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Insulin binding on cultured chick muscle cells: decrease in binding associated with cell fusion.

S L Nissen, A H Trenkle, P J Bechtel

    Hormone and Metabolic Research = Hormon- Und Stoffwechselforschung = Hormones Et Metabolisme
    |June 1, 1984
    PubMed
    Summary
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    This study investigated insulin binding to embryonic chick skeletal muscle cells, finding that both bovine and chicken insulin bind with high and low affinities. Insulin receptor numbers decrease with increased cell fusion, impacting binding.

    Area of Science:

    • Endocrinology
    • Cell Biology
    • Biochemistry

    Background:

    • Insulin is a key metabolic hormone regulating glucose homeostasis.
    • Understanding insulin receptor dynamics is crucial for comprehending cellular responses to insulin.

    Purpose of the Study:

    • To characterize the binding kinetics of bovine and chicken insulin to cultured embryonic chick skeletal muscle cells.
    • To investigate the relationship between insulin receptor expression and cell differentiation.

    Main Methods:

    • Radioligand binding assays using 125I-labeled bovine and chicken insulin.
    • Incubation of cultured embryonic chick skeletal muscle cells at 20°C for varying durations.
    • Quantification of insulin binding in relation to nuclei number and cell fusion.

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    Main Results:

    • Both bovine and chicken insulin exhibited high and low affinity binding to the cells.
    • Optimal insulin binding occurred after 90 minutes of incubation and was maintained for 3 hours.
    • Insulin binding increased linearly with nuclei number, but decreased with increased cell fusion due to a reduction in low-affinity receptors.

    Conclusions:

    • Embryonic chick skeletal muscle cells possess high- and low-affinity insulin receptors.
    • Cell fusion significantly impacts insulin receptor expression, specifically reducing low-affinity receptor numbers.
    • These findings provide insights into the regulation of insulin sensitivity during muscle development.