| First Author | Penning TM | Year | 1996 |
| Journal | Steroids | Volume | 61 |
| Issue | 9 | Pages | 508-23 |
| PubMed ID | 8883217 | Mgi Jnum | J:35248 |
| Mgi Id | MGI:82700 | Doi | 10.1016/s0039-128x(96)00093-1 |
| Citation | Penning TM, et al. (1996) Mammalian 3 alpha-hydroxysteroid dehydrogenases. Steroids 61(9):508-23 |
| abstractText | Mammalian 3 alpha-hydroxysteroid dehydrogenases (3 alpha-HSDs) regulate steroid hormone levels. For example, hepatic 3 alpha-HSDs inactivate circulating androgens, progestins, and glucocorticoids. In target tissues they regulate access of steroid hormones to steroid hormone receptors. For example, in the prostate 3 alpha-HSD acts as a molecular switch and controls the amount of 5 alpha-dihydrotestosterone that can bind to the androgen receptor, while in the brain 3 alpha-HSD can regulate the amount of tetrahydrosteroids that can alter GABAa receptor function. Molecular cloning indicates that these mammalian 3 alpha-HSDs belong to the aldo-keto reductase superfamily and that they are highly homologous proteins. Using the three-dimensional structure of rat liver 3 alpha-HSD as a template for site-directed mutagenesis, details regarding structure function relationships, including catalysis and cofactor and steroid hormone recognition have been elucidated. These details may be relevant to all mammalian 3 alpha-HSDs. |
