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Characterization of specific steroid binding in human amnion at term
Biology of Reproduction
|September 1, 1982
Summary
This study found that a protein in human fetal membranes binds cortisol and corticosterone with higher affinity than progesterone. This suggests the protein may be involved in glucocorticoid metabolism, not progesterone withdrawal, during labor onset.
Area of Science:
- Reproductive biology
- Endocrinology
- Biochemistry
Background:
- Human fetal membranes play a role in labor onset.
- A progesterone-binding protein in these membranes has been implicated in labor initiation.
Purpose of the Study:
- To quantitatively characterize specific steroid binding in human fetal membranes.
- To investigate the binding affinity and characteristics of steroid-binding proteins in the amnion.
Main Methods:
- Cytosol from human amnion was prepared and extracted.
- Specific binding of cortisol and progesterone was measured using a charcoal assay.
- Steroid competition assays were performed to determine binding affinities.
Main Results:
- The amnion cytosol exhibited high-affinity binding for cortisol (KD = 1 nM) and a large number of binding sites.
- Progesterone binding showed a 10-fold lower affinity (KD = 12 nM) compared to cortisol.
- Cortisol binding was stable, reversible, and showed higher affinity for cortisol and corticosterone than progesterone.
Conclusions:
- The steroid-binding protein in human amnion at term has a higher affinity for cortisol and corticosterone than progesterone.
- This suggests a potential role in glucocorticoid metabolism rather than progesterone withdrawal in labor onset.
- Findings challenge previous hypotheses regarding the protein's function in initiating labor.