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Endocrine Reviews 25 (6): 947-970
Copyright © 2004 by The Endocrine Society

Overview of Steroidogenic Enzymes in the Pathway from Cholesterol to Active Steroid Hormones

Anita H. Payne and Dale B. Hales

Division of Reproductive Biology (A.H.P.), Department of Obstetrics and Gynecology, Stanford University School of Medicine, Stanford, California 94305; and Department of Physiology and Biophysics (D.B.H.), University of Illinois at Chicago, Chicago, Illinois 60612

Correspondence: Address all correspondence and requests for reprints to: Anita H. Payne, Division of Reproductive Biology, Department of Obstetrics and Gynecology, Stanford University School of Medicine, 300 Pasteur Drive, Stanford, California 94305-5317. E-mail: anita.payne{at}stanford.edu

Significant advances have taken place in our knowledge of the enzymes involved in steroid hormone biosynthesis since the last comprehensive review in 1988. Major developments include the cloning, identification, and characterization of multiple isoforms of 3ß-hydroxysteroid dehydrogenase, which play a critical role in the biosynthesis of all steroid hormones and 17ß-hydroxysteroid dehydrogenase where specific isoforms are essential for the final step in active steroid hormone biosynthesis. Advances have taken place in our understanding of the unique manner that determines tissue-specific expression of P450aromatase through the utilization of alternative promoters. In recent years, evidence has been obtained for the expression of steroidogenic enzymes in the nervous system and in cardiac tissue, indicating that these tissues may be involved in the biosynthesis of steroid hormones acting in an autocrine or paracrine manner. This review presents a detailed description of the enzymes involved in the biosynthesis of active steroid hormones, with emphasis on the human and mouse enzymes and their expression in gonads, adrenal glands, and placenta.




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