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Related Experiment Videos

Structural analyses of progesterone receptors.

K B Horwitz, L L Wei, M D Francis

    Journal of Steroid Biochemistry
    |January 1, 1986
    PubMed
    Summary

    Human breast cancer cells contain progesterone receptors with two proteins, A and B. These proteins undergo molecular weight changes upon hormone binding and nuclear translocation, indicating dynamic processing.

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    Area of Science:

    • Molecular Endocrinology
    • Cancer Cell Biology
    • Protein Biochemistry

    Background:

    • Progesterone receptors (PRs) are crucial in hormone-dependent cancers like breast cancer.
    • PRs exist as distinct A and B proteins with different functions.
    • Understanding PR dynamics is key to developing targeted therapies.

    Purpose of the Study:

    • To characterize the molecular weight and processing of progesterone receptors in T47Dco human breast cancer cells.
    • To investigate the structural relationship between the A and B progesterone receptor proteins.
    • To analyze the changes in PRs upon hormone binding and nuclear translocation.

    Main Methods:

    • In situ photoaffinity labeling with [3H]R5020.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
    • Immunoblotting with specific antibodies.
    • Cleveland mapping using S. aureaus V8 protease.

    Main Results:

    • Human PRs consist of equimolar A (85 kDa) and B (115 kDa) proteins, heavier than chick oviduct counterparts.
    • Untransformed B protein exists as a doublet (115/119 kDa); A protein is a singlet (85 kDa).
    • Nuclear translocation induces distinct molecular weight shifts in both A and B proteins, followed by their degradation without smaller fragments.

    Conclusions:

    • Progesterone receptors in human breast cancer cells exhibit dynamic molecular weight alterations post-hormone binding and nuclear entry.
    • The A and B proteins are structurally related, as evidenced by identical protease digestion patterns.
    • These findings provide insights into PR regulation and potential therapeutic targets in breast cancer.

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