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Cell surface galactosyltransferase as a recognition molecule during development.

E M Bayna, R B Runyan, N F Scully

    Molecular and Cellular Biochemistry
    |November 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

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    Cell surface galactosyltransferase (GalTase) acts as a receptor, mediating key developmental cell interactions. This enzyme

    Area of Science:

    • Developmental Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Cellular interactions during development are partly mediated by cell surface galactosyltransferase (GalTase) binding to lactosaminoglycan (LAG) substrates.
    • Previous studies identified a regulatory defect in surface GalTase activity in mouse morphogenetic mutations within the T/t-complex.
    • This suggests a unique role for surface GalTase in T/t-complex-influenced cell interactions.

    Purpose of the Study:

    • To investigate the function of surface GalTase in cellular interactions.
    • To explore the role of GalTase in processes regulated by T/t-complex alleles.
    • To examine GalTase expression during spermatogenesis and after the acrosome reaction.

    Main Methods:

    • Multidisciplinary approach utilizing genetic, biochemical, and immunological probes.

    Related Experiment Videos

  • Analysis of surface GalTase activity in morphogenetically abnormal mouse cells.
  • Examination of GalTase expression during spermatogenesis and acrosome reaction.

    • Main Results:

    • Galactosyltransferase (GalTase) functions as a cell surface receptor in fertilization, embryonic cell adhesion, and migration.
    • Specific defect in surface GalTase regulation observed in T/t-complex mutant mouse cells.
    • GalTase expression and fate during spermatogenesis and acrosome reaction were studied.

    Conclusions:

    • Galactosyltransferase (GalTase) plays a crucial role as a cell surface receptor in developmental cell interactions.
    • These interactions are significantly influenced by T/t-complex alleles.
    • Further research supports GalTase's function in processes regulated by the T/t-complex.