| First Author | Takeyama K | Year | 1997 |
| Journal | Science | Volume | 277 |
| Issue | 5333 | Pages | 1827-30 |
| PubMed ID | 9295274 | Mgi Jnum | J:43146 |
| Mgi Id | MGI:1097206 | Doi | 10.1126/science.277.5333.1827 |
| Citation | Takeyama K, et al. (1997) 25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis. Science 277(5333):1827-30 |
| abstractText | Renal 25-hydroxyvitamin D3 1alpha-hydroxylase [1alpha(OH)ase] catalyzes metabolic activation of 25-hydroxyvitamin D3 into 1alpha, 25-dihydroxyvitamin D3 [1alpha,25(OH)2D3], an active form of vitamin D, and is inhibited by 1alpha,25(OH)2D3. 1alpha(OH)ase, which was cloned from the kidney of mice lacking the vitamin D receptor (VDR-/- mice), is a member of the P450 family of enzymes (P450VD1alpha). Expression of 1alpha(OH)ase was suppressed by 1alpha, 25(OH)2D3 in VDR+/+ and VDR+/- mice but not in VDR-/- mice. These results indicate that the negative feedback regulation of active vitamin D synthesis is mediated by 1alpha(OH)ase through liganded VDR. |
