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Cell surface galactosyltransferase: immunochemical localization.

N L Shaper, P L Mann, J H Shaper

    Journal of Cellular Biochemistry
    |January 1, 1985
    PubMed
    Summary
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    Researchers localized UDP-galactose:N-acetylglucosamine galactosyltransferase (GT) on bovine cell surfaces using immunohistochemistry. This cell surface enzyme

    Area of Science:

    • Cell Biology
    • Biochemistry
    • Immunology

    Background:

    • The localization of UDP-galactose:N-acetylglucosamine galactosyltransferase (GT) on cell surfaces is crucial for understanding cellular processes.
    • Previous studies have not definitively localized this enzyme on the surface of bovine cells.

    Purpose of the Study:

    • To directly localize the UDP-galactose:N-acetylglucosamine galactosyltransferase (GT) on the surface of bovine cells in tissue culture.
    • To investigate the dynamic behavior and regulation of cell surface GT.

    Main Methods:

    • Immunohistochemical techniques using a rabbit heteroantiserum against purified soluble GT.
    • Indirect immunofluorescence on fixed and living bovine cell lines.
    • Analysis of GT release and reappearance using trypsin digestion and cycloheximide treatment.

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    Main Results:

    • The GT antigen was detected on the surface of all three bovine cell lines tested.
    • The antigen was uniformly distributed on the membrane surface of fixed cells.
    • Exposure to anti-GT antibody induced time-dependent aggregation of the antigen on living cells.
    • Trypsin digestion released GT from the cell surface, and its reappearance was dependent on protein synthesis.

    Conclusions:

    • UDP-galactose:N-acetylglucosamine galactosyltransferase (GT) is a cell surface enzyme in bovine cells.
    • Cell surface GT exhibits dynamic behavior, including aggregation and turnover.
    • The presence and reappearance of cell surface GT are regulated by protein synthesis.