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

von Willebrand factor: structure and function.

D Meyer1, G Piétu, E Fressinaud

  • 1Institut National de la Santé et de la Recherche Médicale, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.

Mayo Clinic Proceedings
|May 1, 1991
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

Locus and population specific evolution in HLA class II genes.

Annals of human genetics·2000
Same author

Fast and efficient mutation detection method using multiplex PCR and cycle sequencing--application to haemophilia B.

Thrombosis and haemostasis·2000
Same author

Physical, chemical, and biological evaluations of P760: a new gadolinium complex characterized by a low rate of interstitial diffusion.

Journal of magnetic resonance imaging : JMRI·2000
Same author

Thrombotic risk factors in pulmonary hypertension.

The European respiratory journal·2000
Same author

The kinetics of specific immune responses in rhesus monkeys inoculated with live recombinant BCG expressing SIV Gag, Pol, Env, and Nef proteins.

Virology·2000
Same author

Effects of natriuretic peptides on load and myocardial function in normal and heart failure dogs.

American journal of physiology. Heart and circulatory physiology·2000

Von Willebrand factor (vWF) is crucial for platelet adhesion and factor VIII transport. Researchers mapped functional domains and expressed vWF fragments to understand its role in hemostasis and thrombosis.

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Von Willebrand factor (vWF) is a glycoprotein essential for platelet adhesion and factor VIII stability.
  • vWF mediates platelet interaction with subendothelial components like collagen and heparin under high shear stress.
  • Optimal platelet adhesion requires vWF from plasma, platelets, and subendothelium.

Purpose of the Study:

  • To map functional domains of vWF responsible for binding to platelets, collagen, heparin, and factor VIII.
  • To investigate the role of specific vWF fragments in platelet adhesion and aggregation.
  • To express and characterize recombinant vWF fragments for functional analysis.

Main Methods:

  • Protease digestion and monoclonal antibody characterization to map vWF functional domains.

Related Experiment Videos

  • Expression of vWF complementary DNA fragments in Escherichia coli.
  • Assessment of recombinant vWF fragment binding to platelets, collagen, and heparin.
  • Evaluation of recombinant vWF fragment inhibition of ristocetin-induced platelet agglutination.

    • Main Results:

    • Identified at least eight functional domains on the vWF subunit.
    • vWF fragment SpIII (amino acids 1-1,365) promotes platelet adhesion to collagen.
    • Recombinant vWF fragment (amino acids 449-730) binds platelets, collagen, and heparin, inhibiting platelet agglutination.
    • Recombinant vWF fragment (amino acids 914-1,364) binds to collagen.

    Conclusions:

    • Specific vWF domains are critical for mediating platelet-vessel wall interactions.
    • Recombinant vWF fragments can recapitulate key binding functions and inhibit platelet activity.
    • Understanding vWF structure-function relationships is vital for hemostasis and thrombosis research.