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Decrease of hormone binding capacity of estrogen receptor by calcium

Y Maaroufi1, A Ben Hardouze, G Leclercq

  • 1Laboratoire J.-C. Heuson de Cancérologie Mammaire, Service de Médecine Interne, Institut Jules Bordet, Brussels, Belgium.

Journal of Receptor and Signal Transduction Research
|November 20, 1997
PubMed
Summary
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Calcium ions significantly reduce estrogen receptor (ER) binding capacity without affecting affinity. This effect, observed with recombinant ER, suggests calcium interacts with phosphoamino acid residues in the hormone-binding domain.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Biochemistry

Background:

  • Estrogen receptor (ER) plays a crucial role in cellular processes.
  • The influence of calcium ions on ER binding properties requires clarification.
  • Recombinant ER systems offer a controlled environment to study ER-ligand interactions.

Purpose of the Study:

  • To investigate the effect of calcium (Ca++) on the binding characteristics of the estrogen receptor (ER).
  • To determine if calcium influences the binding capacity or affinity of ER for estradiol.
  • To elucidate the mechanism by which calcium might affect ER function.

Main Methods:

  • Utilized a human recombinant full-length ER (yER) expressed in yeast.
  • Assessed [3H]estradiol ([3H]E2) binding capacity and affinity in the presence of varying Ca++ concentrations (0.1-10 mM).

Related Experiment Videos

  • Employed size-exclusion chromatography, immunoreactivity assays with monoclonal antibodies, and binding studies with specific ER ligands and EDTA.

    • Main Results:

    • Calcium ions caused a significant loss of [3H]E2 binding capacity in a dose-dependent manner.
    • Calcium did not alter the hormone binding affinity of the remaining ER.
    • The effect was localized to the hormone-binding domain and reversed by EDTA, suggesting no proteolysis.
    • Calcium's effect was partially antagonized by phosphoamino acids, indicating potential interaction with phosphorylated residues.

    Conclusions:

    • Calcium ions negatively regulate the binding capacity of the estrogen receptor.
    • The interaction appears to occur at the hormone-binding domain, potentially involving phosphoamino acid residues.
    • These findings provide new insights into the post-translational regulation of ER function by divalent cations.