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Related Experiment Videos

Alterations in membrane permeability with trypsin treatment

P A Johnson, R M Johnstone

    Canadian Journal of Biochemistry
    |August 1, 1981
    PubMed
    Summary

    Trypsin treatment disrupts amino acid transport in Ehrlich cells by altering membrane permeability and abolishing ion gradients. Recovery is possible with serum or calcium, independent of protein synthesis.

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    Area of Science:

    • Cell biology
    • Membrane transport
    • Biochemistry

    Background:

    • Sodium-coupled amino acid transport is crucial for cellular function.
    • Ehrlich cells are a model system for studying cellular transport mechanisms.
    • Trypsin is an enzyme that can modify cell surface proteins and affect cell viability.

    Purpose of the Study:

    • To investigate the effects of trypsin treatment on amino acid transport in Ehrlich cells.
    • To elucidate the mechanisms underlying the observed reduction in transport activity.
    • To identify factors involved in the recovery of transport function.

    Main Methods:

    • Treatment of Ehrlich cells with trypsin.
    • Measurement of sodium-coupled amino acid transport rates.
    • Assessment of intracellular ATP levels and cation gradients.
    • Preparation and transport assays using cell-derived vesicles.
    • Incubation of treated cells with serum, cycloheximide, calcium, and glucose.

    Main Results:

    • Trypsin treatment reduced amino acid transport, ATP levels, and cation gradients.
    • The decrease in transport was linked to altered membrane permeability due to released DNA.
    • Vesicles showed normal transport, indicating ion gradients were essential.
    • Serum restored membrane permeability, and calcium facilitated recovery of glycine transport.

    Conclusions:

    • Trypsin-induced DNA release alters Ehrlich cell membrane permeability, inhibiting sodium-coupled amino acid transport.
    • Restoration of transport function depends on membrane integrity and ion gradients, with calcium playing a key role.
    • Recovery mechanisms are independent of de novo protein synthesis.

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