| First Author | Oppermann UC | Year | 1997 |
| Journal | Eur J Biochem | Volume | 249 |
| Issue | 2 | Pages | 355-60 |
| PubMed ID | 9370340 | Mgi Jnum | J:44470 |
| Mgi Id | MGI:1100255 | Doi | 10.1111/j.1432-1033.1997.t01-1-00355.x |
| Citation | Oppermann UC, et al. (1997) Function, gene organization and protein structures of 11beta-hydroxysteroid dehydrogenase isoforms. Eur J Biochem 249(2):355-60 |
| abstractText | Enzymatic interconversion of active and inactive glucocorticoid hormone is important, and is carried out physiologically by 11beta-hydroxysteroid dehydrogenase (11beta-HSD) isoforms, explaining their role in cellular and toxicological processes. Two forms of the enzyme, 11beta-HSD-1 and 11beta-HSD-2, belonging to the protein superfamily of short-chain dehydrogenases/reductases, have been structurally and functionally characterised. Although displaying dehydrogenase and reductase activities in vitro, the dominant in vivo function of the type-1 enzyme might be to work as a reductase, thus generating active cortisol from inactive cortisone precursors. On the other hand, for adrenal glucocorticoids the type-2 enzyme seems to be exclusively a dehydrogenase and, by inactivating glucocorticoids, confers specificity to peripheral mineralocorticoid receptors. |
