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Related Experiment Videos

Recognition at cell surfaces: phytohaemagglutinin-lymphocyte interaction.

M J Crumpton, D Allan, J Auger

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |November 6, 1975
    PubMed
    Summary
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    Lymphocyte activation by Phaseolus vulgaris phytohaemagglutinin (PHA) involves specific glycoprotein receptors. PHA binding likely increases cell membrane permeability to calcium ions (Ca2+), initiating activation.

    Area of Science:

    • Cell Biology
    • Immunology
    • Biochemistry

    Background:

    • Cellular behavior is regulated by ligand-receptor interactions on the cell surface.
    • Receptors are typically membrane proteins, often glycoproteins.
    • Information transmission across the cell membrane is crucial for cellular regulation.

    Purpose of the Study:

    • To investigate the molecular basis of receptor-ligand interactions.
    • To understand the molecular consequences of receptor-ligand binding.
    • To use lymphocyte activation by Phaseolus vulgaris phytohaemagglutinin (PHA) as a model system.

    Main Methods:

    • Characterization of the PHA receptor on lymphocytes.
    • Solubilization and molecular size determination of the PHA-receptor complex.

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  • Investigation of early events in lymphocyte activation.

    • Main Results:

    • Lymphocyte activation by PHA is mediated by a specific glycoprotein receptor (approx. 3 x 10^4 molecules/cell).
    • The PHA-receptor complex has a molecular size of approx. 3 x 10^5.
    • The primary event in PHA-induced lymphocyte activation is likely an increase in Ca2+ permeability.

    Conclusions:

    • PHA binding leads to the cross-linking ('patching') of its specific glycoprotein receptor.
    • This receptor patching may form a polar channel, facilitating Ca2+ influx.
    • Increased intracellular Ca2+ is a probable initial step in lymphocyte activation by PHA.