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Glucocorticoid-binding proteins in rat liver

J A Gustafsson, J Carlstedt-Duke, S Okret

    European Journal of Respiratory Diseases. Supplement
    |January 1, 1982
    PubMed
    Summary

    Male rats show higher corticosterone levels in liver cell nuclei than females. The glucocorticoid receptor exists in multiple forms and binds selectively to specific DNA fragments.

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    Glucocorticoid receptor abnormalities in fibroblasts from patients with idiopathic resistance to dexamethasone diagnosed when evaluated for adrenocortical disorders.

    The Journal of clinical endocrinology and metabolism·1992

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Biochemistry

    Background:

    • Corticosterone is a key glucocorticoid hormone.
    • Glucocorticoid receptors (GRs) mediate hormone action.
    • Understanding GR distribution and function is crucial for hormone signaling research.

    Purpose of the Study:

    • To investigate the time- and sex-dependent distribution and metabolism of corticosterone in rat liver.
    • To characterize the protein binding and biological activity of corticosterone metabolites.
    • To elucidate the structural forms and DNA-binding properties of the glucocorticoid receptor.

    Main Methods:

    • Radioisotope labeling ([3H] corticosterone and [3H] dexamethasone) and tissue distribution studies.
    • Chromatographic techniques (including biospecific adsorption chromatography) for receptor purification.
    • Enzymatic treatment and analysis of receptor forms.
    • Antibody generation and cross-reactivity studies.
    • In vitro DNA-binding assays.

    Main Results:

    • Maximum [3H] corticosterone recovery in rat liver cell nuclei was observed at 5 minutes post-injection, with males exhibiting ten times higher radioactivity than females.
    • Identified nuclear radioactivity as unmetabolized corticosterone and 5 alpha-dihydrocorticosterone, the latter showing low biological activity.
    • Glucocorticoid receptor exists in two major forms (Stokes radii 6.1 nm and 3.6 nm) that are interconvertible and can be further processed.
    • Purification of the 6.1 nm GR form was achieved using biospecific adsorption chromatography.
    • Specific antibodies against the GR were generated and showed cross-reactivity with human GR from various cell types.
    • Activated GR selectively binds to mouse mammary tumor virus DNA but not to bacterial or phage DNA.

    Conclusions:

    • Sex differences exist in corticosterone uptake and distribution in rat liver nuclei.
    • The glucocorticoid receptor undergoes structural changes and exhibits specific DNA-binding properties.
    • The developed purification and antibody-based methods facilitate further GR research.
    • Selective GR-DNA interaction suggests a role in gene regulation specific to viral DNA elements.

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