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Relationship between negative cooperativity and insulin action

J M Olefsky, A Green, T P Ciaraldi

    Biochemistry
    |July 21, 1981
    PubMed
    Summary
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    Porcine insulin enhances insulin receptor dissociation, but the [LeuB25]insulin analogue does not. Despite this, [LeuB25]insulin fully stimulates glucose transport, indicating dissociation is not essential for insulin's metabolic action.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Endocrinology

    Background:

    • Insulin binding to its receptor triggers cellular responses.
    • Native insulin's dissociation from its receptor is influenced by receptor occupancy.
    • Understanding insulin's mechanism of action is crucial for metabolic research.

    Purpose of the Study:

    • To compare porcine insulin and [LeuB25]insulin's effects on insulin receptor dissociation.
    • To investigate the relationship between receptor dissociation and glucose transport.
    • To determine if receptor dissociation is a prerequisite for insulin's metabolic activity.

    Main Methods:

    • Comparing [125I]insulin dissociation rates from lymphocytes and adipocytes with porcine insulin and [LeuB25]insulin.
    • Measuring adipocyte glucose transport and oxidation rates.

    Related Experiment Videos

  • Assessing receptor occupancy and binding affinity.

    • Main Results:

    • Porcine insulin significantly enhanced [125I]insulin dissociation, while [LeuB25]insulin did not.
    • [LeuB25]insulin fully stimulated adipocyte glucose transport and oxidation despite lower binding affinity.
    • The rate of glucose transport activation by [LeuB25]insulin was comparable to native insulin.

    Conclusions:

    • The enhanced dissociation of native insulin is likely due to negative cooperative interactions between occupied receptors.
    • [LeuB25]insulin acts as a noncooperative analogue.
    • Full biological activity of insulin, including glucose transport, can be achieved without enhancing receptor dissociation.