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Departments of Pathology, Pediatrics, and Biological Chemistry, School of Medicine Torrance, California 90509
The Howard Hughes Medical Institute, School of Medicine, Harbor-University of California-Los Angeles Medical Center Torrance, California 90509
Address requests for reprints to: Dr. Eduardo C. Salido, Department of Pathology, Harbor-University of California-Los Angeles Medical Center, 1000 West Carson Street, Torrance, California 90509.
Steroid sulfatase (STS), an important enzyme in the pathway of estrogen synthesis from sulfated steroid precursors, was localized to the syncytial trophoblast of human placentas during different periods of pregnancy by using a mouse monoclonal antibody and immunocytochemical techniques. Preembedding immunoelectron microscopy revealed STS immunoreactivity associated with the rough endoplasmic reticulum of the syncytial trophoblast. STS mRNA was also localized to this outermost layer of the human trophoblast. At a cellular level, both STS message and immunoreactivity seemed to be more abundant during the late first and early second trimesters than in term placentas. Although the syncytial trophoblast is known to originate from the cytotrophoblast, neither STS immunoreactivity nor STS mRNA was detected in the cytotrophoblast at any stage of placental development studied.
* This work was supported by NHLBI Grant RO1-HL-18340, NIH Grant ROl-HD-12178, and the Howard Hughes Medical Institute.
Received November 13, 1989.
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