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Steroid 21-sulfatase activity in human placenta
Journal of Steroid Biochemistry
|May 1, 1983
Summary
Steroid 21-sulfatase activity is present in human placenta, hydrolyzing fetal deoxycorticosterone sulfate. This placental enzyme may explain elevated maternal deoxycorticosterone levels during pregnancy.
Area of Science:
- Biochemistry
- Endocrinology
- Reproductive Biology
Background:
- Deoxycorticosterone sulfate (DOCS) is abundant in fetal plasma.
- DOCS is not metabolized via deoxycorticosterone (DOC) in non-pregnant humans, suggesting low steroid 21-sulfatase activity.
- Hydrolysis of DOCS has been observed in the human placenta.
Purpose of the Study:
- To investigate the presence and characteristics of steroid 21-sulfatase activity in human placenta.
- To determine if placental steroid 21-sulfatase can hydrolyze fetal DOCS.
Main Methods:
- Preparation of microsome-enriched fractions from human placental tissue.
- Assay of steroid 21-sulfatase activity using [3H]-deoxycorticosterone sulfate.
- Determination of enzyme kinetics, including Michaelis constant (KM).
Main Results:
- Steroid 21-sulfatase activity was detected in human placental microsomes.
- Reaction conditions were optimized for linearity with time and protein concentration.
- The apparent KM for deoxycorticosterone sulfate was determined to be 100 microM.
Conclusions:
- Human placenta possesses active steroid 21-sulfatase.
- Placental hydrolysis of fetal DOCS could lead to DOC secretion into maternal circulation.
- This placental pathway may contribute to high maternal DOC levels in late pregnancy.