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-calmodulin interaction and cellular function.

J A Cox

    Journal of Cardiovascular Pharmacology
    |January 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Calmodulin (CaM) function is governed by calcium ion (Ca2+) saturation, not specific binding sites. High Ca2+ levels activate target enzymes, causing delayed cellular responses due to hysteresis.

    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

    Quantifying airborne dispersal routes of pathogens over continents to safeguard global wheat supply.

    Nature plants·2017
    Same author

    Antibiotic stewardship in low- and middle-income countries: the same but different?

    Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2017
    Same author

    Exploring the consequences of mitochondrial differences arising through hybridization of sunfish.

    Comparative biochemistry and physiology. Part A, Molecular & integrative physiology·2014
    Same author

    Calcium-binding and its effect on circular dichroism of plant calmodulin.

    Planta·2013
    Same author

    Differential scattering cross-sections for the different product vibrational States in the ion-molecule reaction Ar(+)+N2.

    Physical review letters·2013
    Same author

    Pulse synthesis in the single-cycle regime from independent mode-locked lasers using attosecond-precision feedback.

    Optics letters·2012
    Same journal

    SGLT2 Inhibitors and Progression of Chronic Kidney Disease in Patients with Elevated Lipoprotein(a): A Real-World Cohort Study.

    Journal of cardiovascular pharmacology·2026
    Same journal

    Aspirin in primary prevention: a case for selective use.

    Journal of cardiovascular pharmacology·2026
    Same journal

    GLP-1 Gene Therapy Trial for Obesity and Type 2 Diabetes: Towards a New Paradigm for Chronic Disease Treatment.

    Journal of cardiovascular pharmacology·2026
    Same journal

    Expert Opinion: Restrictions, Precautions, or Normalcy? Defining Everyday Risk in Patients Treated With IL-1 Blockers for Recurrent Pericarditis.

    Journal of cardiovascular pharmacology·2026
    Same journal

    The Therapeutic Role of Exercise in Diabetic Cardiomyopathy: Underlying Mechanisms and Interactions with Antidiabetic Medications.

    Journal of cardiovascular pharmacology·2026
    Same journal

    Cardiovascular Adverse Events Associated with Immune Checkpoint Inhibitors from the Perspective of Gut Microecology: Potential Roles and Research Advances of the Gut Microbiota.

    Journal of cardiovascular pharmacology·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Signaling

    Background:

    • Calmodulin (CaM) is a crucial calcium-binding protein involved in cellular signaling.
    • CaM's conformational and functional states are modulated by calcium ion (Ca2+) binding.
    • Understanding CaM's interaction with target enzymes is key to deciphering cellular responses.

    Purpose of the Study:

    • To investigate the relationship between Ca2+ saturation levels and CaM's functional states.
    • To explore the role of Ca2+-bound CaM in target enzyme activation.
    • To identify structural requirements for CaM-Ca2+-enzyme complex formation.

    Main Methods:

    • Analysis of CaM conformational changes based on Ca2+ saturation.
    • Characterization of CaM species involved in target enzyme activation.

    Related Experiment Videos

  • Study of natural and synthetic peptides interacting with CaM.

    • Main Results:

    • CaM function is dictated by overall Ca2+ saturation, not specific ion-binding sites.
    • CaM with two or more Ca2+ ions exposes hydrophobic surfaces.
    • CaM with at least three Ca2+ ions is primarily involved in target enzyme activation.
    • CaM-activated systems exhibit 'on-off' behavior and hysteresis due to delayed complex dissociation.

    Conclusions:

    • Ca2+ saturation level is the primary determinant of CaM's functional output.
    • The binding of Ca2+-saturated CaM to target enzymes involves a hysteretic mechanism.
    • A basic amphiphilic alpha-helix of at least 18 angstroms is essential for high-affinity CaM interaction, a feature potentially present in target enzyme binding domains.