메뉴 건너뛰기




Volumn 150, Issue 2, 2009, Pages 679-686

Inactivation of the human vitamin D receptor by caspase-3

Author keywords

[No Author keywords available]

Indexed keywords

CALCITRIOL; CASPASE 3; CASPASE 6; CASPASE 7; STAUROSPORINE; VITAMIN D RECEPTOR;

EID: 59649129312     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2008-1217     Document Type: Article
Times cited : (29)

References (39)
  • 3
    • 23744437421 scopus 로고    scopus 로고
    • Noncalcemic actions of vitamin D receptor ligands
    • Nagpal S, Na S, Rathnachalam R 2005 Noncalcemic actions of vitamin D receptor ligands. Endocr Rev 26:662-687
    • (2005) Endocr Rev , vol.26 , pp. 662-687
    • Nagpal, S.1    Na, S.2    Rathnachalam, R.3
  • 4
    • 84884080872 scopus 로고    scopus 로고
    • Vitamin D: Biology, action, and clinical implications
    • Marcus R, Feldman D, Nelson DA, Rosen CJ, eds, 3rd ed. San Diego: Academic Press;
    • Feldman D, Malloy PJ, Krishnan AV, Balint E 2007 Vitamin D: biology, action, and clinical implications. In: Marcus R, Feldman D, Nelson DA, Rosen CJ, eds. Osteoporosis. 3rd ed. San Diego: Academic Press; 317-382
    • (2007) Osteoporosis , pp. 317-382
    • Feldman, D.1    Malloy, P.J.2    Krishnan, A.V.3    Balint, E.4
  • 5
    • 34548202165 scopus 로고    scopus 로고
    • Vitamin D signalling pathways in cancer: Potential for anticancer therapeutics
    • Deeb KK, Trump DL, Johnson CS 2007 Vitamin D signalling pathways in cancer: potential for anticancer therapeutics. Nat Rev Cancer 7:684-700
    • (2007) Nat Rev Cancer , vol.7 , pp. 684-700
    • Deeb, K.K.1    Trump, D.L.2    Johnson, C.S.3
  • 8
    • 34547737407 scopus 로고    scopus 로고
    • Dissociation of growth arrest and CYP24 induction by VDR ligands in mammary tumor cells
    • Valrance ME, Brunet AH, Acosta A, Welsh J 2007 Dissociation of growth arrest and CYP24 induction by VDR ligands in mammary tumor cells. J Cell Biochem 101:1505-1519
    • (2007) J Cell Biochem , vol.101 , pp. 1505-1519
    • Valrance, M.E.1    Brunet, A.H.2    Acosta, A.3    Welsh, J.4
  • 9
    • 0035937751 scopus 로고    scopus 로고
    • Narvaez CJ, Welsh J 2001 Role of mitochondria and caspases in vitamin D-mediated apoptosis of MCF-7 breast cancer cells. J Biol Chem 276:91019107
    • Narvaez CJ, Welsh J 2001 Role of mitochondria and caspases in vitamin D-mediated apoptosis of MCF-7 breast cancer cells. J Biol Chem 276:91019107
  • 11
    • 0034283578 scopus 로고    scopus 로고
    • Stennicke HR, Renatus M, Meldal M, Salvesen GS 2000 Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem J 350(Pt 2):563-568
    • Stennicke HR, Renatus M, Meldal M, Salvesen GS 2000 Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem J 350(Pt 2):563-568
  • 12
    • 0036470319 scopus 로고    scopus 로고
    • Reprieval from execution: The molecular basis of caspase inhibition
    • Stennicke HR, Ryan CA, Salvesen GS 2002 Reprieval from execution: the molecular basis of caspase inhibition. Trends Biochem Sci 27:94-101
    • (2002) Trends Biochem Sci , vol.27 , pp. 94-101
    • Stennicke, H.R.1    Ryan, C.A.2    Salvesen, G.S.3
  • 14
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM 1997 Caspases: the executioners of apoptosis. Biochem J 326(Pt1):1-16
    • (1997) Biochem J , vol.326 , Issue.PT1 , pp. 1-16
    • Cohen, G.M.1
  • 17
    • 33744963542 scopus 로고    scopus 로고
    • p53 is cleaved by caspases generating fragments localizing to mitochondria
    • Sayan BS, Sayan AE, Knight RA, Melino G, Cohen GM 2006 p53 is cleaved by caspases generating fragments localizing to mitochondria. J Biol Chem 281:13566-13573
    • (2006) J Biol Chem , vol.281 , pp. 13566-13573
    • Sayan, B.S.1    Sayan, A.E.2    Knight, R.A.3    Melino, G.4    Cohen, G.M.5
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0033981234 scopus 로고    scopus 로고
    • Heterogeneous apoptotic responses of prostate cancer cell lines identify an association between sensitivity to staurosporine- induced apoptosis, expression of Bcl-2 family members, and caspase activation
    • Marcelli M, Marani M, Li X, Sturgis L, Haidacher SJ, Trial JA, Mannucci R, Nicoletti I, Denner L 2000 Heterogeneous apoptotic responses of prostate cancer cell lines identify an association between sensitivity to staurosporine- induced apoptosis, expression of Bcl-2 family members, and caspase activation. Prostate 42:260-273
    • (2000) Prostate , vol.42 , pp. 260-273
    • Marcelli, M.1    Marani, M.2    Li, X.3    Sturgis, L.4    Haidacher, S.J.5    Trial, J.A.6    Mannucci, R.7    Nicoletti, I.8    Denner, L.9
  • 21
    • 0036844298 scopus 로고    scopus 로고
    • A novel mutation in helix 12 of the vitamin D receptor impairs coactivator interaction and causes hereditary 1,25-dihydroxyvitamin D-resistant rickets without alopecia
    • Malloy PJ, Xu R, Peng L, Clark PA, Feldman D 2002 A novel mutation in helix 12 of the vitamin D receptor impairs coactivator interaction and causes hereditary 1,25-dihydroxyvitamin D-resistant rickets without alopecia. Mol Endocrinol 16:2538-2546
    • (2002) Mol Endocrinol , vol.16 , pp. 2538-2546
    • Malloy, P.J.1    Xu, R.2    Peng, L.3    Clark, P.A.4    Feldman, D.5
  • 22
    • 0031038088 scopus 로고    scopus 로고
    • Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness
    • Malloy PJ, Eccleshall TR, Gross C, Van Maldergem L, Bouillon R, Feldman D 1997 Hereditary vitamin D resistant rickets caused by a novel mutation in the vitamin D receptor that results in decreased affinity for hormone and cellular hyporesponsiveness. J Clin Invest 99:297-304
    • (1997) J Clin Invest , vol.99 , pp. 297-304
    • Malloy, P.J.1    Eccleshall, T.R.2    Gross, C.3    Van Maldergem, L.4    Bouillon, R.5    Feldman, D.6
  • 23
    • 33847367323 scopus 로고    scopus 로고
    • Nonapoptotic functions of caspases: Caspases as regulatory molecules for immunity and cell-fate determination
    • Kuranaga E, Miura M 2007 Nonapoptotic functions of caspases: caspases as regulatory molecules for immunity and cell-fate determination. Trends Cell Biol 17:135-144
    • (2007) Trends Cell Biol , vol.17 , pp. 135-144
    • Kuranaga, E.1    Miura, M.2
  • 24
    • 0033556005 scopus 로고    scopus 로고
    • Marcelli M, Cunningham GR, Walkup M, He Z, Sturgis L, Kagan C, Mannucci R, Nicoletti I, Teng B, Denner L 1999 Signaling pathway activated during apoptosis of the prostate cancer cell line LNCaP: overexpres- sionofcaspase-7asanewgenetherapystrategyforprostatecancer.Cancer Res 59:382-390
    • Marcelli M, Cunningham GR, Walkup M, He Z, Sturgis L, Kagan C, Mannucci R, Nicoletti I, Teng B, Denner L 1999 Signaling pathway activated during apoptosis of the prostate cancer cell line LNCaP: overexpres- sionofcaspase-7asanewgenetherapystrategyforprostatecancer.Cancer Res 59:382-390
  • 25
    • 0037082102 scopus 로고    scopus 로고
    • Treatment of COS-7 cells with protea- some inhibitors or γ-interferon reduces the increase in caspase 3 activity associated with staurosporine-induced apoptosis
    • Brophy VA, Tavare JM, Rivett AJ 2002 Treatment of COS-7 cells with protea- some inhibitors or γ-interferon reduces the increase in caspase 3 activity associated with staurosporine-induced apoptosis. Arch Biochem Biophys 397:199-205
    • (2002) Arch Biochem Biophys , vol.397 , pp. 199-205
    • Brophy, V.A.1    Tavare, J.M.2    Rivett, A.J.3
  • 28
    • 0033963897 scopus 로고    scopus 로고
    • The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand
    • Rochel N, Wurtz JM, Mitschler A, Klaholz B, Moras D 2000 The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand. Mol Cell 5:173-179
    • (2000) Mol Cell , vol.5 , pp. 173-179
    • Rochel, N.1    Wurtz, J.M.2    Mitschler, A.3    Klaholz, B.4    Moras, D.5
  • 29
    • 0035064150 scopus 로고    scopus 로고
    • Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor
    • Rochel N, Tocchini-Valentini G, Egea PF, Juntunen K, Garnier JM, Vihko P, Moras D 2001 Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor. Eur JBiochem 268:971-979
    • (2001) Eur JBiochem , vol.268 , pp. 971-979
    • Rochel, N.1    Tocchini-Valentini, G.2    Egea, P.F.3    Juntunen, K.4    Garnier, J.M.5    Vihko, P.6    Moras, D.7
  • 30
    • 0642303090 scopus 로고    scopus 로고
    • Procaspase-3 and its active large subunit localized in both cytoplasm and nucleus are activated following application of apoptotic stimulus in Ramos-Burkitt lymphoma B cells
    • An S, Park MJ, Park IC, Hong SI, Knox K 2003 Procaspase-3 and its active large subunit localized in both cytoplasm and nucleus are activated following application of apoptotic stimulus in Ramos-Burkitt lymphoma B cells. Int J Mol Med 12:311-317
    • (2003) Int J Mol Med , vol.12 , pp. 311-317
    • An, S.1    Park, M.J.2    Park, I.C.3    Hong, S.I.4    Knox, K.5
  • 31
    • 0033214051 scopus 로고    scopus 로고
    • Apoptosis induced by vitamin D compounds in breast cancer cells is inhibited by Bcl-2 but does not involve known caspases or p53
    • Mathiasen IS, Lademann U, Jaattela M 1999 Apoptosis induced by vitamin D compounds in breast cancer cells is inhibited by Bcl-2 but does not involve known caspases or p53. Cancer Res 59:4848-4856
    • (1999) Cancer Res , vol.59 , pp. 4848-4856
    • Mathiasen, I.S.1    Lademann, U.2    Jaattela, M.3
  • 32
    • 0036634939 scopus 로고    scopus 로고
    • Apoptosis induction by 1α,25-dihydroxyvitamin D3 in prostate cancer
    • Guzey M, Kitada S, Reed JC 2002 Apoptosis induction by 1α,25-dihydroxyvitamin D3 in prostate cancer. Mol Cancer Ther 1:667-677
    • (2002) Mol Cancer Ther , vol.1 , pp. 667-677
    • Guzey, M.1    Kitada, S.2    Reed, J.C.3
  • 33
    • 0037225438 scopus 로고    scopus 로고
    • p53 is required for 1,25-dihydroxyvitamin D3-induced G0 arrest but is not required for G1 accumulation or apoptosis of LNCaP prostate cancer cells
    • Polek TC, Stewart LV, Ryu EJ, Cohen MB, Allegretto EA, Weigel NL 2003 p53 is required for 1,25-dihydroxyvitamin D3-induced G0 arrest but is not required for G1 accumulation or apoptosis of LNCaP prostate cancer cells. Endocrinology 144:50-60
    • (2003) Endocrinology , vol.144 , pp. 50-60
    • Polek, T.C.1    Stewart, L.V.2    Ryu, E.J.3    Cohen, M.B.4    Allegretto, E.A.5    Weigel, N.L.6
  • 35
    • 33847043095 scopus 로고    scopus 로고
    • 2D3-induced DNA methylation suppresses the human CYP27B1 gene. Mol Cell Endocrinol 265266:168-173
    • 2D3-induced DNA methylation suppresses the human CYP27B1 gene. Mol Cell Endocrinol 265266:168-173
  • 36
    • 0033324493 scopus 로고    scopus 로고
    • Ly LH, Zhao XY, Holloway L, Feldman D 1999 Liarozole acts synergistically with 1α,25-dihydroxyvitamin D3 to inhibit growth of DU 145 human prostate cancer cells by blocking 24-hydroxylase activity. Endocrinology 140:20712076
    • Ly LH, Zhao XY, Holloway L, Feldman D 1999 Liarozole acts synergistically with 1α,25-dihydroxyvitamin D3 to inhibit growth of DU 145 human prostate cancer cells by blocking 24-hydroxylase activity. Endocrinology 140:20712076
  • 37
    • 36049037977 scopus 로고    scopus 로고
    • Fibroblast growth factor 23 impairs phosphorus and vitamin D metabolism in vivo and suppresses 25-hydroxyvitamin D-1α-hydroxylase expression in vitro
    • Perwad F, Zhang MY, Tenenhouse HS, Portale AA 2007 Fibroblast growth factor 23 impairs phosphorus and vitamin D metabolism in vivo and suppresses 25-hydroxyvitamin D-1α-hydroxylase expression in vitro. Am J Physiol Renal Physiol 293:1577-1583
    • (2007) Am J Physiol Renal Physiol , vol.293 , pp. 1577-1583
    • Perwad, F.1    Zhang, M.Y.2    Tenenhouse, H.S.3    Portale, A.A.4
  • 38
    • 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
  • 39
    • 0033304612 scopus 로고    scopus 로고
    • 1,25-Dihydroxyvitamin D3 increases nuclear vitamin D3 receptors by blocking ubiquitin/proteasome-mediated degradation in human skin
    • LiXY,Boudjelal M, Xiao JH, Peng ZH, Asuru A, Kang S, Fisher GJ, Voorhees JJ 1999 1,25-Dihydroxyvitamin D3 increases nuclear vitamin D3 receptors by blocking ubiquitin/proteasome-mediated degradation in human skin. Mol Endocrinol 13:1686-1694
    • (1999) Mol Endocrinol , vol.13 , pp. 1686-1694
    • LiXY1    Boudjelal, M.2    Xiao, J.H.3    Peng, Z.H.4    Asuru, A.5    Kang, S.6    Fisher, G.J.7    Voorhees, J.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.