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

Functional characterization of lanatoside-C-responsive cells.

L Hammarström, C I Smith, U Persson

    Scandinavian Journal of Immunology
    |January 1, 1978
    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

    The influence of the structure of the Au(110) surface on the ordering of a monolayer of cytochrome P450 reductase at the Au(110)/phosphate buffer interface.

    Physica status solidi. B, Basic solid state physics : PSS·2016
    Same author

    Anion replacement at Au(110)/electrolyte interfaces.

    Physical chemistry chemical physics : PCCP·2016
    Same author

    The stability of the Au(1 1 0)-(1  ×  3) surface reconstruction in electrochemical environments.

    Journal of physics. Condensed matter : an Institute of Physics journal·2015
    Same author

    The reflection anisotropy spectroscopy of the Au(1 1 0) surface structures in liquid environments.

    Journal of physics. Condensed matter : an Institute of Physics journal·2015
    Same author

    When does an autoimmune disease start?

    Immunology today·2014
    Same author

    Conformational change in cytochrome P450 reductase adsorbed at a Au(110)-phosphate buffer interface induced by interaction with nicotinamide adenine dinucleotide phosphate.

    Physical review. E, Statistical, nonlinear, and soft matter physics·2014

    Lanatoside C activates immature B cells in various tissues. Suppressor T cells inhibit this response, suggesting lanatoside C can mark direct B cell activation.

    Area of Science:

    • Immunology
    • Cell Biology

    Background:

    • Lanatoside C, a digitalis glycoside, is a known polyclonal B-cell activator (PBA).
    • Previous research indicated its role in immune system modulation.

    Purpose of the Study:

    • To investigate the specific cell populations activated by lanatoside C.
    • To elucidate the regulatory mechanisms, including suppressor T cell involvement, in lanatoside C-induced B-cell activation.
    • To compare lanatoside C-responsive cells with those activated by other mitogens like dextran sulfate (DxS) and lipopolysaccharide (LPS).

    Main Methods:

    • Cell proliferation assays using fetal liver, bone marrow, spleen, lymph node, and peripheral blood cells.
    • Macrophage depletion and antibody-mediated cell depletion (anti-Ig, anti-Ia, anti-Thy 1.2) to identify responding cell types and regulatory cells.

    Related Experiment Videos

  • Synergy experiments with known polyclonal B-cell activators (DxS, LPS).

    • Main Results:

    • Lanatoside C stimulated immature B cells from multiple lymphoid organs and peripheral blood.
    • Macrophage removal did not affect spleen cell response, but anti-Ig/anti-Ia treatment partially inhibited it.
    • T cell depletion significantly enhanced the proliferative response, indicating suppressor T cell activity.
    • Lanatoside C-responding cells showed overlap with DxS- and LPS-sensitive cell populations.

    Conclusions:

    • Lanatoside C directly activates immature B cells, independent of macrophages.
    • A naturally occurring suppressor T cell population regulates glycoside-induced mitogenesis.
    • Lanatoside C can serve as a functional marker for the direct activation of immature B cells.