References

Auchus, R.J. (2017). Steroid 17-hydroxylase and 17,20-lyase deficiencies, genetic and pharmacologic. J. Steroid Biochem. Mol. Biol. 165, 71–78.10.1016/j.jsbmb.2016.02.002Search in Google Scholar

Balmer, J.E. and Blomhoff, R. (2002). Gene expression regulation by retinoic acid. J. Lipid Res. 43, 1773–1808.10.1194/jlr.R100015-JLR200Search in Google Scholar

Bernhardt, R. (2005). Cytochromes P-450. In: Encyclopedia of Biological Chemistry, W. Lennarz, M. Lane, P. Modrich, J. Dixon, E. Carafoli, J. Exton, and D. Cleveland, eds. (Cambridge, MA: Academic Press), pp. 544–549.Search in Google Scholar

Bernhardt, R. and Urlacher, V.B. (2014). Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations. Appl. Microbiol. Biotechnol. 98, 6185–6203.10.1007/s00253-014-5767-7Search in Google Scholar

Broulik, P.D., Vondrova, J., Ruzicka, P., Sedlacek, R., and Zima, T. (2010). The effect of chronic alcohol administration on bone mineral content and bone strength in male rats. Physiol. Res. 59, 599–604.10.33549/physiolres.931799Search in Google Scholar

Carpenter, T.O. (2017). CYP24A1 loss of function: clinical phenotype of monoallelic and biallelic mutations. J. Steroid Biochem. Mol. Biol. doi: 10.1016/j.jsbmb.2017.01.006. [Epub ahead of print].Search in Google Scholar

Chen, J.R., Haley, R.L., Hidestrand, M., Shankar, K., Liu, X., Lumpkin, C.K., Simpson, P.M., Badger, T.M., and Ronis, M.J. (2006). Estradiol protects against ethanol-induced bone loss by inhibiting up-regulation of receptor activator of nuclear factor-κB ligand in osteoblasts. J. Pharmacol. Exp. Ther. 319, 1182–1190.10.1124/jpet.106.109454Search in Google Scholar

Chien, Y., Rosal, K., and Chung, B.C. (2017). Function of CYP11A1 in the mitochondria. Mol. Cell Endocrinol. 441, 55–61.10.1016/j.mce.2016.10.030Search in Google Scholar

Czekanska, E.M., Stoddart, M.J., Richards, R.G., and Hayes, J.S. (2012). In search of an osteoblast cell model for in vitro research. Eur. Cell Mater. 24, 1–17.10.22203/eCM.v024a01Search in Google Scholar

Dauber, A., Nguyen, T.T., Sochett, E., Cole, D.E., Horst, R., Abrams, S.A., Carpenter, T.O., and Hirschhorn, J.N. (2012). Genetic defect in CYP24A1, the vitamin D 24-hydroxylase gene, in a patient with severe infantile hypercalcemia. J. Clin. Endocrinol. Metab. 97, E268–274.10.1210/jc.2011-1972Search in Google Scholar

Ducy, P., Zhang, R., Geoffroy, V., Ridall, A.L., and Karsenty, G. (1997). Osf2/Cbfa1: a transcriptional activator of osteoblast differentiation. Cell 89, 747–754.10.1016/S0092-8674(00)80257-3Search in Google Scholar

Ekstrom, G. and Ingelman-Sundberg, M. (1989). Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450 (P-450IIE1). Biochem. Pharmacol. 38, 1313–1319.10.1016/0006-2952(89)90338-9Search in Google Scholar

Enjuanes, A., Garcia-Giralt, N., Supervia, A., Nogues, X., Ruiz-Gaspa, S., Bustamante, M., Mellibovsky, L., Grinberg, D., Balcells, S., and Diez-Perez, A. (2005). Functional analysis of the I.3, I.6, pII and I.4 promoters of CYP19 (aromatase) gene in human osteoblasts and their role in vitamin D and dexamethasone stimulation. Eur. J. Endocrinol. 153, 981–988.10.1530/eje.1.02032Search in Google Scholar

Gennari, L., Nuti, R., and Bilezikian, J.P. (2004). Aromatase activity and bone homeostasis in men. J. Clin. Endocrinol. Metab. 89, 5898–5907.10.1210/jc.2004-1717Search in Google Scholar

Gorsky, L.D., Koop, D.R., and Coon, M.J. (1984). On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction. J. Biol. Chem. 259, 6812–6817.10.1016/S0021-9258(17)39800-9Search in Google Scholar

Guengerich, F.P. (2001a). Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14, 611–650.10.1021/tx0002583Search in Google Scholar

Guengerich, F.P. (2001b). Uncommon P450-catalyzed reactions. Curr. Drug. Metab. 2, 93–115.10.2174/1389200013338694Search in Google Scholar

Guengerich, F.P. (2017). Intersection of the roles of cytochrome P450 enzymes with xenobiotic and endogenous substrates: relevance to toxicity and drug interactions. Chem. Res. Toxicol. 30, 2–12.10.1021/acs.chemrestox.6b00226Search in Google Scholar

Hannemann, F., Bichet, A., Ewen, K.M., and Bernhardt, R. (2007). Cytochrome P450 systems-biological variations of electron transport chains. Biochim. Biophys. Acta. 1770, 330–344.10.1016/j.bbagen.2006.07.017Search in Google Scholar

Hodges, V.M., Molloy, G.Y., and Wickramasinghe, S.N. (2000). Demonstration of mRNA for five species of cytochrome P450 in human bone marrow, bone marrow-derived macrophages and human haemopoietic cell lines. Br. J. Haematol. 108, 151–156.10.1046/j.1365-2141.2000.01816.xSearch in Google Scholar

Holick, M.F. (2017). The vitamin D deficiency pandemic: approaches for diagnosis, treatment and prevention. Rev. Endocr. Metab. Disord. 18, 153–165.10.1007/s11154-017-9424-1Search in Google Scholar

Huang, N., Pandey, A.V., Agrawal, V., Reardon, W., Lapunzina, P.D., Mowat, D., Jabs, E.W., Van Vliet, G., Sack, J., Fluck, C.E., et al. (2005). Diversity and function of mutations in p450 oxidoreductase in patients with Antley-Bixler syndrome and disordered steroidogenesis. Am. J. Hum. Genet. 76, 729–749.10.1086/429417Search in Google Scholar

Janssen, J.M.M.F., Bland, R., Hewison, M., Coughtrie, M.W.H., Sharp, S., Arts, J., Pols, H.A. P., and van Leeuwen, J.P.T.M. (1999). Estradiol formation by human osteoblasts via multiple pathways: Relation with osteoblast function. J. Cell Biochem. 75, 528–537.10.1002/(SICI)1097-4644(19991201)75:3<528::AID-JCB16>3.0.CO;2-3Search in Google Scholar

Karner, C.M. and Long, F. (2017). Wnt signaling and cellular metabolism in osteoblasts. Cell Mol. Life Sci. 74, 1649–1657.10.1007/s00018-016-2425-5Search in Google Scholar

Keber, R., Motaln, H., Wagner, K. D., Debeljak, N., Rassoulzadegan, M., Acimovic, J., Rozman, D., and Horvat, S. (2011). Mouse knockout of the cholesterogenic cytochrome P450 lanosterol 14alpha-demethylase (Cyp51) resembles Antley-Bixler syndrome. J. Biol. Chem. 286, 29086–29097.10.1074/jbc.M111.253245Search in Google Scholar

Kung, A.W.C. (2003). Androgen and bone mass in men. Asian J. Androl. 5, 148–154.Search in Google Scholar

Lepetsos, P. and Papavassiliou, A.G. (2016). ROS/oxidative stress signaling in osteoarthritis. Biochim. Biophys. Acta. 1862, 576–591.10.1016/j.bbadis.2016.01.003Search in Google Scholar

Leung, T.M. and Nieto, N. (2013). CYP2E1 and oxidant stress in alcoholic and non-alcoholic fatty liver disease. J. Hepatol. 58, 395–398.10.1016/j.jhep.2012.08.018Search in Google Scholar

Lewis, D.F.V. and Ito, Y. (2008) Cytochrome P450 structure and function: an evolutionary perspective. In: Cytochromes P450: Role in the Metabolism and Toxicity of Drugs and other Xenobiotics, C. Ioannides, ed. (Cambridge, UK: RSC Publishing), pp. 3–45.10.1039/9781847558428-00003Search in Google Scholar

Lips, P. and van Schoor, N.M. (2011). The effect of vitamin D on bone and osteoporosis. Best Pract. Res. Clin. Endocrinol. Metab. 25, 585–591.10.1016/j.beem.2011.05.002Search in Google Scholar

Lorbek, G., Lewinska, M., and Rozman, D. (2012). Cytochrome P450s in the synthesis of cholesterol and bile acids–from mouse models to human diseases. FEBS J. 279, 1516–1533.10.1111/j.1742-4658.2011.08432.xSearch in Google Scholar

Moorthy, B. (2008) The CYP1A subfamily. In: Cytochromes P450, C. Ioannides, ed. (Cambridge, UK: Royal Society of Chemistry), pp. 97–135.10.1039/9781847558428-00097Search in Google Scholar

Nakashima, K., Zhou, X., Kunkel, G., Zhang, Z.P., Deng, J.M., Behringer, R.R., and de Crombrugghe, B. (2002). The novel zinc finger-containing transcription factor Osterix is required for osteoblast differentiation and bone formation. Cell 108, 17–29.10.1016/S0092-8674(01)00622-5Search in Google Scholar

Nebert, D.W., Wikvall, K., and Miller, W.L. (2013). Human cytochromes P450 in health and disease. Phil. Trans. R. Soc. Lond. B. Biol. Sci. 368, 20120431.10.1098/rstb.2012.0431Search in Google Scholar

Neunzig, J., Milhim, M., Schiffer, L., Khatri, Y., Zapp, J., Sanchez-Guijo, A., Hartmann, M.F., Wudy, S.A., and Bernhardt, R. (2017). The steroid metabolite 16β-OH-androstenedione generated by CYP21A2 serves as a substrate for CYP19A1. J. Steroid Biochem. Mol. Biol. 167, 182–191.10.1016/j.jsbmb.2017.01.002Search in Google Scholar

Notelovitz, M. (2002). Androgen effects on bone and muscle. Fertil. Steril. 77, S34–S41.10.1016/S0015-0282(02)02968-0Search in Google Scholar

Panda, S., Kellogg, D., Tang, K.J., and Masters, B.S. (2015). Cytochrome P450 expression revealed in long bone growth plates. FASEB J. 29, Supplement 884.63.10.1096/fasebj.29.1_supplement.884.63Search in Google Scholar

Panda, S.P., Guntur, A.R., Polusani, S.R., Fajardo, R.J., Gakunga, P.T., Roman, L.J., and Masters, B.S. (2013). Conditional deletion of cytochrome P450 reductase in osteoprogenitor cells affects long bone and skull development in mice recapitulating Antley-Bixler syndrome: role of a redox enzyme in development. PloS One 8, e75638.10.1371/journal.pone.0075638Search in Google Scholar

Parr, M.K., Zollner, A., Fussholler, G., Opfermann, G., Schlorer, N., Zorio, M., Bureik, M., and Schanzer, W. (2012). Unexpected contribution of cytochrome P450 enzymes CYP11B2 and CYP21, as well as CYP3A4 in xenobiotic androgen elimination – insights from metandienone metabolism. Toxicol. Lett. 213, 381–391.10.1016/j.toxlet.2012.07.020Search in Google Scholar

Rittle, J. and Green, M.T. (2010). Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Science 330, 933–937.10.1126/science.1193478Search in Google Scholar

Rodriguez-Sanz, M., Garcia-Giralt, N., Prieto-Alhambra, D., Servitja, S., Balcells, S., Pecorelli, R., Diez-Perez, A., Grinberg, D., Tusquets, I., and Nogues, X. (2015). CYP11A1 expression in bone is associated with aromatase inhibitor-related bone loss. J. Mol. Endocrinol. 55, 69–79.10.1530/JME-15-0079Search in Google Scholar

Schiffer, L., Brixius-Anderko, S., Hannemann, F., Zapp, J., Neunzig, J., Thevis, M., and Bernhardt, R. (2016). Metabolism of oral turinabol by human steroid hormone-synthesizing cytochrome P450 enzymes. Drug. Metab. Dispos. 44, 227–237.10.1124/dmd.115.066829Search in Google Scholar

Teplyuk, N.M., Zhang, Y., Lou, Y., Hawse, J.R., Hassan, M.Q., Teplyuk, V.I., Pratap, J., Galindo, M., Stein, J.L., Stein, G.S., et al. (2009). The osteogenic transcription factor runx2 controls genes involved in sterol/steroid metabolism, including CYP11A1 in osteoblasts. Mol. Endocrinol. 23, 849–861.10.1210/me.2008-0270Search in Google Scholar

Valentine, J.L., Lee, S.S., Seaton, M.J., Asgharian, B., Farris, G., Corton, J.C., Gonzalez, F.J., and Medinsky, M.A. (1996). Reduction of benzene metabolism and toxicity in mice that lack CYP2E1 expression. Toxicol. Appl. Pharmacol. 141, 205–213.10.1016/S0041-008X(96)80026-3Search in Google Scholar

van der Meijden, K., Lips, P., van Driel, M., Heijboer, A.C., Schulten, E.A., den Heijer, M., and Bravenboer, N. (2014). Primary human osteoblasts in response to 25-hydroxyvitamin D3, 1,25-dihydroxyvitamin D3 and 24R,25-dihydroxyvitamin D3. PLoS One 9, e110283.10.1371/journal.pone.0110283Search in Google Scholar

van Driel, M., Koedam, M., Buurman, C. J., Roelse, M., Weyts, F., Chiba, H., Uitterlinden, A. G., Pols, H.A., and van Leeuwen, J.P. (2006). Evidence that both 1α,25-dihydroxyvitamin D3 and 24-hydroxylated D3 enhance human osteoblast differentiation and mineralization. J . Cell. Biochem. 99, 922–935.10.1002/jcb.20875Search in Google Scholar

Zöllner, A., Parr, M.K., Dragan, C.A., Dras, S., Schlorer, N., Peters, F.T., Maurer, H.H., Schanzer, W., and Bureik, M. (2010). CYP21-catalyzed production of the long-term urinary metandienone metabolite 17β-hydroxymethyl-17α-methyl-18-norandrosta-1,4,13-trien-3-one: a contribution to the fight against doping. Biol. Chem. 391, 119–127.10.1515/bc.2010.002Search in Google Scholar