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25-Hydroxyvitamin D 3 1α-Hydroxylase and Vitamin D Synthesis
Abstract
Renal 25–hydroxyvitamin D 3 1α-hydroxylase [1α(OH)ase] catalyzes metabolic activation of 25–hydroxyvitamin D 3 into 1α,25–dihydroxyvitamin D 3 [1α,25(OH) 2 D 3 ], an active form of vitamin D, and is inhibited by 1α,25(OH) 2 D 3 . 1α(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 (P450 VD1 α ). Expression of 1α(OH)ase was suppressed by 1α,25(OH) 2 D 3 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 1α(OH)ase through liganded VDR.
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Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., et al. (1995) · Science · doi:10.1126/science.270.5241.1491 · Cited by 1,964
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Vitamin D metabolism, mechanism of action, and clinical applications
Bikle, D. D. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.016 · Cited by 1,933
Vitamin D and Human Health: Lessons from Vitamin D Receptor Null Mice
Bouillon, R., Carmeliet, G., Verlinden, L., van Etten, E., Verstuyf, A., Luderer, H. F., Lieben, L., Mathieu, C., & Demay, M. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0004 · Cited by 1,783
Rosenfeld, M. G., Lunyak, V. V., & Glass, C. K. (2006) · Genes & Development · doi:10.1101/gad.1424806 · Cited by 952
Overview of nomenclature of nuclear receptors
Germain, P., Staels, B., Dacquet, C., Spedding, M., & Laudet, V. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.4.2 · Cited by 688
Human cytochromes P450 in health and disease
Nebert, D. W., Wikvall, K., & Miller, W. L. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2012.0431 · Cited by 505
Metadata
- Authors
- Takeyama, K.-I., Kitanaka, S., Sato, T., Kobori, M., Yanagisawa, J., & Kato, S.
- Venue
- Science
- Published
- 1997-09-19
- Volume
- 277
- Issue
- 5333
- Pages
- 1827-1830
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2018381121
- Cited by
- 538
- References
- 1
- FWCI
- 18.75
- Type
- journal article
- Language
- en
- Open access
- closed
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