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Volumn 127, Issue 5, 2000, Pages 717-722

The function of vitamin D receptor in vitamin D action

Author keywords

Nuclear receptor; Transcription factor; VDR KO mice; Vitamin D; Vitamin D 1 hydroxylase

Indexed keywords

TRANSCRIPTION FACTOR; VITAMIN D; VITAMIN D RECEPTOR;

EID: 0034082854     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022662     Document Type: Review
Times cited : (180)

References (45)
  • 1
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • Bouillon, R., Okamura, W.H., and Norman, A.W. (1995) Structure-function relationships in the vitamin D endocrine system. Endocr. Rev. 16, 200-257
    • (1995) Endocr. Rev. , vol.16 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 2
    • 0027050850 scopus 로고
    • Newly identified actions of the vitamin D endocrine system
    • Walters, M.R. (1992) Newly identified actions of the vitamin D endocrine system. Endocr. Rev. 13, 719-764
    • (1992) Endocr. Rev. , vol.13 , pp. 719-764
    • Walters, M.R.1
  • 4
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypocalcemic rickets
    • The HYP Consortoim (1995) A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypocalcemic rickets. Nat. Genet. 11, 130-136
    • (1995) Nat. Genet. , vol.11 , pp. 130-136
  • 8
    • 0020185344 scopus 로고
    • The vitamin D endocrine system:Steroid metabolism, hormone receptors, and biological response (calcium binding proteins)
    • Norman, A.W., Roth, J., and Orchi, L. (1982) The vitamin D endocrine system:steroid metabolism, hormone receptors, and biological response (calcium binding proteins). Endocr. Rev. 3, 331-366
    • (1982) Endocr. Rev. , vol.3 , pp. 331-366
    • Norman, A.W.1    Roth, J.2    Orchi, L.3
  • 9
    • 0022507477 scopus 로고
    • The metabolism and functions of vitamin D
    • DeLuca, H.F. (1986) The metabolism and functions of vitamin D. Adv. Exp. Med. Biol. 196, 361-375
    • (1986) Adv. Exp. Med. Biol. , vol.196 , pp. 361-375
    • DeLuca, H.F.1
  • 13
    • 0033515428 scopus 로고    scopus 로고
    • Increasing the complexity of coactivation in nuclear receptor signalin
    • Freedman, L.P. (1999) Increasing the complexity of coactivation in nuclear receptor signalin. Cell 97, 5-8
    • (1999) Cell , vol.97 , pp. 5-8
    • Freedman, L.P.1
  • 14
    • 0033614417 scopus 로고    scopus 로고
    • Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
    • Rachez, C. et al. (1999) Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature 398, 824-828
    • (1999) Nature , vol.398 , pp. 824-828
    • Rachez, C.1
  • 17
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/ p300
    • Chen, H., Lin, R.J., Schiltz, R.L. et al. (1997) Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/ p300. Cell 90, 569-580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3
  • 20
    • 0032493455 scopus 로고    scopus 로고
    • TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts direct 1y with nuclear receptor in a ligand-depent fashion
    • Yuan, C.X., Ito, M., Fondell, J.D., Fu, Z., and Roeder, R.G. (1998) TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts direct 1y with nuclear receptor in a ligand-depent fashion. Proc. Natl. Acad. Sci. USA 95, 7939-7944
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7939-7944
    • Yuan, C.X.1    Ito, M.2    Fondell, J.D.3    Fu, Z.4    Roeder, R.G.5
  • 21
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor corepressor
    • Horlein, A.J. et al. (1995) Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor corepressor. Nature 377, 397-404
    • (1995) Nature , vol.377 , pp. 397-404
    • Horlein, A.J.1
  • 22
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy, L., Kao, H.Y., Chakravarti, D., Lin, R.J., Hassig, C.A., Ayer, D.E., Schreiber, S.L., and Evans, R.M. (1997) Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89, 373-380
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6    Schreiber, S.L.7    Evans, R.M.8
  • 23
    • 0025607934 scopus 로고
    • The molecular basis of hereditary 1,25-dihydroxyvitamin D3 resistant rickets in seven related families
    • Malloy, P.J., Hochberg, Z., Tiosano, D., Pike, J.W., Hughes, M.R., and Feldman, D. (1990) The molecular basis of hereditary 1,25-dihydroxyvitamin D3 resistant rickets in seven related families. J. Clin. Invest. 86, 2071-2079
    • (1990) J. Clin. Invest. , vol.86 , pp. 2071-2079
    • Malloy, P.J.1    Hochberg, Z.2    Tiosano, D.3    Pike, J.W.4    Hughes, M.R.5    Feldman, D.6
  • 25
    • 0029584593 scopus 로고
    • Nonsteroidy nuclear receptors: What are genetic studies telling us about their role in real life?
    • Kastner, P., Mark, M., and Chambon, P. (1995) Nonsteroidy nuclear receptors: what are genetic studies telling us about their role in real life? Cell 83, 859-869
    • (1995) Cell , vol.83 , pp. 859-869
    • Kastner, P.1    Mark, M.2    Chambon, P.3
  • 26
    • 0030610422 scopus 로고    scopus 로고
    • Targeted ablation of the vitamin D receptor: An animal model of vitamin D-dependent rickets type II with alopecia
    • Li, Y.C., Pirro, A.E., Amling, M., Delling, G., Baron, R., Bronson, R., and Demay M.B. (1997) Targeted ablation of the vitamin D receptor: an animal model of vitamin D-dependent rickets type II with alopecia. Proc. Natl. Acad. Sci. USA 94, 9831-9835
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9831-9835
    • Li, Y.C.1    Pirro, A.E.2    Amling, M.3    Delling, G.4    Baron, R.5    Bronson, R.6    Demay, M.B.7
  • 27
    • 0033304730 scopus 로고    scopus 로고
    • Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families
    • Suda, T. and Takahashi, N. (1999) Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families. Endocr. Rev. 20, 345-357
    • (1999) Endocr. Rev. , vol.20 , pp. 345-357
    • Suda, T.1    Takahashi, N.2
  • 28
    • 0025737036 scopus 로고
    • Deficiency of osteoclasts in osteopetrotic mice is due to a defect in the local microenvironment provided by osteoblastic cells
    • Takahashi, N., Udagawa, N., Akatsu, T. et al. (1991) Deficiency of osteoclasts in osteopetrotic mice is due to a defect in the local microenvironment provided by osteoblastic cells. Endocrinology 128, 1792-1796
    • (1991) Endocrinology , vol.128 , pp. 1792-1796
    • Takahashi, N.1    Udagawa, N.2    Akatsu, T.3
  • 30
    • 0030782757 scopus 로고    scopus 로고
    • Cloning of human 25-hydroxyvitamin D-1α-hydroxylase a mutations causing vitamin D-dependent rickets type 1
    • Fu, G.K., Lin, D., Zhang, M.Y.H., Bikle, D.D., Shackleton, C.H.L., Miller, W.L., Portale, A.A. (1997) Cloning of human 25-hydroxyvitamin D-1α-hydroxylase a mutations causing vitamin D-dependent rickets type 1. Mol. Endocrinol. 11, 1961-1970
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1961-1970
    • Fu, G.K.1    Lin, D.2    Zhang, M.Y.H.3    Bikle, D.D.4    Shackleton, C.H.L.5    Miller, W.L.6    Portale, A.A.7
  • 32
    • 0018133886 scopus 로고
    • Serum1,25-dihydroxyvitamin D levels in normal subjects and patients with hereditary rickets or bone disease
    • Scriver, C.R., Reade, T.M., DeLuca, H.F., and Hamstra, A.J. (1978) Serum1,25-dihydroxyvitamin D levels in normal subjects and patients with hereditary rickets or bone disease. N. Engl. J. Med. 299, 976-979
    • (1978) N. Engl. J. Med. , vol.299 , pp. 976-979
    • Scriver, C.R.1    Reade, T.M.2    DeLuca, H.F.3    Hamstra, A.J.4
  • 33
    • 0025369001 scopus 로고
    • Mapping autosomal recessive vitamin D dependency type 1 to chromosomal 12q14 by linkage abalysis
    • Labuda, M., Morgan, K., and Glorieux, F.H. (1990) Mapping autosomal recessive vitamin D dependency type 1 to chromosomal 12q14 by linkage abalysis. Am. J. Hum. Genet. 47, 28-36
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 28-36
    • Labuda, M.1    Morgan, K.2    Glorieux, F.H.3
  • 35
    • 0024598467 scopus 로고
    • Physiologic regulation of the serum concentration of 1,25-dihydroxyvitamin D by phosphorus in normal men
    • Portale, A.A., Halloran, B.P., Morris, R.C., Jr. (1989) Physiologic regulation of the serum concentration of 1,25-dihydroxyvitamin D by phosphorus in normal men. J. Clin. Invest. 83, 1494-1499
    • (1989) J. Clin. Invest. , vol.83 , pp. 1494-1499
    • Portale, A.A.1    Halloran, B.P.2    Morris R.C., Jr.3
  • 36
    • 1942447828 scopus 로고    scopus 로고
    • Enzymatic properties of human 25-hydroxyvitamin D3 1a-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli
    • Sawada, N., Sakaki, T., Kitanaka, S., Takeyama, K., Kato, S., and Inouye, K. (1999) Enzymatic properties of human 25-hydroxyvitamin D3 1a-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli. Eur. J. Biochem. 265, 950-956
    • (1999) Eur. J. Biochem. , vol.265 , pp. 950-956
    • Sawada, N.1    Sakaki, T.2    Kitanaka, S.3    Takeyama, K.4    Kato, S.5    Inouye, K.6
  • 37
    • 0002819595 scopus 로고    scopus 로고
    • Enzymatic properties of mouse 25-hydroxyvitamin D3 1a-hydroxylase expressed in Escherichia coli
    • Sakaki, T., Sawada, N., Takeyama, K., Kato, S., and Inouye, K. (1999) Enzymatic properties of mouse 25-hydroxyvitamin D3 1a-hydroxylase expressed in Escherichia coli. Eur. J. Biochem. 259, 731-738
    • (1999) Eur. J. Biochem. , vol.259 , pp. 731-738
    • Sakaki, T.1    Sawada, N.2    Takeyama, K.3    Kato, S.4    Inouye, K.5
  • 38
    • 0019485450 scopus 로고
    • Localization of 25-hydroxyvitamin D3-1a-hydroxylase along the rat nephron
    • Kawashima, H., Torikai, S., and Kurokawa, K. (1981) Localization of 25-hydroxyvitamin D3-1a-hydroxylase along the rat nephron. Proc. Natl. Acad. Sci. USA 78, 1199-1203
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1199-1203
    • Kawashima, H.1    Torikai, S.2    Kurokawa, K.3
  • 40
    • 0018396505 scopus 로고
    • Regulation of the hydroxylation of 25-hydroxyvitamin D3-1α-hydroxylase in vivo and in primary cultures of chick kidney cells
    • Henry, H.L. (1979) Regulation of the hydroxylation of 25-hydroxyvitamin D3-1α-hydroxylase in vivo and in primary cultures of chick kidney cells. J. Biol. Chem. 254, 2722-2729
    • (1979) J. Biol. Chem. , vol.254 , pp. 2722-2729
    • Henry, H.L.1
  • 41
    • 0021989993 scopus 로고
    • Parathyroid hormone modulation of 25-hydroxyvitamin D3 metabolism by cultured chick kidney cells is mimicked and enhanced by forskolin
    • Henry, H.L. (1985) Parathyroid hormone modulation of 25-hydroxyvitamin D3 metabolism by cultured chick kidney cells is mimicked and enhanced by forskolin. Endocrinology 116, 503-507
    • (1985) Endocrinology , vol.116 , pp. 503-507
    • Henry, H.L.1
  • 44
    • 0026693809 scopus 로고
    • Sequences in the human parathyroid hormone gene that bind the 1,25-dihydroxyvitamin D receptor and mediate transcriptional response to 1,25-dihydroxyvitamin D
    • Demay, M.B., Kiernan, M.S., DeLuca, H.F., and Kronenberg, H.M. (1992) Sequences in the human parathyroid hormone gene that bind the 1,25-dihydroxyvitamin D receptor and mediate transcriptional response to 1,25-dihydroxyvitamin D. Proc. Natl. Acad. Sci. USA 89, 8097-8101
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8097-8101
    • Demay, M.B.1    Kiernan, M.S.2    DeLuca, H.F.3    Kronenberg, H.M.4
  • 45
    • 0029878795 scopus 로고    scopus 로고
    • Vitamin D receptor binding to the negative human prathyroid hormone vitamin D response element does not require the retinoid X receptor
    • Mackey, S.L., Heymont, J.L., Kronenberg, H.M., and Demay, M.B. (1996) Vitamin D receptor binding to the negative human prathyroid hormone vitamin D response element does not require the retinoid X receptor. Mol. Endocrinol. 10, 298-305
    • (1996) Mol. Endocrinol. , vol.10 , pp. 298-305
    • Mackey, S.L.1    Heymont, J.L.2    Kronenberg, H.M.3    Demay, M.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.