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Volumn 1, Issue 2, 2003, Pages 13-18

Retinoids and retinoic acid receptor in cancer

Author keywords

Arsenic; Leukemia; Receptors; Transformation; Vitamin A

Indexed keywords

ANTINEOPLASTIC AGENT; ARSENIC TRIOXIDE; HYBRID PROTEIN; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR ALPHA; RETINOIC ACID RECEPTOR BETA; RETINOIC ACID RECEPTOR GAMMA; RETINOID; RETINOID X RECEPTOR; RETINOL DERIVATIVE;

EID: 2442495132     PISSN: 13596349     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6349(03)00010-7     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 0035749803 scopus 로고    scopus 로고
    • The promise of retinoids to fight against cancer
    • Altucci L., Gronemeyer H. The promise of retinoids to fight against cancer. Nature Rev Cancer. 1:2001;181-193
    • (2001) Nature Rev Cancer , vol.1 , pp. 181-193
    • Altucci, L.1    Gronemeyer, H.2
  • 2
    • 0022547592 scopus 로고
    • Hepatitis virus DNA integration in a sequence homologous to v-erbA and steroid receptors genes in a hepatocellular carcinoma
    • Dejean A., Bougueleret L., Grzeschick K., Tiollais P. Hepatitis virus DNA integration in a sequence homologous to v-erbA and steroid receptors genes in a hepatocellular carcinoma. Nature. 322:1986;70-72
    • (1986) Nature , vol.322 , pp. 70-72
    • Dejean, A.1    Bougueleret, L.2    Grzeschick, K.3    Tiollais, P.4
  • 3
    • 0025098239 scopus 로고
    • Identification of a retinoic acid responsive element in the retinoic acid receptor beta gene
    • de Thé H., Vivanco-Ruiz MdM., Tiollais P., Stunnenberg H., Dejean A. Identification of a retinoic acid responsive element in the retinoic acid receptor beta gene. Nature. 343:1990;177-180
    • (1990) Nature , vol.343 , pp. 177-180
    • De Thé, H.1    Vivanco-Ruiz, MdM.2    Tiollais, P.3    Stunnenberg, H.4    Dejean, A.5
  • 4
    • 0028967616 scopus 로고
    • R.A.R. specific agonist/antagonists which dissociate transactivation and AP1 transrepression inhibit anchorage-independent cell proliferation
    • Chen J.-Y., Penco S., Ostrowski J., et al. R.A.R. specific agonist/antagonists which dissociate transactivation and AP1 transrepression inhibit anchorage-independent cell proliferation. EMBO J. 14:1995;1187-1197
    • (1995) EMBO J. , vol.14 , pp. 1187-1197
    • Chen, J.-Y.1    Penco, S.2    Ostrowski, J.3
  • 5
    • 0028999532 scopus 로고
    • All-trans retinoic acid as a differentiating agent in the treatment of acute promyelocytic leukemia
    • Degos L., Dombret H., Chomienne C., et al. All-trans retinoic acid as a differentiating agent in the treatment of acute promyelocytic leukemia. Blood. 85:1995;2643-2653
    • (1995) Blood , vol.85 , pp. 2643-2653
    • Degos, L.1    Dombret, H.2    Chomienne, C.3
  • 6
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • Melnick A., Licht J.D. Deconstructing a disease. RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia Blood. 93:1999;3167-3215
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 7
    • 0030615230 scopus 로고    scopus 로고
    • A PML RAR alpha transgene initiates murine acute promyelocytic leukemia
    • Brown D., Kogan S., Lagasse E., et al. A PML RAR alpha transgene initiates murine acute promyelocytic leukemia. Proc. Natl. Acad. Sci. USA. 94:1997;2551-2556
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2551-2556
    • Brown, D.1    Kogan, S.2    Lagasse, E.3
  • 8
    • 0023752982 scopus 로고
    • Use of all trans retinoic acid in the treatment of acute promyelocytic leukaemia
    • Huang M., Ye Y., Chen R., et al. Use of all trans retinoic acid in the treatment of acute promyelocytic leukaemia. Blood. 72:1988;567-572
    • (1988) Blood , vol.72 , pp. 567-572
    • Huang, M.1    Ye, Y.2    Chen, R.3
  • 10
    • 0031561478 scopus 로고    scopus 로고
    • Retinoic acid and arsenic: Towards oncogene targeted treatments of acute promyelocytic leukaemia
    • Quignon F., Chen Z., de Thé H. Retinoic acid and arsenic. towards oncogene targeted treatments of acute promyelocytic leukaemia Biochim. Biophys. Acta. 1333:1997;M53-M61
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Quignon, F.1    Chen, Z.2    De Thé, H.3
  • 11
    • 0035969111 scopus 로고    scopus 로고
    • Pathways of retinoic acid- or arsenic trioxide-induced PML/RARalpha catabolism, role of oncogene degradation in disease remission
    • Zhu J., Lallemand-Breitenbach V., de The H. Pathways of retinoic acid- or arsenic trioxide-induced PML/RARalpha catabolism, role of oncogene degradation in disease remission. Oncogene. 20:2001;7257-7265
    • (2001) Oncogene , vol.20 , pp. 7257-7265
    • Zhu, J.1    Lallemand-Breitenbach, V.2    De The, H.3
  • 12
    • 0033638969 scopus 로고    scopus 로고
    • Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation
    • Minucci S., Maccarana M., Cioce M., et al. Oligomerization of RAR and AML1 transcription factors as a novel mechanism of oncogenic activation. Mol. Cell. 5:2000;811-820
    • (2000) Mol. Cell , vol.5 , pp. 811-820
    • Minucci, S.1    MacCarana, M.2    Cioce, M.3
  • 13
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin R.J., Nagy L., Inoue S., Shao W.L., Miller W.H., Evans R.M. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature. 391:1998;811-814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.L.4    Miller, W.H.5    Evans, R.M.6
  • 14
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia
    • Grignani F., de Matteis S., Nervi C., et al. Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature. 391:1998;815-818
    • (1998) Nature , vol.391 , pp. 815-818
    • Grignani, F.1    De Matteis, S.2    Nervi, C.3
  • 15
    • 0029942879 scopus 로고    scopus 로고
    • Accelerated degradation of PML-retinoic acid receptor alpha (PML-RARA) oncoprotein by all-trans-retinoic acid in acute promyelocytic leukemia. Possible role of the proteasome pathway
    • Yoshida H., Kitamura K., Tanaka K., et al. Accelerated degradation of PML-retinoic acid receptor alpha (PML-RARA) oncoprotein by all-trans-retinoic acid in acute promyelocytic leukemia. Possible role of the proteasome pathway. Cancer Res. 56:1996;2945-2948
    • (1996) Cancer Res. , vol.56 , pp. 2945-2948
    • Yoshida, H.1    Kitamura, K.2    Tanaka, K.3
  • 16
    • 0029919406 scopus 로고    scopus 로고
    • The PML/RAR alpha oncoprotein is a direct molecular target of retinoic acid in acute promyelocytic leukemia cells
    • Raelson J.V., Nervi C., Rosenauer A., et al. The PML/RAR alpha oncoprotein is a direct molecular target of retinoic acid in acute promyelocytic leukemia cells. Blood. 88:1996;2826-2832
    • (1996) Blood , vol.88 , pp. 2826-2832
    • Raelson, J.V.1    Nervi, C.2    Rosenauer, A.3
  • 17
    • 0033592948 scopus 로고    scopus 로고
    • Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RAR alpha) and oncogenic RAR alpha fusion proteins
    • Zhu J., Gianni M., Kopf E., et al. Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RAR alpha) and oncogenic RAR alpha fusion proteins. Proc. Natl. Acad. Sci. USA. 96:1999;14807-14812
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14807-14812
    • Zhu, J.1    Gianni, M.2    Kopf, E.3
  • 18
    • 0028095410 scopus 로고
    • PML, a growth suppressor disrupted in acute promyelocytic leukemia
    • Mu Z.M., Chin K.V., Liu J.H., Lozano G., Chang K.S. PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14:1994;6858-6867
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6858-6867
    • Mu, Z.M.1    Chin, K.V.2    Liu, J.H.3    Lozano, G.4    Chang, K.S.5
  • 20
    • 0028916423 scopus 로고
    • The PML growth-suppressor has an altered expression in human oncogenesis
    • Koken M.H.M., Linares-Cruz G., Quignon F., et al. The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene. 10:1995;1315-1324
    • (1995) Oncogene , vol.10 , pp. 1315-1324
    • Koken, M.H.M.1    Linares-Cruz, G.2    Quignon, F.3
  • 21
    • 0028951531 scopus 로고
    • PML nuclear bodies are general targets for inflammation and cell proliferation
    • Terris B., Baldin V., Dubois S., et al. PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res. 55:1995;1590-1597
    • (1995) Cancer Res. , vol.55 , pp. 1590-1597
    • Terris, B.1    Baldin, V.2    Dubois, S.3
  • 22
    • 0031791875 scopus 로고    scopus 로고
    • PML is essential for multiple apoptotic pathways
    • Wang Z.-G., Ruggero D., Ronchetti S., et al. PML is essential for multiple apoptotic pathways. Nat Genet. 20:1998;266-272
    • (1998) Nat Genet , vol.20 , pp. 266-272
    • Wang, Z.-G.1    Ruggero, D.2    Ronchetti, S.3
  • 23
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and the retinoic acid pathway
    • Wang Z.G., Delva L., Gaboli M., et al. Role of PML in cell growth and the retinoic acid pathway. Science. 279:1998;1547-1551
    • (1998) Science , vol.279 , pp. 1547-1551
    • Wang, Z.G.1    Delva, L.2    Gaboli, M.3
  • 24
    • 0028293945 scopus 로고
    • The t(15;17) translocation alters a nuclear body in a RA-reversible fashion
    • Koken M.H.M., Puvion-Dutilleul F., Guillemin M.C., et al. The t(15;17) translocation alters a nuclear body in a RA-reversible fashion. EMBO J. 13:1994;1073-1083
    • (1994) EMBO J. , vol.13 , pp. 1073-1083
    • Koken, M.H.M.1    Puvion-Dutilleul, F.2    Guillemin, M.C.3
  • 25
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML/RARα in acute promyelocytic leukemia cells
    • Weis K., Rambaud S., Lavau C., et al. Retinoic acid regulates aberrant nuclear localization of PML/RARα in acute promyelocytic leukemia cells. Cell. 76:1994;345-356
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3
  • 26
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte- retinoic acid receptor oncoprotein
    • Dyck J.A., Maul G.G., Miller W.H., Chen J.D., Kakizuka A., Evans R.M. A novel macromolecular structure is a target of the promyelocyte- retinoic acid receptor oncoprotein. Cell. 76:1994;333-343
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 27
    • 0026532516 scopus 로고
    • A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies
    • Stuurman N., de Graaf A., Floore A., et al. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J. Cell Sci. 101:1992;773-784
    • (1992) J. Cell Sci. , vol.101 , pp. 773-784
    • Stuurman, N.1    De Graaf, A.2    Floore, A.3
  • 28
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for N.D.10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1
    • Ishov A.M., Sotnikov A.G., Negorev D., et al. PML is critical for N.D.10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147:1999;221-234
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 29
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As(2)O(3)-induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach V., Zhu J., Puvion F., et al. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As(2)O(3)-induced PML or PML/retinoic acid receptor alpha degradation. J Exp Med. 193:2001;1361-1372
    • (2001) J Exp Med. , vol.193 , pp. 1361-1372
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3
  • 31
    • 0010740572 scopus 로고    scopus 로고
    • 4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR alpha/PML proteins
    • 4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR alpha/PML proteins. Blood. 88:1996;1052-1061
    • (1996) Blood , vol.88 , pp. 1052-1061
    • Chen, G.-Q.1    Zhu, J.2    Shi, X.-G.3
  • 32
    • 0030610686 scopus 로고    scopus 로고
    • 3 exerts dose- dependent dual effects on APL cells
    • 3 exerts dose- dependent dual effects on APL cells Blood. 89:1997;3345-3353
    • (1997) Blood , vol.89 , pp. 3345-3353
    • Chen, G.-Q.1    Shi, X.-G.2    Tang, W.3
  • 33
    • 9344234374 scopus 로고    scopus 로고
    • Pharmacokinetics and efficacy of low-dose all-trans retinoic acid in the treatment of acute promyelocytic leukemia
    • Chen G.Q., Shen Z.X., Wu F., et al. Pharmacokinetics and efficacy of low-dose all-trans retinoic acid in the treatment of acute promyelocytic leukemia. Leukemia. 10:1996;825-828
    • (1996) Leukemia , vol.10 , pp. 825-828
    • Chen, G.Q.1    Shen, Z.X.2    Wu, F.3
  • 34
    • 0033526012 scopus 로고    scopus 로고
    • Retinoic acid and arsenic synergize to eradicate leukemic cells in a mouse model of acute promyelocytic leukemia
    • Lallemand-Breitenbach V., Guillemin M.-C., Janin A., et al. Retinoic acid and arsenic synergize to eradicate leukemic cells in a mouse model of acute promyelocytic leukemia. J. Exp. Med. 189:1999;1043-1052
    • (1999) J. Exp. Med. , vol.189 , pp. 1043-1052
    • Lallemand-Breitenbach, V.1    Guillemin, M.-C.2    Janin, A.3
  • 35
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia
    • Zhu J., Koken M.H.M., Quignon F., et al. Arsenic-induced PML targeting onto nuclear bodies. implications for the treatment of acute promyelocytic leukemia Proc. Natl. Acad. Sci. USA. 94:1997;3978-3983
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3978-3983
    • Zhu, J.1    Koken, M.H.M.2    Quignon, F.3
  • 36
    • 0012316186 scopus 로고    scopus 로고
    • Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1
    • vom Baur E., Zechel C., Heery D., et al. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. 15:1996;110-124
    • (1996) EMBO J. , vol.15 , pp. 110-124
    • Vom Baur, E.1    Zechel, C.2    Heery, D.3
  • 37
    • 17944372810 scopus 로고    scopus 로고
    • Novel differentiation-inducing therapy for acute promyelocytic leukemia with a combination of arsenic trioxide and GM-CSF
    • Muto A., Kizaki M., Kawamura C., et al A. novel differentiation-inducing therapy for acute promyelocytic leukemia with a combination of arsenic trioxide and GM-CSF. Leukemia. 15:2001;1176-1184
    • (2001) Leukemia , vol.15 , pp. 1176-1184
    • Muto, A.1    Kizaki, M.2    Kawamura, C.3    Et Al, A.4
  • 38
    • 0036464602 scopus 로고    scopus 로고
    • Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk
    • Zhu Q., Zhang J.W., Zhu H.Q., et al. Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk. Blood. 99:2002;1014-1022
    • (2002) Blood , vol.99 , pp. 1014-1022
    • Zhu, Q.1    Zhang, J.W.2    Zhu, H.Q.3
  • 39
    • 0034961181 scopus 로고    scopus 로고
    • Retinoic acid-induced apoptosis in leukemia cells is mediated by paracrine action of tumor-selective death ligand TRAIL
    • Altucci L., Rossin A., Raffelsberger W., Reitmair A., Chomienne C., Gronemeyer H. Retinoic acid-induced apoptosis in leukemia cells is mediated by paracrine action of tumor-selective death ligand TRAIL. Nat Med. 7:2001;680-686
    • (2001) Nat Med. , vol.7 , pp. 680-686
    • Altucci, L.1    Rossin, A.2    Raffelsberger, W.3    Reitmair, A.4    Chomienne, C.5    Gronemeyer, H.6
  • 40
    • 0034730198 scopus 로고    scopus 로고
    • Retinoic acid (RA) and As2O3 treatment in transgenic models of acute promyelocytic leukemia (APL) unravel the distinct nature of the leukemogenic process induced by the PML-RARalpha and PLZF-RARalpha oncoproteins
    • Rego E.M., He L.Z., Warrell R.P. Jr., Wang Z.G., Pandolfi P.P. Retinoic acid (RA) and As2O3 treatment in transgenic models of acute promyelocytic leukemia (APL) unravel the distinct nature of the leukemogenic process induced by the PML-RARalpha and PLZF-RARalpha oncoproteins. Proc Natl Acad Sci USA. 97:2000;10173-10178
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10173-10178
    • Rego, E.M.1    He, L.Z.2    Warrell Jr., R.P.3    Wang, Z.G.4    Pandolfi, P.P.5
  • 41
    • 0035161286 scopus 로고    scopus 로고
    • Combined effect of all-trans retinoic acid and arsenic trioxide in acute promyelocytic leukemia cells in vitro and in vivo
    • Jing Y., Wang L., Xia L., et al. Combined effect of all-trans retinoic acid and arsenic trioxide in acute promyelocytic leukemia cells in vitro and in vivo. Blood. 97:2001;264-269
    • (2001) Blood , vol.97 , pp. 264-269
    • Jing, Y.1    Wang, L.2    Xia, L.3
  • 42
    • 0034786069 scopus 로고    scopus 로고
    • Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia
    • Hong S.H., Yang Z., Privalsky M.L. Arsenic trioxide is a potent inhibitor of the interaction of SMRT corepressor with Its transcription factor partners, including the PML-retinoic acid receptor alpha oncoprotein found in human acute promyelocytic leukemia. Mol Cell Biol. 21:2001;7172-7182
    • (2001) Mol Cell Biol. , vol.21 , pp. 7172-7182
    • Hong, S.H.1    Yang, Z.2    Privalsky, M.L.3
  • 43
    • 0035045676 scopus 로고    scopus 로고
    • Modeling acute promyelocytic leukemia in the mouse: New insights in the pathogenesis of human leukemias
    • Merghoub T., Gurrieri C., Piazza F., Pandolfi P.P. Modeling acute promyelocytic leukemia in the mouse. new insights in the pathogenesis of human leukemias Blood Cells Mol Dis. 27:2001;231-248
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 231-248
    • Merghoub, T.1    Gurrieri, C.2    Piazza, F.3    Pandolfi, P.P.4
  • 44
    • 0034144710 scopus 로고    scopus 로고
    • Leukemia initiated by PMLRARalpha: The PML domain plays a critical role while retinoic acid-mediated transactivation is dispensable
    • Kogan S.C., Hong S.H., Shultz D.B., Privalsky M.L., Bishop J.M. Leukemia initiated by PMLRARalpha. the PML domain plays a critical role while retinoic acid-mediated transactivation is dispensable Blood. 95:2000;1541-1550
    • (2000) Blood , vol.95 , pp. 1541-1550
    • Kogan, S.C.1    Hong, S.H.2    Shultz, D.B.3    Privalsky, M.L.4    Bishop, J.M.5
  • 45
    • 0035189761 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia
    • He L.Z., Tolentino T., Grayson P., et al. Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia. J Clin Invest. 108:2001;1321-1330
    • (2001) J Clin Invest. , vol.108 , pp. 1321-1330
    • He, L.Z.1    Tolentino, T.2    Grayson, P.3


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