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Volumn 17, Issue 12, 2002, Pages 2196-2205

Inhibition of 1,25-dihydroxyvitamin D3-dependent transcription by synthetic LXXLL peptide antagonists that target the activation domains of the vitamin D and retinoid X receptors

Author keywords

Comodulators; LXXLL motifs; Osteocalcin; Peptides; Retinoid X receptor; Transcription; Vitamin D receptor

Indexed keywords

ALITRETINOIN; CALCITRIOL; HYBRID PROTEIN; OSTEOCALCIN; PEPTIDE; RETINOIC ACID; RETINOID X RECEPTOR; THYMIDINE KINASE; VITAMIN D RECEPTOR; CALCITRIOL RECEPTOR; OLIGOPEPTIDE; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0036894463     PISSN: 08840431     EISSN: None     Source Type: Journal    
DOI: 10.1359/jbmr.2002.17.12.2196     Document Type: Article
Times cited : (46)

References (44)
  • 1
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM 1989 The steroid and thyroid hormone receptor superfamily. Science 240:889-895.
    • (1989) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 7
    • 0025724977 scopus 로고
    • A 55 kilodalton accessory factor facilitates vitamin D receptor DNA binding
    • Sone T, Ozono K, Pike JW 1991 A 55 kilodalton accessory factor facilitates vitamin D receptor DNA binding. Mol Endocrinol 5:1578-1586.
    • (1991) Mol Endocrinol , vol.5 , pp. 1578-1586
    • Sone, T.1    Ozono, K.2    Pike, J.W.3
  • 11
    • 0029737695 scopus 로고    scopus 로고
    • Transcriptional activation and dimerization functions in the human vitamin D receptor
    • Jin CH, Kerner SA, Hong MH, Pike JW 1996 Transcriptional activation and dimerization functions in the human vitamin D receptor. Mol Endocrinol 10:945-957.
    • (1996) Mol Endocrinol , vol.10 , pp. 945-957
    • Jin, C.H.1    Kerner, S.A.2    Hong, M.H.3    Pike, J.W.4
  • 12
    • 0029123088 scopus 로고
    • 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
    • Whitefield GK, Hsieh J-C, Nakajima S, MacDonald PN, Thompson PD, Jurutka PW, Haussler CA, Haussler MR 1995 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 9:1166-1179.
    • (1995) Mol Endocrinol , vol.9 , pp. 1166-1179
    • Whitefield, G.K.1    Hsieh, J.-C.2    Nakajima, S.3    MacDonald, P.N.4    Thompson, P.D.5    Jurutka, P.W.6    Haussler, C.A.7    Haussler, M.R.8
  • 13
    • 0037192817 scopus 로고    scopus 로고
    • The structural basis for the specificity of retinoid-X-receptor selective agonists: New insights into the role of helix H12
    • Love JD, Gooch JT, Benko S, Li C, Nagy L, Chatterjee VKK, Evans RM, Schwabe JWR 2002 The structural basis for the specificity of retinoid-X-receptor selective agonists: New insights into the role of helix H12. J Biol Chem 277: 11385-11391.
    • (2002) J Biol Chem , vol.277 , pp. 11385-11391
    • Love, J.D.1    Gooch, J.T.2    Benko, S.3    Li, C.4    Nagy, L.5    Chatterjee, V.K.K.6    Evans, R.M.7    Schwabe, J.W.R.8
  • 15
    • 0029930872 scopus 로고    scopus 로고
    • Modulation of nuclear receptor interactions by ligands: Kinetic analysis using surface plasmon resonance
    • Cheskis B. Freedman LP 1996 Modulation of nuclear receptor interactions by ligands: Kinetic analysis using surface plasmon resonance. Biochemistry 35:3309-3318.
    • (1996) Biochemistry , vol.35 , pp. 3309-3318
    • Cheskis, B.1    Freedman, L.P.2
  • 16
    • 0034731436 scopus 로고    scopus 로고
    • Dimerization with retinoid X receptors promotes nuclear localization and subnuclear targeting of vitamin D receptors
    • Prufer K, Racz A, Lin GC, Barsony J 2000 Dimerization with retinoid X receptors promotes nuclear localization and subnuclear targeting of vitamin D receptors. J Biol Chem 275:41114-41125.
    • (2000) J Biol Chem , vol.275 , pp. 41114-41125
    • Prufer, K.1    Racz, A.2    Lin, G.C.3    Barsony, J.4
  • 17
    • 0034603725 scopus 로고    scopus 로고
    • 3 receptor: A network of coactivator interactions
    • 3 receptor: A network of coactivator interactions. Gene 246:9-21.
    • (2000) Gene , vol.246 , pp. 9-21
    • Rachez, C.1    Freedman, L.P.2
  • 19
    • 0033521956 scopus 로고    scopus 로고
    • The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Spl
    • Ryu S, Zhou S, Ladurner AG, Tjian R 1999 The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Spl. Nature 397:446-450.
    • (1999) Nature , vol.397 , pp. 446-450
    • Ryu, S.1    Zhou, S.2    Ladurner, A.G.3    Tjian, R.4
  • 20
    • 0034034013 scopus 로고    scopus 로고
    • The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes
    • Rachez C, Gamble M, Chang CP, Atkins GB, Lazar MA, Freedman LP 2000 The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes. Mol Cell Biol 20:2718-2726.
    • (2000) Mol Cell Biol , vol.20 , pp. 2718-2726
    • Rachez, C.1    Gamble, M.2    Chang, C.P.3    Atkins, G.B.4    Lazar, M.A.5    Freedman, L.P.6
  • 21
    • 0033996567 scopus 로고    scopus 로고
    • 3-stimulated alkaline phosphatase in human osteosarcoma cells
    • 3-stimulated alkaline phosphatase in human osteosarcoma cells. Calcif Tissue Int 66:370-374.
    • (2000) Calcif Tissue Int , vol.66 , pp. 370-374
    • Gill, R.K.1    Bell, N.H.2
  • 22
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong H, Kohli K, Garabedian MJ, Stallcup MR 1997 GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol Cell Biol 17:2735-2744.
    • (1997) Mol Cell Biol , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 23
    • 0034612264 scopus 로고    scopus 로고
    • The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development
    • Xu J, Liao L, Ning G, Yoshida-Komiya H, Deng C, O'Malley BW 2000 The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc Natl Acad Sci USA 97:6379-6384.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6379-6384
    • Xu, J.1    Liao, L.2    Ning, G.3    Yoshida-Komiya, H.4    Deng, C.5    O'Malley, B.W.6
  • 24
    • 0035798571 scopus 로고    scopus 로고
    • Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription
    • Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN 2001 Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription. J Biol Chem 276:40614-40620.
    • (2001) J Biol Chem , vol.276 , pp. 40614-40620
    • Zhang, C.1    Baudino, T.A.2    Dowd, D.R.3    Tokumaru, H.4    Wang, W.5    MacDonald, P.N.6
  • 25
    • 0032404015 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the vitamin D receptor (VDR) and a putative role for SUG1 interaction with the AF-2 domain of VDR
    • Masuyama H, MacDonald PN 1998 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 71:429-440.
    • (1998) J Cell Biochem , vol.71 , pp. 429-440
    • Masuyama, H.1    MacDonald, P.N.2
  • 26
    • 0036135671 scopus 로고    scopus 로고
    • Genetic ablation of the steroid receptor coactivator-ubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction
    • Smith CL, DeVera DG, Lamb DJ, Nawaz Z, Jiang YH, Beaudet AL, O'Malley BW 2002 Genetic ablation of the steroid receptor coactivator-ubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction. Mol Cell Biol 22:525-535.
    • (2002) Mol Cell Biol , vol.22 , pp. 525-535
    • Smith, C.L.1    DeVera, D.G.2    Lamb, D.J.3    Nawaz, Z.4    Jiang, Y.H.5    Beaudet, A.L.6    O'Malley, B.W.7
  • 30
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/ coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL 1998 The structural basis of estrogen receptor/ coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 32
    • 0033513582 scopus 로고    scopus 로고
    • Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: Discovery of peptide antagonists of estrogen receptors alpha and beta
    • Chang C, Norris JD, Gron H, Paige LA, Hamilton PT, Kenan DJ, Fowlkes D, McDonnell DP 1999 Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: Discovery of peptide antagonists of estrogen receptors alpha and beta. Mol Cell Biol 19:8226-8239.
    • (1999) Mol Cell Biol , vol.19 , pp. 8226-8239
    • Chang, C.1    Norris, J.D.2    Gron, H.3    Paige, L.A.4    Hamilton, P.T.5    Kenan, D.J.6    Fowlkes, D.7    McDonnell, D.P.8
  • 33
    • 0034353127 scopus 로고    scopus 로고
    • Development of peptide antagonists that target estrogen receptor beta-coactivator interactions
    • Hall JM, Chang CY, McDonnell DP 2000 Development of peptide antagonists that target estrogen receptor beta-coactivator interactions. Mol Endocrinol 14:2010-2023.
    • (2000) Mol Endocrinol , vol.14 , pp. 2010-2023
    • Hall, J.M.1    Chang, C.Y.2    McDonnell, D.P.3
  • 34
    • 0025938132 scopus 로고
    • A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR
    • Mangelsdorf DJ, Umesono K, Kliewer SA, Borgmeyer U, Ong ES, Evans RM 1991 A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR. Cell 66:555-561.
    • (1991) Cell , vol.66 , pp. 555-561
    • Mangelsdorf, D.J.1    Umesono, K.2    Kliewer, S.A.3    Borgmeyer, U.4    Ong, E.S.5    Evans, R.M.6
  • 36
    • 0030027490 scopus 로고    scopus 로고
    • 3 receptor- and retinoid X receptor-mediated gene activation in vivo
    • 3 receptor- and retinoid X receptor-mediated gene activation in vivo. Mol Cell Biol 16:1006-1016.
    • (1996) Mol Cell Biol , vol.16 , pp. 1006-1016
    • Lemon, B.D.1    Freedman, L.P.2
  • 39
    • 0035204814 scopus 로고    scopus 로고
    • Vitamin D: Its role and uses in immunology
    • DeLuca HF, Cantorna MT 2001 Vitamin D: Its role and uses in immunology. FASEB J 15:2579-2585.
    • (2001) FASEB J , vol.15 , pp. 2579-2585
    • DeLuca, H.F.1    Cantorna, M.T.2
  • 41
    • 0030112256 scopus 로고    scopus 로고
    • The concept of multiple vitamin D signaling pathways
    • Carlberg C 1996 The concept of multiple vitamin D signaling pathways. J Investig Dermatol Symp Proc 1:10-14.
    • (1996) J Investig Dermatol Symp Proc , vol.1 , pp. 10-14
    • Carlberg, C.1
  • 42
    • 0032562621 scopus 로고    scopus 로고
    • 3 receptor. Implications for allosteric influences on nuclear receptor structure and function by a DNA element
    • 3 receptor. Implications for allosteric influences on nuclear receptor structure and function by a DNA element. J Biol Chem 273:10338-10348.
    • (1998) J Biol Chem , vol.273 , pp. 10338-10348
    • Towers, T.L.1    Freedman, L.P.2
  • 43
    • 0030032309 scopus 로고    scopus 로고
    • A composite element binding the vitamin D receptor, retinoid X receptor alpha and a member of the CTF/NF-1 family of transcription factors mediates the vitamin D responsiveness of the c-fos promoter
    • Candeliere GA, Jurutka PW, Haussler MR, St.-Arnaud R 1996 A composite element binding the vitamin D receptor, retinoid X receptor alpha and a member of the CTF/NF-1 family of transcription factors mediates the vitamin D responsiveness of the c-fos promoter. Mol Cell Biol 16:584-592.
    • (1996) Mol Cell Biol , vol.16 , pp. 584-592
    • Candeliere, G.A.1    Jurutka, P.W.2    Haussler, M.R.3    St.-Arnaud, R.4
  • 44
    • 0029878795 scopus 로고    scopus 로고
    • Vitamin D receptor binding to the negative human parathyroid hormone vitamin D response element does not require the retinoid x receptor
    • Mackey SL, Heymont JL, Kronenberg HM, Demay MB 1996 Vitamin D receptor binding to the negative human parathyroid 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.