Bauman David R, Steckelbroeck Stephan, Penning Trevor M
Department of Pharmacology, University of Pennsylvania School of Medicine, 3620 Hamilton Walk, 135 John Morgan Building, Philadelphia, Pennsylvania 19104, USA.
Drug News Perspect. 2004 Nov;17(9):563-78. doi: 10.1358/dnp.2004.17.9.872570.
The human aldo-keto reductase 1C (AKR1C) isozymes are implicated in the pre-receptor regulation of steroid receptors, nuclear orphan receptors and membrane-bound ligand-gated ion channels. Human AKR members that may regulate the local concentration of steroid hormones include: AKR1C1, AKR1C2, AKR1C3, AKR1C4 and AKR1D1. Since, these enzymes are pluripotent, the physiological role for the human AKR1C isozymes is determined by their tissue-specific expression patterns and their substrate availability in target tissues. AKRs work in concert with short-chain dehydrogenases/reductases as switches to control ligand access to nuclear receptors. Consequently, they are potential targets in treating prostate cancer, breast cancer, endometriosis and endometrial cancer.
人类醛酮还原酶1C（AKR1C）同工酶参与类固醇受体、核孤儿受体和膜结合配体门控离子通道的受体前调节。可能调节类固醇激素局部浓度的人类AKR成员包括：AKR1C1、AKR1C2、AKR1C3、AKR1C4和AKR1D1。由于这些酶具有多能性，人类AKR1C同工酶的生理作用取决于它们的组织特异性表达模式及其在靶组织中的底物可用性。AKR与短链脱氢酶/还原酶协同作用，作为控制配体进入核受体的开关。因此，它们是治疗前列腺癌、乳腺癌、子宫内膜异位症和子宫内膜癌的潜在靶点。
