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 theenzymes involved in steroid hormone biosynthesis since the lastcomprehensive review in 1988. Major developments include thecloning, identification, and characterization of multiple isoformsof 3ß-hydroxysteroid dehydrogenase, which play a criticalrole in the biosynthesis of all steroid hormones and 17ß-hydroxysteroiddehydrogenase where specific isoforms are essential for thefinal step in active steroid hormone biosynthesis. Advanceshave taken place in our understanding of the unique manner thatdetermines tissue-specific expression of P450aromatase throughthe utilization of alternative promoters. In recent years, evidencehas been obtained for the expression of steroidogenic enzymesin the nervous system and in cardiac tissue, indicating thatthese tissues may be involved in the biosynthesis of steroidhormones acting in an autocrine or paracrine manner. This reviewpresents a detailed description of the enzymes involved in thebiosynthesis of active steroid hormones, with emphasis on thehuman and mouse enzymes and their expression in gonads, adrenalglands, and placenta.
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