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

Calcium-dependent proteolysis occurs during platelet aggregation.

J E Fox, C C Reynolds, D R Phillips

    The Journal of Biological Chemistry
    |August 25, 1983
    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

    How Well Do We Know the Neutron-Matter Equation of State at the Densities Inside Neutron Stars? A Bayesian Approach with Correlated Uncertainties.

    Physical review letters·2020
    Same author

    Power counting of contact-range currents in effective field theory.

    Physical review letters·2015
    Same author

    Measurement of Compton scattering from the deuteron and an improved extraction of the neutron electromagnetic polarizabilities.

    Physical review letters·2015
    Same author

    Radioarsenic from a portable (72)Se/(72)As generator: a current perspective.

    Current radiopharmaceuticals·2012
    Same author

    Processing of anthracycline-DNA adducts via DNA replication and interstrand crosslink repair pathways.

    Biochemical pharmacology·2012
    Same author

    Barminomycin, a model for the development of new anthracyclines.

    Anti-cancer agents in medicinal chemistry·2009
    Same journal

    Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

    The Journal of biological chemistry·2026
    Same journal

    Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

    The Journal of biological chemistry·2026
    Same journal

    Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

    The Journal of biological chemistry·2026
    Same journal

    Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

    The Journal of biological chemistry·2026
    Same journal

    YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

    The Journal of biological chemistry·2026
    Same journal

    ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

    The Journal of biological chemistry·2026
    See all related articles

    Platelet activation by thrombin or collagen triggers a calcium-dependent protease, generating new proteins during aggregation. This protease activation is crucial for platelet response to stimulation.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Hematology

    Background:

    • Platelet activation is a complex process involving protein modifications.
    • Understanding protein alterations during platelet stimulation is key to comprehending hemostasis and thrombosis.

    Purpose of the Study:

    • To investigate protein changes in platelets upon activation with various stimuli.
    • To identify specific proteins altered during platelet aggregation and their potential role.

    Main Methods:

    • Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) was used to analyze platelet proteins.
    • Platelets were stimulated with thrombin, collagen, and calcium ionophore A23187.
    • Proteolytic digestion with Staphylococcus aureus V8 protease and calcium-dependent protease inhibitors were employed.

    Related Experiment Videos

    Main Results:

    • Three novel polypeptides (Mr 200,000, 100,000, and 91,000) were identified in activated platelets.
    • A fourth polypeptide (Mr 97,000) was specific to thrombin-activated platelets.
    • These polypeptides were generated by a calcium-dependent protease activated during aggregation, and their formation was inhibited by protease inhibitors.

    Conclusions:

    • Platelet activation by physiological agents leads to the activation of a calcium-dependent protease.
    • This protease plays a significant role in the protein modifications observed during platelet aggregation.
    • The identified polypeptides are potential markers or mediators of platelet activation and response.