Center Retrospective Cohort Study.

Seminars in thrombosis and hemostasis·2026
See all related articles

Platelets use the glycoprotein (GP) Ib-V-IX complex to bind von Willebrand factor (vWf) during hemostasis. This complex also mediates platelet activation by thrombin, crucial for rapid responses.

Area of Science:

  • Hematology
  • Molecular Biology
  • Biochemistry

Background:

  • Platelet adhesion to damaged blood vessels is initiated by the glycoprotein (GP) Ib-V-IX complex binding to von Willebrand factor (vWf).
  • This complex comprises GPIb alpha, GPIb beta, GPIX, and GPV subunits, playing a role in primary hemostasis and platelet activation.
  • Defects in this complex lead to bleeding disorders like Bernard-Soulier syndrome (BSS) and pseudo-von Willebrand disease, aiding in understanding vWf binding.

Purpose of the Study:

  • To elucidate the mechanism of vWf binding to the GPIb-V-IX complex.
  • To investigate the role of the GPIb-V-IX complex in platelet activation by thrombin.
  • To understand how thrombin cleavage of GPV affects platelet function.

Main Methods:

  • Analysis of platelet glycoprotein defects and their associated disorders (e.g., BSS).

Related Experiment Videos

  • Characterization of the vWf binding site on GPIb alpha.
  • Investigating thrombin's interaction with the GPIb-V-IX complex and its effect on platelet activation.

    • Main Results:

    • The GPIb-V-IX complex binds vWf via GPIb alpha, with binding likely involving conformational changes.
    • The complex possesses a thrombin binding site on GPIb alpha, essential for thrombin-mediated platelet activation.
    • Thrombin cleavage of GPV occurs, but its functional significance remains unclear.
    • Platelet activation by thrombin, especially at low doses via the seven-transmembrane receptor, is dependent on the GPIb-V-IX complex.

    Conclusions:

    • The GPIb-V-IX complex is critical for both initial platelet adhesion via vWf and subsequent activation by thrombin.
    • Understanding the complex's structure-function relationship is key to comprehending hemostasis and developing treatments for related disorders.