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

The collagen-platelet interaction

M J Barnes1, C G Knight, R W Farndale

  • 1Biochemistry Department, University of Cambridge, UK.

Current Opinion in Hematology
|October 17, 1998
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

Antimutator and Mutational Spectrum Effects Can Combine to Reduce Evolutionary Potential in Escherichia coli ΔnudJ.

Molecular biology and evolution·2025
Same author

SyncMRT: a solution to image-guided synchrotron radiotherapy for quality assurance and pre-clinical trials.

Journal of synchrotron radiation·2022
Same author

Training injury incidence in an amateur women's rugby union team in New Zealand over two consecutive seasons.

Journal of science and medicine in sport·2020
Same author

Intraperitoneal injection of sodium pentobarbital has the potential to elicit pain in adult rats (Rattus norvegicus).

PloS one·2020
Same author

The chaperone protein HSP47: a platelet collagen binding protein that contributes to thrombosis and hemostasis.

Journal of thrombosis and haemostasis : JTH·2018
Same author

Platelet collagen receptor Glycoprotein VI-dimer recognizes fibrinogen and fibrin through their D-domains, contributing to platelet adhesion and activation during thrombus formation.

Journal of thrombosis and haemostasis : JTH·2017
Same journal

Dynamic myeloid suppressor states in cancer and inflammation and their therapeutic potential.

Current opinion in hematology·2026
Same journal

Factor XIa inhibition for the prevention of thrombosis: mechanism, clinical trial signals, and indication-specific positioning.

Current opinion in hematology·2026
Same journal

Nutrition as a regulator of hematopoietic stem cell biology and transplantation.

Current opinion in hematology·2026
Same journal

From biomimicry to clinical actionability: rethinking high-shear thrombosis as a mechanobiological system.

Current opinion in hematology·2026
Same journal

Bidirectional relationship between metabolic and thrombotic disease mechanisms.

Current opinion in hematology·2026
Same journal

The dual role of the brain-derived neurotrophic factor as a regulator of hemostasis and thrombotic risk.

Current opinion in hematology·2026
See all related articles

Platelet activation involves collagen-platelet interaction through distinct receptors. This process, crucial for hemostasis and thrombosis, includes adhesion and activation steps mediated by specific collagen sequences and platelet receptors.

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Collagen-platelet interaction is a critical process in both hemostasis (blood clotting) and thrombosis (unwanted clot formation).
  • This interaction is a sequential, two-step process involving platelet adhesion and subsequent activation.
  • Distinct platelet receptors mediate the recognition of collagen and initiate downstream signaling.

Purpose of the Study:

  • To elucidate the sequential receptor-ligand interactions during collagen-platelet adhesion.
  • To detail the specific collagen sequences and platelet receptors involved in initiating platelet activation.
  • To outline the unique signaling pathways triggered by collagen as a platelet agonist.

Main Methods:

  • Analysis of collagen-platelet adhesion mechanisms.

Related Experiment Videos

  • Identification of key platelet receptors involved in collagen recognition (e.g., Gp Ib/IX/V, alpha2beta1, Gp VI).
  • Investigation of collagen sequences (e.g., GER motif, GPP* sequences) critical for receptor binding.
  • Characterization of downstream signaling molecules (e.g., Fc receptor gamma-chain, p72syk, phospholipase Cgamma2).

    • Main Results:

    • Adhesion involves initial reversible binding via Gp Ib/IX/V to von Willebrand factor, followed by direct collagen binding to alpha2beta1.
    • The integrin alpha2beta1 specifically recognizes collagen sequences, with the GER motif being important.
    • Platelet activation is triggered by Gp VI binding to GPP* sequences in collagen.
    • Gp VI initiates unique signaling cascades, including the recruitment of the Fc receptor gamma-chain, p72syk, and phospholipase Cgamma2.

    Conclusions:

    • Collagen-platelet interaction is a multi-step process mediated by a cascade of specific receptor-collagen interactions.
    • The distinct recognition of collagen by Gp Ib/IX/V, alpha2beta1, and Gp VI orchestrates both adhesion and activation.
    • The Gp VI-mediated pathway represents a unique signaling mechanism for collagen-induced platelet activation, essential for understanding thrombotic and hemostatic events.