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Activation of protein kinase C modulates the expression of the T3/T cell antigen receptor complex on human T

A A Davies, D A Cantrell, M J Crumpton

    Bioscience Reports
    |October 1, 1985
    PubMed

    Insights

    Protein kinase C activators rapidly decrease T3 antigen and T-cell receptor expression on HPB-ALL cells. This is accompanied by phosphorylation of T3 gamma and delta polypeptides, primarily on serine residues.

    Area of Science:

    • Immunology
    • Cell Biology
    • Biochemistry

    Background:

    • The T3 antigen and T-lymphocyte antigen receptor (Ti) complex plays a crucial role in T-cell activation.
    • Protein kinase C (PKC) is a key signaling enzyme involved in various cellular processes, including immune responses.

    Purpose of the Study:

    • To investigate the effect of protein kinase C activators on the surface expression and phosphorylation of the T3/Ti complex in HPB-ALL cells.

    Main Methods:

    • HPB-ALL cells were treated with activators of protein kinase C.
    • Surface expression of T3 antigen and Ti was measured.
    • Phosphorylation of T3 polypeptides (gamma, delta, epsilon) and Ti polypeptides (alpha, beta) was analyzed.

    Main Results:

    • PKC activators caused a rapid decrease in surface expression of T3 antigen and Ti within 15 minutes.
    • Concomitant phosphorylation of T3 gamma and delta polypeptides was observed.
    • The T3 gamma chain showed more extensive phosphorylation than the delta chain.
    • No phosphorylation was detected on T3 epsilon, Ti alpha, or Ti beta polypeptides.
    • Phosphorylation of the T3 gamma chain occurred exclusively on serine residues.

    Conclusions:

    • Protein kinase C activation leads to rapid modulation of T3/Ti complex surface expression.
    • Specific T3 polypeptides (gamma and delta) are targets of PKC-mediated phosphorylation.
    • The findings highlight the role of PKC in regulating T-cell receptor signaling and surface expression.

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