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Related Experiment Videos

Specific rosette formation between fibroblasts and erythrocytes

S D Rosen, M S Singer, C G Glabe

    Journal of Cell Science
    |October 1, 1981
    PubMed
    Summary

    Fibroblast cells form rosettes by binding to specific erythrocytes. Ox erythrocyte glycolipids act as receptors for baby hamster kidney cell binding sites, indicating a role in cell-surface carbohydrate recognition.

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    Area of Science:

    • Cell Biology
    • Biochemistry
    • Glycobiology

    Background:

    • Fibroblast cell lines exhibit specific binding to erythrocytes, forming rosettes.
    • This cell-specific binding varies between different cell lines.
    • Baby hamster kidney (BHK) cells demonstrate this binding in both suspended and monolayer cultures.

    Purpose of the Study:

    • To investigate the molecular mechanisms underlying rosette formation between BHK cells and trypsinized-ox (TOx) erythrocytes.
    • To identify the specific molecules on ox erythrocytes responsible for binding to BHK cells.

    Main Methods:

    • Protease treatment of BHK cells to assess the role of proteins in binding.
    • Inhibition assays using simple saccharides and glycopeptides from ox erythrocytes.
    • Testing neutral glycosphingolipids from ox and rabbit erythrocytes for inhibitory effects.
    • Incorporation of ox glycolipids into guinea-pig erythrocytes to assess their adhesive properties.

    Main Results:

    • Protease treatment of BHK cells dose- and time-dependently reduced their ability to bind TOx erythrocytes.
    • Simple saccharides and glycopeptides did not inhibit rosette formation.
    • Neutral glycosphingolipids from ox erythrocytes inhibited BHK-TOx rosetting, while those from rabbit erythrocytes did not.
    • Incorporation of ox glycolipids into guinea-pig erythrocytes induced adhesion to BHK cells.

    Conclusions:

    • Specific glycolipids on ox erythrocytes serve as receptors for binding sites on BHK cell surfaces.
    • These findings suggest a role for cell-specific glycolipid-protein interactions in cell-surface carbohydrate recognition events.

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