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Volumn 59, Issue 19, 1999, Pages 4848-4856

Apoptosis induced by vitamin D compounds in breast cancer cells is inhibited by Bcl-2 but does not involve known caspases or p53

Author keywords

[No Author keywords available]

Indexed keywords

20 EPI 22 ETHOXY 24A,26A,27A TRIHOMO 9,10 SECOCHOLESTA 5,7,10(19) TRIEN 23 YNE 1ALPHA,3BETA,25 TRIOL; CASPASE 3; COLECALCIFEROL DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BCL 2; PROTEIN P53; SEOCALCITOL; STAUROSPORINE; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

EID: 0033214051     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (201)

References (55)
  • 1
    • 0027050850 scopus 로고
    • Newly identified actions of the vitamin D endocrine system
    • Walters, M. R. Newly identified actions of the vitamin D endocrine system. Endocr. Rev., 13: 719-764, 1992.
    • (1992) Endocr. Rev. , vol.13 , pp. 719-764
    • Walters, M.R.1
  • 2
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • Bouillon, R., Okamura, W. H., and Norman, A. W. Structure-function relationships in the vitamin D endocrine system. Endocr. Rev., 16: 200-257, 1995.
    • (1995) Endocr. Rev. , vol.16 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 4
    • 0028543614 scopus 로고
    • Induction of apoptosis in breast cancer cells in response to vitamin D and antiestrogens
    • Welsh, J. E. Induction of apoptosis in breast cancer cells in response to vitamin D and antiestrogens. Biochem. Cell Biol., 72: 537-545, 1994.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 537-545
    • Welsh, J.E.1
  • 5
    • 0028970562 scopus 로고
    • Effects of vitamin D3 derivatives on growth, differentiation and apoptosis in tumoral colonic HT 29 cells: Possible implication of intracellular calcium
    • Vandewalle, B., Wattez, N., and Lefebvre, J. Effects of vitamin D3 derivatives on growth, differentiation and apoptosis in tumoral colonic HT 29 cells: possible implication of intracellular calcium. Cancer Lett., 97: 99-106, 1995.
    • (1995) Cancer Lett. , vol.97 , pp. 99-106
    • Vandewalle, B.1    Wattez, N.2    Lefebvre, J.3
  • 6
    • 0028979430 scopus 로고
    • Vitamin-D3 derivatives and breast-tumor cell growth: Effect on intracellular calcium and apoptosis
    • Vandewalle, B., Hornez, L., Wattez, N., Revillion, F., and Lefebvre, J. Vitamin-D3 derivatives and breast-tumor cell growth: effect on intracellular calcium and apoptosis. Int. J. Cancer, 9: 806-811, 1995.
    • (1995) Int. J. Cancer , vol.9 , pp. 806-811
    • Vandewalle, B.1    Hornez, L.2    Wattez, N.3    Revillion, F.4    Lefebvre, J.5
  • 10
    • 0025086226 scopus 로고
    • The mechanism of vitamin D toxicity
    • Vieth, R. The mechanism of vitamin D toxicity. Bone Miner., 11: 267-272, 1990.
    • (1990) Bone Miner. , vol.11 , pp. 267-272
    • Vieth, R.1
  • 11
    • 0027488715 scopus 로고
    • EB1089, a novel vitamin D analogue, has strong antiproliferative and differentiation inducing effects on cancer cells
    • Mathiasen, I. S., Colston, K. W., and Binderup, L. EB1089, a novel vitamin D analogue, has strong antiproliferative and differentiation inducing effects on cancer cells. J. Steroid Biochem. Mol. Biol., 46: 365-371, 1993.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 365-371
    • Mathiasen, I.S.1    Colston, K.W.2    Binderup, L.3
  • 13
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Washington DC
    • Ashkenazi, A., and Dixit, V. M. Death receptors: signaling and modulation. Science (Washington DC), 281: 1305-1308, 1998.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 14
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Washington DC
    • Green, D. R., and Reed, J. C. Mitochondria and apoptosis. Science (Washington DC), 281: 1309-1312, 1998.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 15
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Washington DC
    • Thornberry, N. A., and Lazebnik, Y. Caspases: enemies within. Science (Washington DC), 281: 1312-1316, 1998.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 16
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jäättelä, M. Escaping cell death: survival proteins in cancer. Exp. Cell Res., 248: 30-43, 1999.
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jäättelä, M.1
  • 17
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Washington DC
    • Adams, J. M., and Cory, S. The Bcl-2 protein family: arbiters of cell survival. Science (Washington DC), 281: 1322-1326, 1998.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 18
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1β-converting enzyme-like proteases
    • Xiang, J., Chao, D. T., and Korsmeyer, S. J. Bax-induced cell death may not require interleukin 1β-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA, 93: 14559-14563, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 19
    • 0029807603 scopus 로고    scopus 로고
    • Selective induction of apoptosis in Hep 3B cells by topisomerase I inhibitors: Evidence for a protease-dependent pathway that does not activate cystein protease P32
    • Adjei, P. N., Kaufmann, S. H., Leung, W-Y., Mao, F., and Gores, G. J. Selective induction of apoptosis in Hep 3B cells by topisomerase I inhibitors: evidence for a protease-dependent pathway that does not activate cystein protease P32. J. Clin. Invest., 98: 2588-2596, 1996.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2588-2596
    • Adjei, P.N.1    Kaufmann, S.H.2    Leung, W.-Y.3    Mao, F.4    Gores, G.J.5
  • 21
    • 0030777366 scopus 로고    scopus 로고
    • Activation of CPP32-like proteases is not sufficient to trigger apoptosis: Inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity
    • Wright, S. C., Schellenberger, U., Wang, H., Kinder, D. H., Talhouk, J. W., and Larrick, J. W. Activation of CPP32-like proteases is not sufficient to trigger apoptosis: inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity. J. Exp. Med., 186: 1107-1117, 1997.
    • (1997) J. Exp. Med. , vol.186 , pp. 1107-1117
    • Wright, S.C.1    Schellenberger, U.2    Wang, H.3    Kinder, D.H.4    Talhouk, J.W.5    Larrick, J.W.6
  • 22
    • 0029782494 scopus 로고    scopus 로고
    • Catepsin D protease mediates programmed cell death induced by interferon-γ, Fas/APO-1 and TNF-α
    • Deiss, L. P., Galinka, H., Berissi, H., Cohen, O., and Kimchi, A. Catepsin D protease mediates programmed cell death induced by Interferon-γ, Fas/APO-1 and TNF-α. EMBO J., 15: 3861-3870, 1996.
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 24
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • Patel, T., Gores, G. J., and Kaufmann, S. H. The role of proteases during apoptosis. FASEB J., 10: 587-597, 1996.
    • (1996) FASEB J. , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 25
    • 0028997181 scopus 로고
    • Vitamin D derivatives in combination with 9-cis retinoic acid promote active cell death in breast cancer cells
    • James, S. Y., Mackay, A. G., and Colston, K. W. Vitamin D derivatives in combination with 9-cis retinoic acid promote active cell death in breast cancer cells. J. Mol. Endocrinol., 14: 391-394, 1995.
    • (1995) J. Mol. Endocrinol. , vol.14 , pp. 391-394
    • James, S.Y.1    Mackay, A.G.2    Colston, K.W.3
  • 26
    • 0027946430 scopus 로고
    • Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands
    • Guenette, R. S., Mooibroek, M., Wong, K., Wong, P., and Tenniswood, M. Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands. Eur. J. Biochem., 226: 311-321, 1994.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 311-321
    • Guenette, R.S.1    Mooibroek, M.2    Wong, K.3    Wong, P.4    Tenniswood, M.5
  • 28
    • 0030699254 scopus 로고    scopus 로고
    • Modulation of cell cycle control by vitamin D3 and its analogue, EB1089, in human breast cancer cells
    • Wu, G., Fan, R. S., Li, W., Ko, T. C., and Brattain, M. G. Modulation of cell cycle control by vitamin D3 and its analogue, EB1089, in human breast cancer cells. Oncogene, 15: 1555-1563, 1997.
    • (1997) Oncogene , vol.15 , pp. 1555-1563
    • Wu, G.1    Fan, R.S.2    Li, W.3    Ko, T.C.4    Brattain, M.G.5
  • 32
    • 0030974122 scopus 로고    scopus 로고
    • Involvement of caspase-dependent activation of cytosolic phospholipase A2 in tumor necrosis factor-induced apoptosis
    • Wissing, D., Mouritzen, H., Egeblad, M., Poirier, G. G., and Jäättelä, M. Involvement of caspase-dependent activation of cytosolic phospholipase A2 in tumor necrosis factor-induced apoptosis. Proc. Natl. Acad. Sci. USA, 94: 5073-5077, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5073-5077
    • Wissing, D.1    Mouritzen, H.2    Egeblad, M.3    Poirier, G.G.4    Jäättelä, M.5
  • 34
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods, 65: 55-63, 1983.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 35
    • 0032124879 scopus 로고    scopus 로고
    • TNF-induced mitochondrial changes and activation of apoptotic proteases are inhibited by A20
    • Wissing, D., Mouritzen, H., and Jäättelä, M. TNF-induced mitochondrial changes and activation of apoptotic proteases are inhibited by A20. Free Radical Biol. Med., 25: 57-65, 1999.
    • (1999) Free Radical Biol. Med. , vol.25 , pp. 57-65
    • Wissing, D.1    Mouritzen, H.2    Jäättelä, M.3
  • 36
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lond.
    • Lazebnik, Y. A., Kaufmann, S. H., Desnoyers, S., Poirier, G. G., and Earnshaw, W. C. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature (Lond.), 371: 346-347, 1994.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 37
    • 0028990125 scopus 로고
    • Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari, M., Quan, L. T., O'Rourke, K., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S., and Dixit, V. M. Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell, 81: 801-809, 1995.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 38
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fasmediated apoptosis
    • Lond.
    • Enari, M., Hug, H., and Nagata, S. Involvement of an ICE-like protease in Fasmediated apoptosis. Nature (Lond.), 375: 78-81, 1995.
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 39
    • 0029884711 scopus 로고    scopus 로고
    • Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors
    • Shimizu, S., Eguchi, Y., Kamiike, W., Waguri, S., Uchiyama, Y., Matsuda, H., and Tsujimoto, Y. Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors. Oncogene, 13: 21-29, 1996.
    • (1996) Oncogene , vol.13 , pp. 21-29
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3    Waguri, S.4    Uchiyama, Y.5    Matsuda, H.6    Tsujimoto, Y.7
  • 40
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin crma: Analysis of five caspases
    • Zhou, Q., Snipas, S., Orth, K., Muzio, M., Dixit, V. M., and Salvesen, G. S. Target protease specificity of the viral serpin CrmA: analysis of five caspases. J. Biol. Chem., 272: 7797-7800, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6
  • 41
    • 0029670265 scopus 로고    scopus 로고
    • ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis
    • Nicholson, D. W. ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis. Nat. Biotechnol., 14: 297-301, 1996.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 297-301
    • Nicholson, D.W.1
  • 42
    • 0030134624 scopus 로고    scopus 로고
    • The cell-death machine
    • Chinnaiyan, A., and Dixit, V. The cell-death machine. Curr. Biol., 6: 555-562, 1996.
    • (1996) Curr. Biol. , vol.6 , pp. 555-562
    • Chinnaiyan, A.1    Dixit, V.2
  • 43
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Jänicke, R. U., Sprengart, M. L., Wati, M. R., and Porter, A. G. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem., 273: 9357-9360, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 44
    • 0028981091 scopus 로고
    • 20-epi-vitamin D3 analogues: A novel class of potent inhibitors of proliferation and inducers of differentiation of human breast cancer cell lines
    • Elstner, E., Linker-Israeli, M., Said, J., Umiel, T., de Vos, S., Shintaku, I. P., Heber, D., Binderup, L., Uskovic, M., and Koeffler, H. P. 20-epi-vitamin D3 analogues: a novel class of potent inhibitors of proliferation and inducers of differentiation of human breast cancer cell lines. Cancer Res., 55: 2822-2830, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 2822-2830
    • Elstner, E.1    Linker-Israeli, M.2    Said, J.3    Umiel, T.4    De Vos, S.5    Shintaku, I.P.6    Heber, D.7    Binderup, L.8    Uskovic, M.9    Koeffler, H.P.10
  • 45
    • 0025367297 scopus 로고
    • Genetic and immunochemical analysis of mutant p53 in human breast cancer cell lines
    • Bartek, J., Iggo, R., Gannon, J., and Lane, D. P. Genetic and immunochemical analysis of mutant p53 in human breast cancer cell lines. Oncogene, 5: 893-899, 1990.
    • (1990) Oncogene , vol.5 , pp. 893-899
    • Bartek, J.1    Iggo, R.2    Gannon, J.3    Lane, D.P.4
  • 46
    • 0030731407 scopus 로고    scopus 로고
    • Differential effects of 1,25-dihydroxyvitamin D3 and tetradecanoylphorbol acetate on cell cycle and apoptosis of MCF-7 cells and a vitamin D3-resistant variant
    • Narvez, C. J., and Welsh, J. Differential effects of 1,25-dihydroxyvitamin D3 and tetradecanoylphorbol acetate on cell cycle and apoptosis of MCF-7 cells and a vitamin D3-resistant variant. Endocrinology, 138: 4690-4698, 1997.
    • (1997) Endocrinology , vol.138 , pp. 4690-4698
    • Narvez, C.J.1    Welsh, J.2
  • 47
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Henzel, W. J., Liu, X., Lutschg, A., and Wang, X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell, 90: 405-413, 1997.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 48
    • 0027451668 scopus 로고
    • p53-dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe, S. W., Ruley, H. E., Jacks, T., and Housman, D. E. p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell, 74: 957-967, 1993.
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3    Housman, D.E.4
  • 49
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis in leukemia cells
    • Friesen, C., Krammer, P. H., and Debatin, K. M. Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis in leukemia cells. Nat. Med., 2: 574-577, 1996.
    • (1996) Nat. Med. , vol.2 , pp. 574-577
    • Friesen, C.1    Krammer, P.H.2    Debatin, K.M.3
  • 51
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Washington DC
    • Sherr, C. J. Cancer cell cycles. Science (Washington DC), 274: 1672-1677, 1996.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 52
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • Washington DC
    • Evan, G., and Littlewood, T. A matter of life and cell death. Science (Washington DC), 281: 1317-1322, 1998.
    • (1998) Science , vol.281 , pp. 1317-1322
    • Evan, G.1    Littlewood, T.2
  • 53
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Lond.
    • Deveraux, Q. L., Takahashi, R., Salvesen, G. S., and Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature (Lond.), 388: 300-304, 1997.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 54
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy, N., Deveraux, Q. L., Takahashi, R., Salvesen, G. S., and Reed, J. C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J., 16: 6914-6925, 1997.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 55
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä, M., Wissing, D., Kokholm, K., Kallunki, T., and Egeblad, M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J., 17: 6124-6134, 1998.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5


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