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Effect of tunicamycin on receptors for tumor promoters

V Solanki, M K Logani, T J Slaga

    Cancer Letters
    |September 1, 1982
    PubMed

    Insights

    Tunicamycin treatment reduced phorbol ester receptor binding in mouse epidermal cells, suggesting this receptor is a glycoprotein. This impacts understanding of cell surface protein function.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Glycobiology

    Background:

    • Phorbol esters are known to interact with specific cell surface receptors.
    • Glycosylation is a crucial post-translational modification affecting protein function.
    • Tunicamycin inhibits dolichol-mediated glycosylation, impacting glycoprotein synthesis.

    Purpose of the Study:

    • To investigate the role of glycosylation in the function of the phorbol ester receptor.
    • To determine if the phorbol ester receptor is a glycoprotein or associated with one.

    Main Methods:

    • Primary mouse epidermal cells were treated with tunicamycin.
    • Specific binding of [3H]phorbol 12,13-dibutyrate ([3H]PDBu) was measured.
    • Glycoprotein synthesis was assessed.
    • Total protein synthesis was determined using leucine incorporation.

    Main Results:

    • Tunicamycin treatment led to a progressive decline in [3H]PDBu specific binding (33-56% of control after 18h).
    • Glycoprotein synthesis was significantly reduced by tunicamycin.
    • Total protein synthesis remained unaffected by tunicamycin treatment.

    Conclusions:

    • The phorbol ester receptor is likely a glycoprotein or functionally linked to one.
    • Glycosylation is essential for the proper binding or function of the phorbol ester receptor.
    • These findings provide insights into the molecular nature of cell surface receptors.

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