The vitamin D receptor: Biochemical, molecular, biological, and genomic era investigations

Vitamin D

Volumn , Issue , 2011, Pages 97-135

  Pike, J Wesley ^a   Meyer, Mark B ^a   Lee, Seong Min ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84884811433     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-381978-9.10007-1     Document Type: Chapter

References (339)

1. Beato M. Gene regulation by steroid hormones. Cell 1989, 56:335-344.
2. Evans R. The steroid and thyroid hormone receptor superfamily. Science 1988, 240:889-895.
3. Tsai M., O'Malley B. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 1994, 63:451-486.
4. Beato M., Herrlich P., Schütz G. Steroid hormone receptors: many actors in search of a plot. Cell 1995, 83:851-857.
5. Mangelsdorf D., Evans R. The RXR heterodimers and orphan receptors. Cell 1995, 83:841-850.
6. Mangelsdorf D.J., Thummel C., Beato M., Herrlich P., Schutz G., Umesono K., et al. The nuclear receptor superfamily: the second decade. Cell 1995, 83:835-839.
7. Norman A. The mode of action of vitamin D. Biol. Rev. Camb. Philos. Soc. 1968, 43:97-137.
8. Lawson D., Fraser D., Kodicek E., Morris H., Williams D. Identification of 1,25-dihydroxycholecalciferol, a new kidney hormone controlling calcium metabolism. Nature 1971, 230:228-230.
9. 3 in the intestine. Science 1971, 173:51-54.
10. Holick M., Schnoes H., DeLuca H., Suda T., Cousins R. Isolation and identification of 1,25-dihydroxycholecalciferol. A metabolite of vitamin D active in intestine. Biochemistry 1971, 10:2799-2804.
11. Fraser D.R., Kodicek E. Unique biosynthesis by kidney of a biological active vitamin D metabolite. Nature 1970, 228:764-766.
12. Haussler M.R., Norman A.W. Chromosomal receptor for a vitamin D metabolite. Proc. Natl. Acad. Sci. USA 1969, 62:155-162.
13. McDonnell D., Mangelsdorf D., Pike J., Haussler M., O'Malley B. Molecular cloning of complementary DNA encoding the avian receptor for vitamin D. Science 1987, 235:1214-1217.
14. DeLuca H., Zierold C. Mechanisms and functions of vitamin D. Nutr. Rev. 1998, 56:S4-10. Discussion S54-75.
15. Boyle W.J., Simonet W.S., Lacey D.L. Osteoclast differentiation and activation. Nature 2003, 423:337-342.
16. Hsu H., Lacey D.L., Dunstan C.R., Solovyev I., Colombero A., Timms E., et al. Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand. Proc. Natl. Acad. Sci. USA 1999, 96:3540-3545.
17. Bergwitz C., Jüppner H. Regulation of phosphate homeostasis by PTH, vitamin D, and FGF23. Annu. Rev. Med. 2010, 61:91-104.
18. 3. Proc. Natl. Acad. Sci. USA 1981, 78:4990-4994.
19. 3 and the immune system. Mol. Cell Endocrinol. 1985, 43:113-122.
20. 3 receptors in human leukocytes. Science 1983, 221:1181-1183.
21. 3 induces maturation of the human monocyte cell line U937, and, in association with a factor from human T lymphocytes, augments production of the monokine, mononuclear cell factor. J. Clin. Invest. 1984, 73:731-739.
22. 3 in human peripheral blood mononuclear cells: presence in monocytes and induction in T lymphocytes following activation. J. Clin. Endocrinol. Metab. 1983, 57:1308-1310.
23. Reddy Vanga S., Good M., Howard P., Vacek J. Role of vitamin D in cardiovascular health. Am. J. Cardiol. 2010, 106:798-805.
24. 3 receptors in human skin biopsies. J. Clin. Endocrinol. Metab. 1980, 51:1463-1465.
25. Kragballe K. Vitamin D analogues in the treatment of psoriasis. J. Cell Biochem. 1992, 49:46-52.
26. Brumbaugh P., Haussler M. 1 Alpha,25-dihydroxycholecalciferol receptors in intestine. I. Association of 1 alpha,25-dihydroxycholecalciferol with intestinal mucosa chromatin. J. Biol. Chem. 1974, 249:1251-1257.
27. Lawson D.E., Wilson P.W. Intranuclear localization and receptor proteins for 1,25-dihydroxycholecalciferol in chick intestine. Biochem. J. 1974, 144:573-583.
28. Brumbaugh P., Haussler M. Specific binding of 1alpha,25-dihydroxycholecalciferol to nuclear components of chick intestine. J. Biol. Chem. 1975, 250:1588-1594.
29. 3 in chick parathyroid glands. Proc. Natl. Acad. Sci. USA 1975, 72:4871-4875.
30. Pike J., Goozé L., Haussler M. Biochemical evidence for 1,25-dihydroxyvitamin D receptor macromolecules in parathyroid, pancreatic, pituitary, and placental tissues. Life Sci. 1980, 26:407-414.
31. 3 in fetal bone. Science 1977, 197:1086-1088.
32. 3 receptors in rat kidney cytosol. Biochem. Biophys. Res. Commun. 1979, 90:1057-1063.
33. Colston K., Feldman D. Nuclear translocation of the 1,25-dihydroxycholecalciferol receptor in mouse kidney. J. Biol. Chem. 1980, 255:7510-7513.
34. 3 in rat intestine. J. Biol. Chem. 1977, 252:4501-4505.
35. 3 induces differentiation of human myeloid leukemia cells. Biochem. Biophys. Res. Commun. 1981, 102:937-943.
36. 3. Proc. Natl. Acad. Sci. USA 1983, 80:5907-5911.
37. 3 in chick pancreas: a partial physical and functional characterization. J. Steroid. Biochem. 1982, 16:385-395.
38. 3 receptor-like macromolecule in rat pituitary. J. Biol. Chem. 1980, 255:5007-5010.
39. 3. Endocrinology 1983, 112:200-206.
40. Merke J., Kreusser W., Bier B., Ritz E. Demonstration and characterisation of a testicular receptor for 1,25-dihydroxycholecalciferol in the rat. Eur. J. Biochem. 1983, 130:303-308.
41. 3 receptor in breast cancer. Cancer Res. 1987, 47:6793-6799.
42. Berger U., Wilson P., McClelland R., Colston K., Haussler M., Pike J., et al. Immunocytochemical detection of 1,25-dihydroxyvitamin D receptors in normal human tissues. J. Clin. Endocrinol. Metab. 1988, 67:607-613.
43. Colston K., Hirt M., Feldman D. Organ distribution of the cytoplasmic 1,25-dihydroxycholecalciferol receptor in various mouse tissues. Endocrinology 1980, 107:1916-1922.
44. 3 receptors identified in the rat heart. J. Mol. Cell Cardiol. 1986, 18:67-72.
45. 3 receptors in human epithelial cancer cell lines. Cancer Res. 1982, 42:856-859.
46. 3 and malignant melanoma: the presence of receptors and inhibition of cell growth in culture. Endocrinology 1981, 108:1083-1086.
47. Crofts L.A., Hancock M.S., Morrison N.A., Eisman J.A. Multiple promoters direct the tissue-specific expression of novel N-terminal variant human vitamin D receptor gene transcripts. Proc. Natl. Acad. Sci. USA 1998, 95:10529-10534.
48. 3 receptor in a cultured human breast cancer cell line (MCF 7 cells). Biochem. Biophys. Res. Commun. 1980, 93:9-15.
49. 3 receptors in cancer. Lancet 1980, 1:1188.
50. 3. Clin. Endocrinol. (Oxf.) 1980, 13:267-272.
51. 3 in intestinal nuclei in vivo. Arch. Biochem. Biophys. 1978, 186:15-24.
52. 3 in chick intestine. Endocrinology 1979, 104:313-321.
53. 3 in intestinal tract, stomach, kidney, skin, pituitary, and parathyroid. Science 1979, 206:1188-1190.
54. 3. Science 1982, 215:1403-1405.
55. 3 receptor in target cells. Endocrinology 1988, 122:1224-1230.
56. 3 receptors and estrogen receptors by monoclonal antibodies: comparison of four immunoperoxidase methods. J. Histochem. Cytochem. 1989, 37:1609-1617.
57. Wang Y., Becklund B., DeLuca H. Identification of a highly specific and versatile vitamin D receptor antibody. Arch. Biochem. Biophys. 2010, 494:166-177.
58. 3 in the parathyroid in vivo. J. Clin. Invest. 1990, 86:1968-1975.
59. 3. Mol. Endocrinol. 2006, 20:1231-1247.
60. Zella L., Meyer M., Nerenz R., Lee S., Martowicz M., Pike J. Multifunctional enhancers regulate mouse and human vitamin D receptor gene transcription. Mol. Endocrinol. 2010, 24:128-147.
61. Pike J.W., Haussler M.R. Purification of chicken intestinal receptor for 1,25-dihydroxyvitamin D. Proc. Natl. Acad. Sci. USA 1979, 76:5485-5489.
62. 3: new cultured cell models. Ann. N.Y. Acad. Sci. 1981, 372:502-517.
63. Katzenellenbogen J., Katzenellenbogen B. Nuclear hormone receptors: ligand-activated regulators of transcription and diverse cell responses. Chem. Biol. 1996, 3:529-536.
64. Katzenellenbogen J., O'Malley B., Katzenellenbogen B. Tripartite steroid hormone receptor pharmacology: interaction with multiple effector sites as a basis for the cell- and promoter-specific action of these hormones. Mol. Endocrinol. 1996, 10:119-131.
65. 3. Arch. Biochem. Biophys. 1979, 197:90-95.
66. 3 with its cytosol receptor from chick intestinal mucosa. J. Biol. Chem. 1980, 255:3571-3574.
67. 3: a study of analog binding. Arch. Biochem. Biophys. 1977, 179:462-468.
68. 3 with its chick intestinal mucosa receptor system. J. Steroid Biochem. 1978, 9:929-937.
69. 3 with cultured 3T6 mouse fibroblasts. Cellular uptake and receptor-mediated migration to the nucleus. J. Biol. Chem. 1983, 258:8554-8560.
70. Rochel N., Wurtz J.M., Mitschler A., Klaholz B., Moras D. The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand. Mol. Cell 2000, 5:173-179.
71. Tocchini-Valentini G., Rochel N., Wurtz J.M., Mitschler A., Moras D. Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands. Proc. Natl. Acad. Sci. USA 2001, 98:5491-5496.
72. 3 hormone analogues and a LXXLL-containing coactivator peptide. Biochemistry 2004, 43:4101-4110.
73. 3 intestinal receptors. Multiple biochemical forms and evidence for transformation. J. Biol. Chem. 1983, 258:8642-8648.
74. Malloy P.J., Pike J.W., Feldman D. The vitamin D receptor and the syndrome of hereditary 1,25-dihydroxyvitamin D-resistant rickets. Endocr. Rev. 1999, 20:156-188.
75. 3. Generation by a preparation enriched in a 64,000-dalton protein. J. Biol. Chem. 1983, 258:1289-1296.
76. 3: interaction with distinct receptor domains. Biochemistry 1986, 25:4523-4534.
77. 3. Immunologic characterization and homogeneous isolation of a 60,000-dalton protein. J. Biol. Chem. 1987, 262:1305-1311.
78. 3: in vitro translation to characterize size and hormone-dependent regulation. Proc. Natl. Acad. Sci. USA 1987, 84:354-358.
79. Elaroussi M.A., Prahl J.M., DeLuca H.F. The avian vitamin D receptors: primary structures and their origins. Proc. Natl. Acad. Sci. USA 1994, 91:11596-11600.
80. Gardiner E., Esteban L., Fong C., Allison S., Flanagan J., Kouzmenko A., et al. Vitamin D receptor B1 and exon 1d: functional and evolutionary analysis. J. Steroid Biochem. Mol. Biol. 2004, 89-90:233-238.
81. Sunn K., Cock T., Crofts L., Eisman J., Gardiner E. Novel N-terminal variant of human VDR. Mol. Endocrinol. 2001, 15:1599-1609.
82. Heyman R., Mangelsdorf D., Dyck J., Stein R., Eichele G., Evans R., et al. 9-Cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell 1992, 68:397-406.
83. Forman B., Tontonoz P., Chen J., Brun R., Spiegelman B., Evans R. 15-Deoxy-delta 12, 14-prostaglandin J2 is a ligand for the adipocyte determination factor PPAR gamma. Cell 1995, 83:803-812.
84. Forman B., Goode E., Chen J., Oro A., Bradley D., Perlmann T., et al. Identification of a nuclear receptor that is activated by farnesol metabolites. Cell 1995, 81:687-693.
85. Janowski B., Willy P., Devi T., Falck J., Mangelsdorf D. An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha. Nature 1996, 383:728-731.
86. Peet D., Janowski B., Mangelsdorf D. The LXRs: a new class of oxysterol receptors. Curr. Opin. Genet. Dev. 1998, 8:571-575.
87. Chawla A., Repa J., Evans R., Mangelsdorf D. Nuclear receptors and lipid physiology: opening the X-files. Science 2001, 294:1866-1870.
88. Mangelsdorf D. Commentary: the year in nuclear receptor control of metabolism. Mol. Endocrinol. 2010, 24:2075-2080.
89. McDonnell D.P., Mangelsdorf D.J., Pike J.W., Haussler M.R., O'Malley B.W. Molecular cloning of complementary DNA encoding the avian receptor for vitamin D. Science 1987, 235:1214-1217.
90. Baker A.R., McDonnell D.P., Hughes M., Crisp T.M., Mangelsdorf D.J., Haussler M.R., et al. Cloning and expression of full-length cDNA encoding human vitamin D receptor. Proc. Natl. Acad. Sci. USA 1988, 85:3294-3298.
91. 3 receptor cDNA. Proc. Natl. Acad. Sci. USA 1988, 85:1005-1009.
92. Kamei Y., Kawada T., Fukuwatari T., Ono T., Kato S., Sugimoto E. Cloning and sequencing of the gene encoding the mouse vitamin D receptor. Gene 1995, 152:281-282.
93. Li Y., Bergwitz C., Jüppner H., Demay M. Cloning and characterization of the vitamin D receptor from Xenopus laevis. Endocrinology 1997, 138:2347-2353.
94. Whitfield G., Dang H., Schluter S., Bernstein R., Bunag T., Manzon L., et al. Cloning of a functional vitamin D receptor from the lamprey (Petromyzon marinus), an ancient vertebrate lacking a calcified skeleton and teeth. Endocrinology 2003, 144:2704-2716.
95. Ciana P., Vegeto E., Beato M., Chambon P., Gustafsson J., Parker M., et al. Looking at nuclear receptors from the heights of Erice. Workshop on nuclear receptor structure and function. EMBO. Rep. 2002, 3:125-129.
96. Enmark E., Gustafsson J. Comparing nuclear receptors in worms, flies and humans. Trends. Pharmacol. Sci. 2001, 22:611-615.
97. McDonnell D., Pike J., O'Malley B. The vitamin D receptor: a primitive steroid receptor related to thyroid hormone receptor. J. Steroid Biochem. 1988, 30:41-46.
98. Saijo T., Ito M., Takeda E., Huq A.H., Naito E., Yokota I., et al. A unique mutation in the vitamin D receptor gene in three Japanese patients with vitamin D-dependent rickets type II: utility of single-strand conformation polymorphism analysis for heterozygous carrier detection. Am. J. Hum. Genet. 1991, 49:668-673.
99. Jurutka P., Remus L., Whitfield G., Thompson P., Hsieh J., Zitzer H., et al. The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB. Mol. Endocrinol. 2000, 14:401-420.
100. Arai H., Miyamoto K., Taketani Y., Yamamoto H., Iemori Y., Morita K., et al. A vitamin D receptor gene polymorphism in the translation initiation codon: effect on protein activity and relation to bone mineral density in Japanese women. J. Bone Miner. Res. 1997, 12:915-921.
101. Gross C., Krishnan A.V., Malloy P.J., Eccleshall T.R., Zhao X.Y., Feldman D. The vitamin D receptor gene start codon polymorphism: a functional analysis of FokI variants. J. Bone Miner. Res. 1998, 13:1691-1699.
102. Chiu K., Chuang L., Yoon C. The vitamin D receptor polymorphism in the translation initiation codon is a risk factor for insulin resistance in glucose tolerant Caucasians. BMC. Med. Genet. 2001, 2:2.
103. Kubota M., Yoshida S., Ikeda M., Okada Y., Arai H., Miyamoto K., et al. Association between two types of vitamin D receptor gene polymorphism and bone status in premenopausal Japanese women. Calcif. Tissue. Int. 2001, 68:16-22.
104. Whitfield G., Remus L., Jurutka P., Zitzer H., Oza A., Dang H., et al. Functionally relevant polymorphisms in the human nuclear vitamin D receptor gene. Mol. Cell. Endocrinol. 2001, 177:145-159.
105. Hollenberg S.M., Weinberger C., Ong E.S., Cerelli G., Oro A., Lebo R., et al. Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature 1985, 318:635-641.
106. Green S., Walter P., Kumar V., Krust A., Bornert J.M., Argos P., et al. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature 1986, 320:134-139.
107. Green S., Kumar V., Krust A., Walter P., Chambon P. Structural and functional domains of the estrogen receptor. Cold Spring Harb. Symp. Quant. Biol. 51 Pt. 1986, 2:751-758.
108. Gerisch B., Rottiers V., Li D., Motola D.L., Cummins C.L., Lehrach H., et al. A bile acid-like steroid modulates Caenorhabditis elegans lifespan through nuclear receptor signaling. Proc. Natl. Acad. Sci. USA 2007, 104:5014-5019.
109. Sharma K.K., Wang Z., Motola D.L., Cummins C.L., Mangelsdorf D.J., Auchus R.J. Synthesis and activity of dafachronic acid ligands for the C. elegans DAF-12 nuclear hormone receptor. Mol. Endocrinol. 2009, 23:640-648.
110. Enmark E., Gustafsson J. [Nuclear receptors in man, fly and worm provide greater understanding of disease]. Lakartidningen. 2002, 99:1186-1190.
111. Evans R.M. The steroid and thyroid hormone receptor superfamily. Science 1988, 240:889-895.
112. Mangelsdorf D., Thummel C., Beato M., Herrlich P., Schütz G., Umesono K., et al. The nuclear receptor superfamily: the second decade. Cell 1995, 83:835-839.
113. 3 receptor regulate osteocalcin gene expression. Mol. Endocrinol. 1989, 3:635-644.
114. Hughes M.R., Malloy P.J., Kieback D.G., Kesterson R.A., Pike J.W., Feldman D., et al. Point mutations in the human vitamin D receptor gene associated with hypocalcemic rickets. Science 1988, 242:1702-1705.
115. Jin C.H., Pike J.W. Human vitamin D receptor-dependent transactivation in Saccharomyces cerevisiae requires retinoid X receptor. Mol. Endocrinol. 1996, 10:196-205.
116. Jin C.H., Kerner S.A., Hong M.H., Pike J.W. Transcriptional activation and dimerization functions in the human vitamin D receptor. Mol. Endocrinol. 1996, 10:945-957.
117. MacDonald P.N., Sherman D.R., Dowd D.R., Jefcoat S.C., DeLisle R.K. The vitamin D receptor interacts with general transcription factor IIB. J. Biol. Chem. 1995, 270:4748-4752.
118. Cairns C., Gustafsson J.A., Carlstedt-Duke J. Identification of protein contact sites within the glucocorticoid/progestin response element. Mol. Endocrinol. 1991, 5:598-604.
119. Carlstedt-Duke J., Wrange O., Okret S., Gustafsson J.A. The glucocorticoid receptor in rat liver. Biochem. Pharmacol. 1984, 33:913-916.
120. Carlstedt-Duke J., Strömstedt P.E., Wrange O., Bergman T., Gustafsson J.A., Jörnvall H. Domain structure of the glucocorticoid receptor protein. Proc. Natl. Acad. Sci. USA 1987, 84:4437-4440.
121. Carlstedt-Duke J., Gustafsson J.A. Structure and function of the glucocorticoid receptor. J. Steroid. Biochem. 1987, 27:99-104.
122. Carlstedt-Duke J., Gustafsson J.A. Functional probing of glucocorticoid receptor structure. J. Steroid Biochem. 1988, 31:593-597.
123. 3. Interaction and effects of binding on receptor function. J. Biol. Chem. 1984, 259:1167-1173.
124. 3 receptors. Generation of discrete polypeptides which retain hormone but are unreactive to DNA and monoclonal antibody. J. Biol. Chem. 1985, 260:10139-10145.
125. 3 receptor. Distinct 20-kDa DNA-binding and 45-kDa hormone-binding species. J. Biol. Chem. 1987, 262:1312-1319.
126. 3 receptor. Biochem. Biophys. Res. Commun. 1987, 147:479-485.
127. Berg J.M. DNA binding specificity of steroid receptors. Cell 1989, 57:1065-1068.
128. Berg J.M. Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins. Proc. Natl. Acad. Sci. USA 1988, 85:99-102.
129. Mader S., Kumar V., de Verneuil H., Chambon P. Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element. Nature 1989, 338:271-274.
130. 3 receptors. Cell 1991, 65:1255-1266.
131. Schwabe J.W., Neuhaus D., Rhodes D. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 1990, 348:458-461.
132. Härd T., Kellenbach E., Boelens R., Maler B.A., Dahlman K., Freedman L.P., et al. Solution structure of the glucocorticoid receptor DNA-binding domain. Science 1990, 249:157-160.
133. Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 1991, 352:497-505.
134. Lee M.S., Kliewer S.A., Provencal J., Wright P.E., Evans R.M. Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding. Science 1993, 260:1117-1121.
135. Rastinejad F., Perlmann T., Evans R.M., Sigler P.B. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 1995, 375:203-211.
136. Forman B.M., Yang C.R., Au M., Casanova J., Ghysdael J., Samuels H.H. A domain containing leucine-zipper-like motifs mediate novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Mol. Endocrinol. 1989, 3:1610-1626.
137. Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 1995, 375:377-382.
138. Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., et al. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature 1995, 378:681-689.
139. Wagner R.L., Apriletti J.W., McGrath M.E., West B.L., Baxter J.D., Fletterick R.J. A structural role for hormone in the thyroid hormone receptor. Nature 1995, 378:690-697.
140. Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 1998, 95:927-937.
141. Williams S.P., Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature 1998, 393:392-396.
142. Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R., et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature 1998, 395:137-143.
143. Downes M., Verdecia M.A., Roecker A.J., Hughes R., Hogenesch J.B., Kast-Woelbern H.R., et al. A chemical, genetic, and structural analysis of the nuclear bile acid receptor FXR. Mol. Cell 2003, 11:1079-1092.
144. 3 are associated with enhanced activation of the vitamin D receptor. J. Biol. Chem. 1995, 270:10551-10558.
145. Chandra V., Huang P., Hamuro Y., Raghuram S., Wang Y., Burris T.P., et al. Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature 2008, 456:350-356.
146. Tocchini-Valentini G., Rochel N., Wurtz J.M., Moras D. Crystal structures of the vitamin D nuclear receptor liganded with the vitamin D side chain analogues calcipotriol and seocalcitol, receptor agonists of clinical importance. Insights into a structural basis for the switching of calcipotriol to a receptor antagonist by further side chain modification. J. Med. Chem. 2004, 47:1956-1961.
147. 3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis. J. Steroid. Biochem. Mol. Biol. 2004, 89-90:55-59.
148. Ciesielski F., Rochel N., Moras D. Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation. J. Steroid Biochem. Mol. Biol. 2007, 103:235-242.
149. Whitfield G., Hsieh J., Nakajima S., MacDonald P., Thompson P., Jurutka P., et al. A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation. Mol. Endocrinol. 1995, 9:1166-1179.
150. Danielian P.S., White R., Lees J.A., Parker M.G. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 1992, 11:1025-1033.
151. Xu J., O'Malley B.W. Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function. Rev. Endocr. Metab. Disord. 2002, 3:185-192.
152. Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naar A.M., et al. Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature 1999, 398:824-828.
153. Rachez C., Freedman L.P. Mediator complexes and transcription. Curr. Opin. Cell Biol. 2001, 13:274-280.
154. McInerney E.M., Rose D.W., Flynn S.E., Westin S., Mullen T.M., Krones A., et al. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 1998, 12:3357-3368.
155. 3-dependent transcription by synthetic LXXLL peptide antagonists that target the activation domains of the vitamin D and retinoid X receptors. J. Bone Miner. Res. 2002, 17:2196-2205.
156. Brzozowski A.M., Pike A.C., Dauter Z., Hubbard R.E., Bonn T., Engström O., et al. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 1997, 389:753-758.
157. Shiau A.K., Barstad D., Radek J.T., Meyers M.J., Nettles K.W., Katzenellenbogen B.S., et al. Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism. Nat. Struct. Biol. 2002, 9:359-364.
158. Tzukerman M.T., Esty A., Santiso-Mere D., Danielian P., Parker M.G., Stein R.B., et al. Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol. Endocrinol. 1994, 8:21-30.
159. McDonnell D.P., Clemm D.L., Hermann T., Goldman M.E., Pike J.W. Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens. Mol. Endocrinol. 1995, 9:659-669.
160. Ducy P., Desbois C., Boyce B., Pinero G., Story B., Dunstan C., et al. Increased bone formation in osteocalcin-deficient mice. Nature 1996, 382:448-452.
161. Rached M.T., Kode A., Silva B.C., Jung D.Y., Gray S., Ong H., et al. FoxO1 expression in osteoblasts regulates glucose homeostasis through regulation of osteocalcin in mice. J. Clin. Invest. 2010, 120:357-368.
162. Ferron M., Wei J., Yoshizawa T., Del Fattore A., DePinho R.A., Teti A., et al. Insulin signaling in osteoblasts integrates bone remodeling and energy metabolism. Cell 2010, 142:296-308.
163. 3 increases synthesis of the vitamin K-dependent bone protein by osteosarcoma cells. J. Biol. Chem. 1980, 255:11660-11663.
164. Celeste A.J., Rosen V., Buecker J.L., Kriz R., Wang E.A., Wozney J.M. Isolation of the human gene for bone Gla protein utilizing mouse and rat cDNA clones. EMBO J. 1986, 5:1885-1890.
165. 3. Proc. Natl. Acad. Sci. USA 1989, 86:4455-4459.
166. Morrison N.A., Shine J., Fragonas J.C., Verkest V., McMenemy M.L., Eisman J.A. 1,25-Dihydroxyvitamin D-responsive element and glucocorticoid repression in the osteocalcin gene. Science 1989, 246:1158-1161.
167. 3. Biochemistry 1988, 27:8521-8526.
168. Ozono K., Liao J., Kerner S.A., Scott R.A., Pike J.W. The vitamin D-responsive element in the human osteocalcin gene. Association with a nuclear proto-oncogene enhancer. J. Biol. Chem. 1990, 265:21881-21888.
169. 3. Proc. Natl. Acad. Sci. USA 1990, 87:369-373.
170. Lian J., Stewart C., Puchacz E., Mackowiak S., Shalhoub V., Collart D., et al. Structure of the rat osteocalcin gene and regulation of vitamin
171. 3-mediated transcriptional activation. Mol. Endocrinol. 1991, 5:373-385.
172. 3 enhancement of mouse secreted phosphoprotein 1 (SPP-1 or osteopontin) gene expression. Proc. Natl. Acad. Sci. USA 1990, 87:9995-9999.
173. 3- and butyrate-inducible responses. Proc. Natl. Acad. Sci. USA 1993, 90:2984-2988.
174. 3-response element in the 5'-flanking region of the rat calbindin D-9k gene. Proc. Natl. Acad. Sci. USA 1992, 89:603-607.
175. 3 24-hydroxylase gene. J. Biol. Chem. 1994, 269:10545-10550.
176. 3) 24-hydroxylase gene. Proc. Natl. Acad. Sci. USA 1994, 91:900-902.
177. Zierold C., Darwish H.M., DeLuca H.F. Two vitamin D response elements function in the rat 1,25-dihydroxyvitamin D 24-hydroxylase promoter. J. Biol. Chem. 1995, 270:1675-1678.
178. Chen K.S., DeLuca H.F. Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements. Biochim. Biophys. Acta. 1995, 1263:1-9.
179. 3 leads to the induced differentiation of the myelomonocytic cell line U937. Genes Dev. 1996, 10:142-153.
180. van den Bemd G.J., Jhamai M., Staal A., van Wijnen A.J., Lian J.B., Stein G.S., et al. A central dinucleotide within vitamin D response elements modulates DNA binding and transactivation by the vitamin D receptor in cellular response to natural and synthetic ligands. J. Biol. Chem. 2002, 277:14539-14546.
181. Mackey S.L., Heymont J.L., Kronenberg H.M., Demay M.B. Vitamin D receptor binding to the negative human parathyroid hormone vitamin D response element does not require the retinoid x receptor. Mol. Endocrinol. 1996, 10:298-305.
182. 3-mediated transcriptional repression. Mol. Endocrinol. 1996, 10:672-681.
183. 3-responsive repressor sequences in the rat parathyroid hormone-related peptide gene. J. Biol. Chem. 1996, 271:16310-16316.
184. Kato S., Fujiki R., Kim M.S., Kitagawa H. Ligand-induced transrepressive function of VDR requires a chromatin remodeling complex, WINAC. J. Steroid. Biochem. Mol. Biol. 2007, 103:372-380.
185. 2 vitamin D. Curr. Opin. Nephrol. Hypertens. 2007, 16:297-304.
186. 3-induced DNA methylation suppresses the human CYP27B1 gene. Mol. Cell Endocrinol. 2007, 265-266:168-173.
187. 3-induced transrepression by vitamin D receptor through E-box-type elements in the human parathyroid hormone gene promoter. Mol. Endocrinol. 2007, 21:334-342.
188. Kim M., Kondo T., Takada I., Youn M., Yamamoto Y., Takahashi S., et al. DNA demethylation in hormone-induced transcriptional derepression. Nature 2009, 461:1007-1012.
189. Murayama A., Kim M.S., Yanagisawa J., Takeyama K., Kato S. Transrepression by a liganded nuclear receptor via a bHLH activator through co-regulator switching. EMBO J. 2004, 23:1598-1608.
190. 3. Proc. Natl. Acad. Sci. USA 1990, 87:9751-9755.
191. 3 receptor zinc finger region. Mol. Endocrinol. 1991, 5:1815-1826.
192. 3 receptor: mechanism of dimer binding to an asymmetric repeat element. Proc. Natl. Acad. Sci. USA 1993, 90:6310-6314.
193. 3-dependent cell-free transcription. Mol. Cell Biol. 1997, 17:1923-1937.
194. Nishikawa J., Kitaura M., Matsumoto M., Imagawa M., Nishihara T. Difference and similarity of DNA sequence recognized by VDR homodimer and VDR/RXR heterodimer. Nucleic Acids Res. 1994, 22:2902-2907.
195. 3 in humans are transcriptionally inactive in vitro. J. Biol. Chem. 1989, 264:20230-20234.
196. 3 receptor. J. Recept. Res. 1991, 11:699-716.
197. Nakajima S., Hsieh J.C., MacDonald P.N., Galligan M.A., Haussler C.A., Whitfield G.K., et al. The C-terminal region of the vitamin D receptor is essential to form a complex with a receptor auxiliary factor required for high affinity binding to the vitamin D-responsive element. Mol. Endocrinol. 1994, 8:159-172.
198. 3. Proc. Natl. Acad. Sci. USA 1990, 87:9751-9755.
199. 3-modulated heterodimer. J. Biol. Chem. 1991, 266:23296-23305.
200. Sone T., Ozono K., Pike J.W. A 55-kilodalton accessory factor facilitates vitamin D receptor DNA binding. Mol. Endocrinol. 1991, 5:1578-1586.
201. Sone T., McDonnell D., O'Malley B., Pike J. Expression of human vitamin D receptor in Saccharomyces cerevisiae. Purification, properties, and generation of polyclonal antibodies. J. Biol. Chem. 1990, 265:21997-22003.
202. MacDonald P.N., Haussler C.A., Terpening C.M., Galligan M.A., Reeder M.C., Whitfield G.K., et al. Baculovirus-mediated expression of the human vitamin D receptor. Functional characterization, vitamin D response element interactions, and evidence for a receptor auxiliary factor. J. Biol. Chem. 1991, 266:18808-18813.
203. 3 receptor to its response elements. Proc. Natl. Acad. Sci. USA 1992, 89:256-260.
204. Yu V.C., Delsert C., Andersen B., Holloway J.M., Devary O.V., Näär A.M., et al. RXR beta: a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements. Cell 1991, 67:1251-1266.
205. Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewski T., et al. Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. Cell 1992, 68:377-395.
206. Zhang X.K., Hoffmann B., Tran P.B., Graupner G., Pfahl M. Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors. Nature 1992, 355:441-446.
207. 3 signalling. Nature 1992, 355:446-449.
208. Perlmann T., Umesono K., Rangarajan P.N., Forman B.M., Evans R.M. Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 1996, 10:958-966.
209. Perlmann T., Rangarajan P.N., Umesono K., Evans R.M. Determinants for selective RAR and TR recognition of direct repeat HREs. Genes Dev. 1993, 7:1411-1422.
210. Kurokawa R., Yu V.C., Näär A., Kyakumoto S., Han Z., Silverman S., et al. Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers. Genes Dev. 1993, 7:1423-1435.
211. Sucov H.M., Murakami K.K., Evans R.M. Characterization of an autoregulated response element in the mouse retinoic acid receptor type beta gene. Proc. Natl. Acad. Sci. USA 1990, 87:5392-5396.
212. Fyodorov D.V., Kadonaga J.T. The many faces of chromatin remodeling: SWItching beyond transcription. Cell 2001, 106:523-525.
213. Narlikar G.J., Fan H.Y., Kingston R.E. Cooperation between complexes that regulate chromatin structure and transcription. Cell 2002, 108:475-487.
214. Chakravarti D., LaMorte V.J., Nelson M.C., Nakajima T., Schulman I.G., Juguilon H., et al. Role of CBP/P300 in nuclear receptor signalling. Nature 1996, 383:99-103.
215. Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996, 87:953-959.
216. Imhof A., Yang X.J., Ogryzko V.V., Nakatani Y., Wolffe A.P., Ge H. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 1997, 7:689-692.
217. Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., Mizzen C.A., et al. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 1997, 389:194-198.
218. Jiang Y.W., Veschambre P., Erdjument-Bromage H., Tempst P., Conaway J.W., Conaway R.C., et al. Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways. Proc. Natl. Acad. Sci. USA 1998, 95:8538-8543.
219. Masuyama H., Brownfield C.M., St-Arnaud R., MacDonald P.N. Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction. Mol. Endocrinol. 1997, 11:1507-1517.
220. Kagey M.H., Newman J.J., Bilodeau S., Zhan Y., Orlando D.A., van Berkum N.L., et al. Mediator and cohesin connect gene expression and chromatin architecture. Nature 2010, 467:430-435.
221. Kraichely D.M., Collins J.J., DeLisle R.K., MacDonald P.N. The autonomous transactivation domain in helix H3 of the vitamin D receptor is required for transactivation and coactivator interaction. J. Biol. Chem. 1999, 274:14352-14358.
222. Leo C., Li H., Chen J.D. Differential mechanisms of nuclear receptor regulation by receptor-associated coactivator 3. J. Biol. Chem. 2000, 275:5976-5982.
223. Issa L.L., Leong G.M., Barry J.B., Sutherland R.L., Eisman J.A. Glucocorticoid receptor-interacting protein-1 and receptor-associated coactivator-3 differentially interact with the vitamin D receptor (VDR) and regulate VDR-retinoid X receptor transcriptional cross-talk. Endocrinology 2001, 142:1606-1615.
224. Baudino T.A., Kraichely D.M., Jefcoat S.C., Winchester S.K., Partridge N.C., MacDonald P.N. Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription. J. Biol. Chem. 1998, 273:16434-16441.
225. Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., et al. The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome. Cell 2003, 113:905-917.
226. Polly P., Herdick M., Moehren U., Baniahmad A., Heinzel T., Carlberg C. VDR-Alien: a novel, DNA-selective vitamin D(3) receptor-corepressor partnership. FASEB J. 2000, 14:1455-1463.
227. Hsieh J., Sisk J., Jurutka P., Haussler C., Slater S., Haussler M., et al. Physical and functional interaction between the vitamin D receptor and hairless corepressor, two proteins required for hair cycling. J. Biol. Chem. 2003, 278:38665-38674.
228. Masuyama H., MacDonald P.N. Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR. J. Cell Biochem. 1998, 71:429-440.
229. Perissi V., Staszewski L.M., McInerney E.M., Kurokawa R., Krones A., Rose D.W., et al. Molecular determinants of nuclear receptor-corepressor interaction. Genes Dev. 1999, 13:3198-3208.
230. Tagami T., Lutz W.H., Kumar R., Jameson J.L. The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators. Biochem. Biophys. Res. Commun. 1998, 253:358-363.
231. Blanco J.C., Wang I.M., Tsai S.Y., Tsai M.J., O'Malley B.W., Jurutka P.W., et al. Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription. Proc. Natl. Acad. Sci. USA 1995, 92:1535-1539.
232. Thompson P.D., Remus L.S., Hsieh J.C., Jurutka P.W., Whitfield G.K., Galligan M.A., et al. Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contexts. J. Mol. Endocrinol. 2001, 27:211-227.
233. Bettoun D.J., Burris T.P., Houck K.A., Buck D.W., Stayrook K.R., Khalifa B., et al. Retinoid X receptor is a nonsilent major contributor to vitamin D receptor-mediated transcriptional activation. Mol. Endocrinol. 2003, 17:2320-2328.
234. Pike J.W. Genomic-scale techniques highlight the epigenome and redefine fundamental principles of gene regulation. J. Bone Min. Res. 2011.
235. Hoffman B.G., Jones S.J. Genome-wide identification of DNA-protein interactions using chromatin immunoprecipitation coupled with flow cell sequencing. J. Endocrinol. 2009, 201:1-13.
236. Hawkins R., Hon G., Lee L., Ngo Q., Lister R., Pelizzola M., et al. Distinct epigenomic landscapes of pluripotent and lineage-committed human cells. Cell Stem Cell 2010, 6:479-491.
237. Lister R., Gregory B.D., Ecker J.R. Next is now: new technologies for sequencing of genomes, transcriptomes, and beyond. Curr. Opin. Plant Biol. 2009, 12:107-118.
238. Wang Z., Gerstein M., Snyder M. RNA-Seq: a revolutionary tool for transcriptomics. Nat. Rev. Genet. 2009, 10:57-63.
239. 3 receptor but not p300 intrinsic histone acetyltransferase activity. Mol. Cell Biol. 2003, 23:3339-3351.
240. Zhang C., Dowd D.R., Staal A., Gu C., Lian J.B., van Wijnen A.J., et al. Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing. J. Biol. Chem. 2003, 278:35325-35336.
241. 3 potently stimulates gene-specific DNA binding of the vitamin D receptor in osteoblasts. J. Biol. Chem. 2003, 278:31756-31765.
242. 3 stimulates cyclic vitamin D receptor/retinoid X receptor DNA-binding, co-activator recruitment, and histone acetylation in intact osteoblasts. J. Bone Miner. Res. 2005, 20:305-317.
243. Shang Y., Hu X., DiRenzo J., Lazar M.A., Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 2000, 103:843-852.
244. Reid G., Hübner M., Métivier R., Brand H., Denger S., Manu D., et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 2003, 11:695-707.
245. Métivier R., Penot G., Hübner M., Reid G., Brand H., Kos M., et al. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003, 115:751-763.
246. Shang Y., Myers M., Brown M. Formation of the androgen receptor transcription complex. Mol. Cell 2002, 9:601-610.
247. Burakov D., Crofts L.A., Chang C.P., Freedman L.P. Reciprocal recruitment of DRIP/mediator and p160 coactivator complexes in vivo by estrogen receptor. J. Biol. Chem. 2002, 277:14359-14362.
248. Meyer M.B., Goetsch P.D., Pike J.W. Genome-wide analysis of the VDR/RXR cistrome in osteoblast cells provides new mechanistic insight into the actions of the vitamin D hormone. J. Steroid Biochem. Mol. Biol. 2010, 121:136-141.
249. 3. J. Biol. Chem. 2010, 285:15599-15610.
250. Burgess T., Qian Y., Kaufman S., Ring B., Van G., Capparelli C., et al. The ligand for osteoprotegerin (OPGL) directly activates mature osteoclasts. J. Cell Biol. 1999, 145:527-538.
251. Kong Y.Y., Yoshida H., Sarosi I., Tan H.L., Timms E., Capparelli C., et al. OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis. Nature 1999, 397:315-323.
252. Lacey D.L., Timms E., Tan H.L., Kelley M.J., Dunstan C.R., Burgess T., et al. Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation. Cell 1998, 93:165-176.
253. 3 supports osteoclastogenesis via functional vitamin D response element of human RANKL gene promoter. J. Cell Biochem. 2003, 89:771-777.
254. 3. J. Cell Biochem. 2008, 105:1289-1297.
255. 3 is mediated through multiple long-range enhancers. Mol. Cell Biol. 2006, 26:6469-6486.
256. Kim S., Yamazaki M., Shevde N.K., Pike J.W. Transcriptional control of receptor activator of nuclear factor-kappaB ligand by the protein kinase A activator forskolin and the transmembrane glycoprotein 130-activating cytokine, oncostatin M, is exerted through multiple distal enhancers. Mol. Endocrinol. 2007, 21:197-214.
257. 3. Mol. Endocrinol. 2008, 22:1044-1056.
258. Bishop K.A., Meyer M.B., Pike J.W. A novel distal enhancer mediates cytokine induction of mouse RANKl gene expression. Mol. Endocrinol. 2009, 23:2095-2110.
259. Meyer M., Goetsch P.D., Pike J.W. Cistrome for the VDR/RXR heterodimer in Colorectal Cancer Cells. Mol. Cell. Biol. 2011.
260. 3 in intestinal cells. Mol. Endocrinol. 2006, 20:1447-1461.
261. 3 in mouse kidney and intestine in vivo. J. Biol. Chem. 2007, 282:22344-22352.
262. 2+ absorption between enterocytes. Mol. Biol. Cell 2008, 19:1912-1921.
263. Drocourt L., Ourlin J., Pascussi J., Maurel P., Vilarem M. Expression of CYP3A4, CYP2B6, and CYP2C9 is regulated by the vitamin D receptor pathway in primary human hepatocytes. J. Biol. Chem. 2002, 277:25125-25132.
264. Pascussi J.M., Gerbal-Chaloin S., Drocourt L., Maurel P., Vilarem M.J. The expression of CYP2B6, CYP2C9 and CYP3A4 genes: a tangle of networks of nuclear and steroid receptors. Biochim. Biophys. Acta. 2003, 1619:243-253.
265. Pascussi J.M., Gerbal-Chaloin S., Duret C., Daujat-Chavanieu M., Vilarem M.J., Maurel P. The tangle of nuclear receptors that controls xenobiotic metabolism and transport: crosstalk and consequences. Annu. Rev. Pharmacol. Toxicol. 2008, 48:1-32.
266. Tachibana S., Yoshinari K., Chikada T., Toriyabe T., Nagata K., Yamazoe Y. Involvement of Vitamin D receptor in the intestinal induction of human ABCB1. Drug. Metab. Dispos. 2009, 37:1604-1610.
267. 3 and vitamin D analogs, in the Caco-2 cell monolayer. J. Pharmacol. Exp. Ther. 2009, 330:389-402.
268. Tuupanen S., Turunen M., Lehtonen R., Hallikas O., Vanharanta S., Kivioja T., et al. The common colorectal cancer predisposition SNP rs6983267 at chromosome 8q24 confers potential to enhanced Wnt signaling. Nat. Genet. 2009, 41:885-890.
269. Ahmadiyeh N., Pomerantz M., Grisanzio C., Herman P., Jia L., Almendro V., et al. 8q24 prostate, breast, and colon cancer risk loci show tissue-specific long-range interaction with MYC. Proc. Natl. Acad. Sci. USA 2010, 107:9742-9746.
270. Pomerantz M., Ahmadiyeh N., Jia L., Herman P., Verzi M., Doddapaneni H., et al. The 8q24 cancer risk variant rs6983267 shows long-range interaction with MYC in colorectal cancer. Nat. Genet. 2009, 41:882-884.
271. Wright J.B., Brown S.J., Cole M.D. Upregulation of c-MYC in cis through a large chromatin loop linked to a cancer risk-associated single-nucleotide polymorphism in colorectal cancer cells. Mol. Cell Biol. 2010, 30:1411-1420.
272. Bishop K.P.J.W. T cell activation induces RANKL gene expression in mouse and human T cells. Molecular Endocrinology 2011.
273. Wang X., Song X., Glass C.K., Rosenfeld M.G. The long arm of long noncoding RNAs: roles as sensors regulating gene transcriptional programs. Cold Spring Harb. Perspect. Biol. 2010.
274. Szutorisz H., Dillon N., Tora L. The role of enhancers as centres for general transcription factor recruitment. Trends Biochem. Sci. 2005, 30:593-599.
275. Wang X., Arai S., Song X., Reichart D., Du K., Pascual G., et al. Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription. Nature 2008, 454:126-130.
276. Rinn J.L., Kertesz M., Wang J.K., Squazzo S.L., Xu X., Brugmann S.A., et al. Functional demarcation of active and silent chromatin domains in human HOX loci by noncoding RNAs. Cell 2007, 129:1311-1323.
277. Heinz S., Benner C., Spann N., Bertolino E., Lin Y.C., Laslo P., et al. Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. Mol. Cell 2010, 38:576-589.
278. Lin Y.C., Jhunjhunwala S., Benner C., Heinz S., Welinder E., Mansson R., et al. A global network of transcription factors, involving E2A, EBF1 and Foxo1, that orchestrates B cell fate. Nat. Immunol. 2010, 11:635-643.
279. Carroll J., Meyer C., Song J., Li W., Geistlinger T., Eeckhoute J., et al. Genome-wide analysis of estrogen receptor binding sites. Nat. Genet. 2006, 38:1289-1297.
280. Lupien M., Eeckhoute J., Meyer C.A., Wang Q., Zhang Y., Li W., et al. FoxA1 translates epigenetic signatures into enhancer-driven lineage-specific transcription. Cell 2008, 132:958-970.
281. Lupien M., Brown M. Cistromics of hormone-dependent cancer. Endocr. Relat. Cancer 2009, 16:381-389.
282. Lupien M., Eeckhoute J., Meyer C.A., Krum S.A., Rhodes D.R., Liu X.S., et al. Coactivator function defines the active estrogen receptor alpha cistrome. Mol. Cell Biol. 2009, 29:3413-3423.
283. Lupien M., Meyer C.A., Bailey S.T., Eeckhoute J., Cook J., Westerling T., et al. Growth factor stimulation induces a distinct ER(alpha) cistrome underlying breast cancer endocrine resistance. Genes Dev. 2010, 24:2219-2227.
284. Cui J.Y., Gunewardena S.S., Rockwell C.E., Klaassen C.D. ChIPing the cistrome of PXR in mouse liver. Nucleic Acids Res. 2010.
285. Cullum R., Alder O., Hoodless P.A. The next generation: using new sequencing technologies to analyze gene regulation. Respirology 2010.
286. Costa V., Gallo M.A., Letizia F., Aprile M., Casamassimi A., Ciccodicola A. 2010 PPARG: gene expression regulation and next-generation sequencing for unsolved issues. PPAR. Res. 2010.
287. Birney E., Stamatoyannopoulos J.A., Dutta A., Guigó R., Gingeras T.R., Margulies E.H., et al. Center BCoMHGS, Center WUGS, Institute B, Institute CsHOR. Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project. Nature 2007, 447:799-816.
288. Blahnik K.R., Dou L., O'Geen H., McPhillips T., Xu X., Cao A.R., et al. Sole-Search: an integrated analysis program for peak detection and functional annotation using ChIP-seq data. Nucleic Acids Res. 2010, 38:e13.
289. Farnham P.J. Insights from genomic profiling of transcription factors. Nat. Rev. Genet. 2009, 10:605-616.
290. Ramagopalan S.V., Heger A., Berlanga A.J., Maugeri N.J., Lincoln M.R., Burrell A., et al. A ChIP-seq defined genome-wide map of vitamin D receptor binding: associations with disease and evolution. Genome Res. 2010, 20:1352-1360.
291. Copeland N.G., Jenkins N.A., Court D.L. Recombineering: a powerful new tool for mouse functional genomics. Nat. Rev. Genet. 2001, 2:769-779.
292. Fu Q., Manolagas S.C., O'Brien C.A. Parathyroid hormone controls receptor activator of NF-kappaB ligand gene expression via a distant transcriptional enhancer. Mol. Cell Biol. 2006, 26:6453-6468.
293. Galli C., Zella L.A., Fretz J.A., Fu Q., Pike J.W., Weinstein R.S., et al. Targeted deletion of a distant transcriptional enhancer of the receptor activator of nuclear factor-kappaB ligand gene reduces bone remodeling and increases bone mass. Endocrinology 2008, 149:146-153.
294. Pink R.C., Eskiw C.H., Caley D.P., Carter D.R. Analysis of β-globin chromatin micro-environment using a novel 3C variant, 4Cv. PLoS One 5 2010.
295. Dostie J., Rousseau M., Blanchette M., Fraser J. Computing chromosome conformation. Methods Mol. Biol. 2010, 674:251-268.
296. Fraser J., Rousseau M., Shenker S., Ferraiuolo M.A., Hayashizaki Y., Blanchette M., et al. Chromatin conformation signatures of cellular differentiation. Genome Biol. 2009, 10:R37.
297. Lajoie B.R., van Berkum N.L., Sanyal A., Dekker J. My5C: web tools for chromosome conformation capture studies. Nat. Methods 2009, 6:690-691.
298. Lieberman-Aiden E., van Berkum N.L., Williams L., Imakaev M., Ragoczy T., Telling A., et al. Comprehensive mapping of long-range interactions reveals folding principles of the human genome. Science 2009, 326:289-293.
299. Vassetzky Y., Gavrilov A., Eivazova E., Priozhkova I., Lipinski M., Razin S. Chromosome conformation capture (from 3C to 5C) and its ChIP-based modification. Methods Mol. Biol. 2009, 567:171-188.
300. van Berkum N.L., Lieberman-Aiden E., Williams L., Imakaev M., Gnirke A., Mirny L.A., et al. Hi-C: a method to study the three-dimensional architecture of genomes. J. Vis. Exp. 2010.
301. 3 receptor gene expression and enhances hormone action. Mol. Endocrinol. 1992, 6:198-206.
302. Krishnan A.V., Feldman D. Regulation of vitamin D receptor abundance. Vitamin D 1997, 179-200. Academic Press, San Diego. D.G.F.P.J.W. Feldman (Ed.).
303. Maiti A., Hait N.C., Beckman M.J. Extracellular calcium-sensing receptor activation induces vitamin D receptor levels in proximal kidney HK-2G cells by a mechanism that requires phosphorylation of p38alpha MAPK. J. Biol. Chem. 2008, 283:175-183.
304. Mendoza F.J., Lopez I., Canalejo R., Almaden Y., Martin D., Aguilera-Tejero E., et al. Direct upregulation of parathyroid calcium-sensing receptor and vitamin D receptor by calcimimetics in uremic rats. Am. J. Physiol. Renal. Physiol. 2009, 296:F605-613.
305. Canadillas S., Canalejo R., Rodriguez-Ortiz M.E., Martinez-Moreno J.M., Estepa J.C., Zafra R., et al. The up-regulation of the parathyroid VDR expression by extracellular calcium is mediated by the ERK1/2-MAPK signaling pathway. Am. J. Physiol. Renal. Physiol. 2010.
306. Qi X., Pramanik R., Wang J., Schultz R.M., Maitra R.K., Han J., et al. The p38 and JNK pathways cooperate to trans-activate vitamin D receptor via c-Jun/AP-1 and sensitize human breast cancer cells to vitamin D(3)-induced growth inhibition. J. Biol. Chem. 2002, 277:25884-25892.
307. 3 24-hydroxylase. Mol. Cell Biol. 2005, 25:472-487.
308. 3 associated to the differentiation of human colon cancer cells. Carcinogenesis 2007, 28:1877-1884.
309. 3 is abrogated by Snail1 in human colon cancer cells. Endocr. Relat. Cancer 2007, 14:141-151.
310. Larriba M.J., Martín-Villar E., García J.M., Pereira F., Peña C., de Herreros A.G., et al. Snail2 cooperates with Snail1 in the repression of vitamin D receptor in colon cancer. Carcinogenesis 2009, 30:1459-1468.
311. Larriba M.J., Bonilla F., Muñoz A. The transcription factors Snail1 and Snail2 repress vitamin D receptor during colon cancer progression. J. Steroid Biochem. Mol. Biol. 2010, 121:106-109.
312. Pálmer H.G., Larriba M.J., García J.M., Ordóñez-Morán P., Peña C., Peiró S., et al. The transcription factor SNAIL represses vitamin D receptor expression and responsiveness in human colon cancer. Nat. Med. 2004, 10:917-919.
313. Mittal M.K., Myers J.N., Misra S., Bailey C.K., Chaudhuri G. In vivo binding to and functional repression of the VDR gene promoter by SLUG in human breast cells. Biochem. Biophys. Res. Commun. 2008, 372:30-34.
314. Bai S., Wang H., Shen J., Zhou R., Bushinsky D.A., Favus M.J. Elevated vitamin D receptor levels in genetic hypercalciuric stone-forming rats are associated with downregulation of Snail. J. Bone Miner. Res. 2010, 25:830-840.
315. Vitamin D 1997, Academic Press, San Diego. D. Feldman, F. Glorieux, J. Pike (Eds.).
316. Vitamin D 2005, Elsevier, San Diego. second ed. D. Feldman, J. Pike, F. Glorieux (Eds.).
317. 3 receptors by vitamin D analogs in cultured mammalian cells. Endocrinology 1985, 117:2203-2210.
318. 3 but does not directly modulate the bioactive levels of the hormone in vivo. Endocrinology 2008, 149:3656-3667.
319. 3 results from a selective and prolonged induction of intestinal calcium-regulating genes. Endocrinology 2009, 150:3448-3456.
320. 3 receptor during neonatal development in the rat. Arch. Biochem. Biophys. 1988, 261:241-249.
321. 3-binding macromolecules in human B lymphocytes: effects on immunoglobulin production. J. Immunol. 1986, 136:2734-2740.
322. 3: a novel immunoregulatory hormone. Science 1984, 224:1438-1440.
323. 3 receptor gene (VDR) are colocalized on human chromosome arm 12q and rat chromosome 7. Genomics 1991, 11:168-173.
324. Miyamoto K., Kesterson R.A., Yamamoto H., Taketani Y., Nishiwaki E., Tatsumi S., et al. Structural organization of the human vitamin D receptor chromosomal gene and its promoter. Mol. Endocrinol. 1997, 11:1165-1179.
325. Jehan F., DeLuca H.F. Cloning and characterization of the mouse vitamin D receptor promoter. PNAS 1997, 94:10138-10143.
326. Jehan F., DeLuca H.F. The mouse vitamin D receptor is mainly expressed through an Sp1-driven promoter in vivo. Arch. Biochem. Biophys. 2000, 377:273-283.
327. Pike J.W., Meyer M.B., Martowicz M.L., Bishop K.A., Lee S.M., Nerenz R.D., et al. Emerging regulatory paradigms for control of gene
328. Huening M., Yehia G., Molina C.A., Christakos S. Evidence for a regulatory role of inducible cAMP early repressor in protein kinase A-mediated enhancement of vitamin D receptor expression and modulation of hormone action. Mol. Endocrinol. 2002, 16:2052-2064.
329. Lee S.M., Bishop K.A., Meyer M.B., Nerenz R.D., O'Brien C.A., Pike J.W. Both intronic and upstream distal enhancers mediate factor- and tissue-specific expression of the mouse VDR chromosomal gene in cells and in BAC clone transgenic mice. Mol. Endocrinol. 2011.
330. Lee S.M., Bishop K.A., Meyer M.B., Nerenz R.D., O'Brien C.A., Pike J.W. A transgene containing the human vitamin D receptor gene locus recapitulates endogenous tissue-specific expression of the receptor in the mouse. Mol. Endocrinol. 2011.
331. Santiso-Mere D., Sone T., Pike J.W., Hilliard G.M.T., McDonnell D.P. Positive regulation of the vitamin D receptor by its cognate ligand in heterologous expression systems. Mol. Endocrinol. 1993, 7:833-839.
332. Hsieh J.C., Jurutka P.W., Galligan M.A., Terpening C.M., Haussler C.A., Samuels D.S., et al. Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function. Proc. Natl. Acad. Sci. USA 1991, 88:9315-9319.
333. Hsieh J.C., Jurutka P.W., Nakajima S., Galligan M.A., Haussler C.A., Shimizu Y., et al. Phosphorylation of the human vitamin D receptor by protein kinase C. Biochemical and functional evaluation of the serine 51 recognition site. J. Biol. Chem. 1993, 268:15118-15126.
334. 3-dependent transactivation. Biochem. Biophys. Res. Commun. 2004, 324:801-809.
335. Jurutka P.W., Hsieh J.C., MacDonald P.N., Terpening C.M., Haussler C.A., Haussler M.R., et al. Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells. J. Biol. Chem. 1993, 268:6791-6799.
336. 3 receptor by cAMP-dependent protein kinase, in vitro, and in transfected COS-7 cells. Biochem. Biophys. Res. Commun. 1993, 191:1089-1096.
337. Jurutka P.W., Hsieh J.C., Nakajima S., Haussler C.A., Whitfield G.K., Haussler M.R. Human vitamin D receptor phosphorylation by casein kinase II at Ser-208 potentiates transcriptional activation. Proc. Natl. Acad. Sci. USA 1996, 93:3519-3524.
338. 3 modulates phosphorylation of serine 205 in the human vitamin D receptor: site-directed mutagenesis of this residue promotes alternative phosphorylation. Biochemistry 1994, 33:4300-4311.
339. 3 receptor modulates the interaction with transcriptional coactivators. J. Steroid Biochem. Mol. Biol. 2007, 103:425-429.