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Published on: August 2, 2017
Aromatase and steroid sulfatase from human placenta
1Department of Pharmacology, State University of New York Upstate Medical University, Syracuse, NY, United States.
This study details the extraction and purification of two key human estrogen-biosynthesizing enzymes: Cytochrome P450 aromatase (AROM) and steroid sulfatase (STS). Procedures and activity assays are described for these critical enzymes involved in hormone balance and disease treatment.
Area of Science:
- Biochemistry
- Endocrinology
- Molecular Biology
Background:
- Cytochrome P450 aromatase (AROM) and steroid sulfatase (STS) are crucial enzymes in human estrogen biosynthesis and maintaining androgen-estrogen balance.
- AROM converts androgens to estrogens, while STS hydrolyzes steroid sulfates, yielding precursors for potent sex hormones.
- Local expression of these enzymes is vital for reproductive steroid levels, making them therapeutic targets for hormone-related diseases.
Approach:
- Detailed review of extraction and purification procedures for human AROM and STS from term placenta.
- Description of established activity assays for quantifying AROM and STS enzyme function.
- Focus on methodologies developed over six decades of research.
Key Points:
- AROM is an Fe-heme cytochrome P450 enzyme catalyzing androgen to estrogen conversion.
- STS is a Ca2+-dependent enzyme hydrolyzing steroid sulfates to produce estrogen and androgen precursors.
- Both enzymes are integral endoplasmic reticulum membrane proteins.
Conclusions:
- Understanding AROM and STS function and purification is essential for developing treatments for hormone-dependent diseases.
- These enzymes are significant drug targets for conditions like breast and prostate cancer, and endometriosis.
- Continued research into AROM and STS is vital for advancing reproductive endocrinology and therapeutics.
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