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Cortisol binding in rat skeletal muscle.

M Mayer, N Kaiser, R J Milholland

    The Journal of Biological Chemistry
    |February 25, 1975
    PubMed
    Summary
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    This study identifies a specific [3H]cortisol-binding protein in rat muscle cytosol. This binding protein does not correlate with glucocorticoid potency, suggesting it

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Endocrinology

    Background:

    • Glucocorticoids play crucial roles in skeletal muscle physiology.
    • Understanding glucocorticoid binding in muscle is essential for elucidating their mechanisms of action.

    Purpose of the Study:

    • To characterize the specific binding of [3H]cortisol in rat gastrocnemius muscle cytosol.
    • To investigate the nature and properties of the [3H]cortisol-binding molecule.

    Main Methods:

    • In vitro incubation of rat gastrocnemius muscle cytosol with [3H]cortisol.
    • Sucrose density gradient centrifugation to determine sedimentation properties.
    • Competition assays with various steroids to assess binding specificity.

    Main Results:

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    • Specific [3H]cortisol binding was observed in the 27,000 x g supernatant fraction at 0°C.
    • The binding molecule exhibited a Kd of 1.7 x 10^-7 M and approximately 0.99 pmol/mg cytosol protein binding sites.
    • Binding increased in adrenalectomized rats and decreased with cortisol pretreatment.
    • Steroid competition assays revealed a lack of correlation with glucocorticoid potency, with progesterone inhibiting binding but not dexamethasone or triamcinolone acetonide.

    Conclusions:

    • The [3H]cortisol-binding protein in muscle cytosol may not be directly involved in the biological effects of potent glucocorticoids.
    • The properties of this binding protein are similar to rat plasma corticosteroid-binding globulin, making definitive distinction challenging.