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Related Experiment Videos

LETS glycoprotein: arrangement and function at the cell surface.

R O Hynes, I U Ali, V M Mautner

    Birth Defects Original Article Series
    |January 1, 1978
    PubMed
    Summary
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    Large external transformation-sensitive (LETS) glycoprotein is crucial for normal cell adhesion. Its absence in transformed cells suggests a role in cell morphology and attachment, with potential therapeutic implications.

    Area of Science:

    • Cell Biology
    • Biochemistry
    • Molecular Biology

    Background:

    • Large external transformation-sensitive (LETS) glycoprotein is a surface protein found on normal fibroblasts.
    • LETS protein is absent or present in low amounts on transformed cells.
    • LETS protein forms disulfide-bonded aggregates on the cell surface.

    Purpose of the Study:

    • To investigate the role of LETS glycoprotein in cell adhesion and morphology.
    • To determine the effects of LETS protein addition on transformed cells.
    • To explore the mechanisms regulating LETS protein function.

    Main Methods:

    • Immunofluorescent staining to visualize LETS protein distribution.
    • Disulfide bond reduction and cytochalasin B treatment to study LETS protein release.

    Related Experiment Videos

  • Addition of purified LETS protein to transformed cells.
  • Inhibition studies using antisera and proteolysis.

    • Main Results:

    • LETS protein is localized in fibrils around normal fibroblasts, concentrated beneath cells and between them.
    • Disulfide bond reduction and cytochalasin B increase LETS protein release.
    • Purified LETS protein binds to transformed cells, restoring normal cell attachment, spreading, and alignment.
    • LETS protein induces actin cable formation in transformed cells.
    • Antisera and disulfide bond reduction inhibit LETS protein's effects; proteolysis blocks or reverses them.

    Conclusions:

    • LETS glycoprotein plays a significant role in cell adhesion.
    • Restoring LETS protein on transformed cells can partially normalize their morphology and behavior.
    • Disulfide bonding is critical for LETS protein's function and cell surface localization.