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

Ca2+-calmodulin-dependent phosphorylation and platelet secretion

M Nishikawa, T Tanaka, H Hidaka

    Nature
    |October 30, 1980
    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

    Anti-immunoglobulin M activates nuclear calcium/calmodulin-dependent protein kinase II in human B lymphocytes.

    The Journal of experimental medicine·1995
    Same author

    Elucidation of the protein kinase C-dependent apoptosis pathway in distinct subsets of T lymphocytes in MRL-lpr/lpr mice.

    European journal of immunology·1995
    Same author

    Purification and characterization of a novel protein activator of Ca2+/calmodulin-dependent protein kinase I.

    Biochemical and biophysical research communications·1995
    Same author

    Effect of KN-62, Ca2+/calmodulin-dependent protein kinase II inhibitor, on adriamycin resistance of human ovarian cancer cells.

    Biochemical and biophysical research communications·1995
    Same author

    The regulatory region of calcium/calmodulin-dependent protein kinase I contains closely associated autoinhibitory and calmodulin-binding domains.

    The Journal of biological chemistry·1995
    Same author

    Prophylaxis of genetically determined diabetes by diazoxide: a study in a rat model of naturally occurring obese diabetes.

    The Journal of pharmacology and experimental therapeutics·1995
    Same journal

    Keep the Hubble and James Webb Space Telescopes alive - the science is worth the price tag.

    Nature·2026
    Same journal

    Say hello to hard helium.

    Nature·2026
    Same journal

    How to avoid dementia - what the science really says.

    Nature·2026
    Same journal

    Save Hubble: the race to preserve the space telescope kicks off.

    Nature·2026
    Same journal

    How long can humans live? All evidence points to a maximum of 125 years.

    Nature·2026
    Same journal

    Listen to Gen Z when it comes to AI in education.

    Nature·2026
    See all related articles

    Platelet secretion involves protein phosphorylation, specifically of myosin light chain, which activates actomyosin contraction. This process is regulated by calcium and calmodulin, crucial for the platelet release reaction.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Pharmacology

    Background:

    • Platelet activation involves stimulus-coupled secretion.
    • Protein phosphorylation, particularly of myosin light chain, is implicated in platelet function.
    • The role of calcium-calmodulin-dependent light chain phosphorylation in platelet release reaction requires further clarification.

    Purpose of the Study:

    • To investigate the role of calmodulin-mediated myosin light chain phosphorylation in platelet secretion.
    • To provide pharmacological evidence for the involvement of this system in the platelet release reaction.

    Main Methods:

    • Identification of platelet phosphoproteins, including myosin light chain.
    • Characterization of platelet myosin light chain kinase as a calcium-dependent, calmodulin-requiring enzyme.

    Related Experiment Videos

  • In vitro studies using N-(6-aminohexyl)-5-chloro-1-napthalene-sulphonamide (W-7) to inhibit calmodulin activity.

    • Main Results:

    • Phosphorylation of myosin light chain (20,000 MW) enhances actin-activated myosin ATPase activity.
    • Actomyosin contraction, mediated by this phosphorylation, is presumed to cause the release reaction.
    • Pharmacological inhibition of calmodulin with W-7 provides evidence for its role in the release reaction.

    Conclusions:

    • Ca2+-dependent myosin light chain phosphorylation, regulated by calmodulin, plays a significant role in the platelet release reaction.
    • The findings support the hypothesis that non-muscle actomyosin regulation by light chain phosphorylation is functionally relevant in platelets.
    • Calmodulin is a key mediator in the stimulus-coupled secretion process of platelets.