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Related Experiment Videos

Microsomal dexamethasone binding sites identified by affinity labelling.

E C LaCasse1, G M Howell, Y A Lefebvre

  • 1Department of Medicine, University of Ottawa, Moses and Rose Loeb Medical Research Institute, Ottawa Civic Hospital, Ontario, Canada.

Journal of Steroid Biochemistry
|January 1, 1990
PubMed
Summary
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Researchers identified novel dexamethasone binding sites in male rat liver microsomes, distinct from the known glucocorticoid receptor. These sites, located in the endoplasmic reticulum, involve a 45 kDa peptide doublet whose function requires further investigation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Glucocorticoids play crucial roles in various physiological processes.
  • The cytosolic glucocorticoid receptor is well-characterized, but extranuclear binding sites may also exist.
  • Understanding non-genomic effects of glucocorticoids requires identification of their cellular targets.

Purpose of the Study:

  • To characterize novel binding sites for [3H]dexamethasone in male rat liver microsomes.
  • To determine the molecular identity and subcellular localization of these binding sites.
  • To differentiate these sites from the classical cytosolic glucocorticoid receptor.

Main Methods:

  • Radioligand binding assays using [3H]dexamethasone.
  • Scatchard analysis and competition studies with various steroids.

Related Experiment Videos

  • Immunoblotting with an anti-glucocorticoid receptor antibody.
  • Affinity labeling with [3H]dexamethasone 21-mesylate.
  • Isopycnic centrifugation of microsomal subfractions.

    • Main Results:

    • A class of glucocorticoid- and progestin-specific binding sites was identified in male rat liver microsomes.
    • These sites are distinct from the cytosolic glucocorticoid receptor based on binding parameters and antibody recognition.
    • Affinity labeling revealed two specifically labeled peptides: ~66 kDa (likely serum contamination) and a 45 kDa doublet.
    • The 45 kDa doublet, absent in serum, exhibited binding characteristics identical to the identified microsomal binding sites.
    • Binding sites were localized to the endoplasmic reticulum.

    Conclusions:

    • Male rat liver microsomes possess a distinct class of dexamethasone binding sites.
    • These sites are associated with a 45 kDa peptide doublet located in the endoplasmic reticulum.
    • The precise identity and physiological role of this 45 kDa peptide doublet warrant further investigation.