메뉴 건너뛰기




Volumn 36, Issue SUPPL. 1, 2009, Pages

Anaplastic Lymphoma Kinase (ALK)-Induced Malignancies: Novel Mechanisms of Cell Transformation and Potential Therapeutic Approaches

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 5 AZA 2' DEOXYCYTIDINE; ANAPLASTIC LYMPHOMA KINASE; AZACITIDINE; DNA METHYLTRANSFERASE 1; HERBIMYCIN A; HYBRID PROTEIN; IMATINIB; INTERLEUKIN 10; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE KINASE; NUCLEOPHOSMIN; NUCLEOPHOSMIN ANAPLASTIC LYMPHOMA KINASE FUSION PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN TYROSINE PHOSPHATASE SHP 1; RAPAMYCIN; STAT3 PROTEIN; STAT5 PROTEIN; STAT5A PROTEIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; UO 126; WORTMANNIN;

EID: 64849103123     PISSN: 00937754     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.seminoncol.2009.02.007     Document Type: Article
Times cited : (38)

References (78)
  • 1
    • 0031008896 scopus 로고    scopus 로고
    • ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK)
    • Morris S.W., Naeve C., Mathew P., James P.L., Kirstein M.N., Cui X., et al. ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK). Oncogene 14 (1997) 2175-2188
    • (1997) Oncogene , vol.14 , pp. 2175-2188
    • Morris, S.W.1    Naeve, C.2    Mathew, P.3    James, P.L.4    Kirstein, M.N.5    Cui, X.6
  • 2
    • 0031689795 scopus 로고    scopus 로고
    • ALK expression defines a distinct group of T/null lymphomas ("ALK lymphomas") with a wide morphological spectrum
    • Falini B., Bigerna B., Fizzotti M., Pulford K., Pileri S.A., Delsol G., et al. ALK expression defines a distinct group of T/null lymphomas ("ALK lymphomas") with a wide morphological spectrum. Am J Pathol 153 (1998) 875-886
    • (1998) Am J Pathol , vol.153 , pp. 875-886
    • Falini, B.1    Bigerna, B.2    Fizzotti, M.3    Pulford, K.4    Pileri, S.A.5    Delsol, G.6
  • 3
    • 0031055562 scopus 로고    scopus 로고
    • Detection of anaplastic lymphoma kinase (ALK) and nucleolar protein nucleophosmin (NPM)-ALK protein in normal and neoplastic cells with the monoclonal antibody ALK1
    • Pulford K., Lamant L., Morris S.W., Butler L.H., Wood K.M., Stroud D., et al. Detection of anaplastic lymphoma kinase (ALK) and nucleolar protein nucleophosmin (NPM)-ALK protein in normal and neoplastic cells with the monoclonal antibody ALK1. Blood 89 (1997) 1394-1404
    • (1997) Blood , vol.89 , pp. 1394-1404
    • Pulford, K.1    Lamant, L.2    Morris, S.W.3    Butler, L.H.4    Wood, K.M.5    Stroud, D.6
  • 4
    • 34547638047 scopus 로고    scopus 로고
    • Identification of the transforming EML4-ALK fusion gene in non-small-cell lung cancer
    • Soda M., Choi Y.L., Enomoto M., Takada S., Yamashita Y., Ishikawa S., et al. Identification of the transforming EML4-ALK fusion gene in non-small-cell lung cancer. Nature 448 (2007) 561-566
    • (2007) Nature , vol.448 , pp. 561-566
    • Soda, M.1    Choi, Y.L.2    Enomoto, M.3    Takada, S.4    Yamashita, Y.5    Ishikawa, S.6
  • 5
    • 54049094708 scopus 로고    scopus 로고
    • Identification of ALK as a major familial neuroblastoma predisposition gene
    • 930-5
    • Mossé Y.P., Laudenslager M., Longo L., Cole K.A., Wood A., Attiyeh E.F., et al. Identification of ALK as a major familial neuroblastoma predisposition gene. Nature 16 (2008) 455 930-5
    • (2008) Nature , vol.16 , pp. 455
    • Mossé, Y.P.1    Laudenslager, M.2    Longo, L.3    Cole, K.A.4    Wood, A.5    Attiyeh, E.F.6
  • 6
    • 54049120220 scopus 로고    scopus 로고
    • Activating mutations in ALK provide a therapeutic target in neuroblastoma
    • George R.E., Sanda T., Hanna M., Fröhling S., Luther II W., Zhang J., et al. Activating mutations in ALK provide a therapeutic target in neuroblastoma. Nature 455 (2008) 975-978
    • (2008) Nature , vol.455 , pp. 975-978
    • George, R.E.1    Sanda, T.2    Hanna, M.3    Fröhling, S.4    Luther II, W.5    Zhang, J.6
  • 8
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer R.A., Lehner C.F., Eppenberger H.M., and Nigg E.A. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56 (1989) 379-390
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.F.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 9
    • 0024595908 scopus 로고
    • Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth
    • Chan W.Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A., et al. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth. Biochemistry 28 (1989) 1033-1039
    • (1989) Biochemistry , vol.28 , pp. 1033-1039
    • Chan, W.Y.1    Liu, Q.R.2    Borjigin, J.3    Busch, H.4    Rennert, O.M.5    Tease, L.A.6
  • 10
  • 11
    • 0028275645 scopus 로고
    • Hyperphosphorylation of a novel 80 kDa protein-tyrosine kinase similar to Ltk in a human Ki-1 lymphoma cell line, AMS3
    • Shiota M., Fujimoto J., Semba T., Satoh H., Yamamoto T., and Mori S. Hyperphosphorylation of a novel 80 kDa protein-tyrosine kinase similar to Ltk in a human Ki-1 lymphoma cell line, AMS3. Oncogene 9 (1994) 1567-1574
    • (1994) Oncogene , vol.9 , pp. 1567-1574
    • Shiota, M.1    Fujimoto, J.2    Semba, T.3    Satoh, H.4    Yamamoto, T.5    Mori, S.6
  • 12
    • 0030003813 scopus 로고    scopus 로고
    • Characterization of the transforming activity of p80, a hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5)
    • Fujimoto J., Shiota M., Iwahara T., Seki N., Satoh H., Mori S., et al. Characterization of the transforming activity of p80, a hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5). Proc Natl Acad Sci U S A 93 (1996) 4181-4186
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4181-4186
    • Fujimoto, J.1    Shiota, M.2    Iwahara, T.3    Seki, N.4    Satoh, H.5    Mori, S.6
  • 13
    • 0030934862 scopus 로고    scopus 로고
    • Role of the nucleophosmin (NPM) portion of the non Hodgkin's lymphoma-associated NPM-anaplastic lymphoma kinase fusion protein in oncogenesis
    • Bischof D., Pulford K., Mason D.Y., and Morris S.W. Role of the nucleophosmin (NPM) portion of the non Hodgkin's lymphoma-associated NPM-anaplastic lymphoma kinase fusion protein in oncogenesis. Mol Cell Biol 17 (1997) 2312-2325
    • (1997) Mol Cell Biol , vol.17 , pp. 2312-2325
    • Bischof, D.1    Pulford, K.2    Mason, D.Y.3    Morris, S.W.4
  • 14
    • 0030809095 scopus 로고    scopus 로고
    • Retrovirus-mediated gene transfer of NPM-ALK causes lymphoid malignancy in mice
    • Kuefer M.U., Look A.T., Pulford K., Behm F.G., Pattengale P.K., Mason D.Y., et al. Retrovirus-mediated gene transfer of NPM-ALK causes lymphoid malignancy in mice. Blood 90 (1997) 2901-2910
    • (1997) Blood , vol.90 , pp. 2901-2910
    • Kuefer, M.U.1    Look, A.T.2    Pulford, K.3    Behm, F.G.4    Pattengale, P.K.5    Mason, D.Y.6
  • 15
    • 0037372285 scopus 로고    scopus 로고
    • NPM-ALK transgenic mice spontaneously develop T-cell lymphomas and plasma cell tumors
    • Chiarle R., Gong J.Z., Guasparri I., Pesci A., Cai J., Liu J., et al. NPM-ALK transgenic mice spontaneously develop T-cell lymphomas and plasma cell tumors. Blood 101 (2003) 1919-1927
    • (2003) Blood , vol.101 , pp. 1919-1927
    • Chiarle, R.1    Gong, J.Z.2    Guasparri, I.3    Pesci, A.4    Cai, J.5    Liu, J.6
  • 16
    • 0031755958 scopus 로고    scopus 로고
    • Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity
    • Bai R.Y., Dieter P., Peschel C., Morris S.W., and Duyster J. Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity. Mol Cell Biol 18 (1998) 6951-6961
    • (1998) Mol Cell Biol , vol.18 , pp. 6951-6961
    • Bai, R.Y.1    Dieter, P.2    Peschel, C.3    Morris, S.W.4    Duyster, J.5
  • 17
    • 0034672140 scopus 로고    scopus 로고
    • Nucleophosminanaplastic lymphoma kinase associated with anaplastic large cell lymphoma activates the phosphatidylinositol 3-kinase/Akt antiapoptotic signaling pathway
    • Bai R.Y., Ouyang T., Miething C., Morris S.W., Peschel C., and Duyster J. Nucleophosminanaplastic lymphoma kinase associated with anaplastic large cell lymphoma activates the phosphatidylinositol 3-kinase/Akt antiapoptotic signaling pathway. Blood 96 (2000) 4319-4327
    • (2000) Blood , vol.96 , pp. 4319-4327
    • Bai, R.Y.1    Ouyang, T.2    Miething, C.3    Morris, S.W.4    Peschel, C.5    Duyster, J.6
  • 18
    • 0035266314 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase-Akt pathway in nucleophosmin/anaplastic lymphoma kinase-mediated lymphomagenesis
    • Slupianek A., Nieborowska-Skorska M., Hoser G., Morrione A., Majewski M., Xue L., et al. Role of phosphatidylinositol 3-kinase-Akt pathway in nucleophosmin/anaplastic lymphoma kinase-mediated lymphomagenesis. Cancer Res 61 (2001) 2194-2199
    • (2001) Cancer Res , vol.61 , pp. 2194-2199
    • Slupianek, A.1    Nieborowska-Skorska, M.2    Hoser, G.3    Morrione, A.4    Majewski, M.5    Xue, L.6
  • 19
    • 10044252102 scopus 로고    scopus 로고
    • NPM/ALK down regulates p27Kip1 in a PI-3K-dependent manner
    • Slupianek A., and Skorski T. NPM/ALK down regulates p27Kip1 in a PI-3K-dependent manner. Exp Hematol 32 (2004) 1265-1271
    • (2004) Exp Hematol , vol.32 , pp. 1265-1271
    • Slupianek, A.1    Skorski, T.2
  • 20
    • 2942618200 scopus 로고    scopus 로고
    • NPM-ALK fusion kinase of anaplastic large-cell lymphoma regulates survival and proliferative signaling through modulation of FOXO3a
    • Gu T.L., Tothova Z., Scheijen B., Griffin J.D., Gilliland D.G., and Sternberg D.W. NPM-ALK fusion kinase of anaplastic large-cell lymphoma regulates survival and proliferative signaling through modulation of FOXO3a. Blood 103 (2004) 4622-4629
    • (2004) Blood , vol.103 , pp. 4622-4629
    • Gu, T.L.1    Tothova, Z.2    Scheijen, B.3    Griffin, J.D.4    Gilliland, D.G.5    Sternberg, D.W.6
  • 21
  • 22
    • 85047699293 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase (ALK) activates Stat3 and protects hematopoietic cells from cell death
    • Zamo A., Chiarle R., Piva R., Howes J., Fan Y., Chilosi M., et al. Anaplastic lymphoma kinase (ALK) activates Stat3 and protects hematopoietic cells from cell death. Oncogene 21 (2002) 1038-1047
    • (2002) Oncogene , vol.21 , pp. 1038-1047
    • Zamo, A.1    Chiarle, R.2    Piva, R.3    Howes, J.4    Fan, Y.5    Chilosi, M.6
  • 23
    • 20944441928 scopus 로고    scopus 로고
    • Validating Stat3 in cancer therapy
    • Darnell J.E. Validating Stat3 in cancer therapy. Nat Med 11 (2005) 595-596
    • (2005) Nat Med , vol.11 , pp. 595-596
    • Darnell, J.E.1
  • 24
    • 22144431929 scopus 로고    scopus 로고
    • Genome-wide analysis of STAT target genes: elucidating the mechanism of STAT-mediated oncogenesis
    • Alvarez J.V., and Frank D.A. Genome-wide analysis of STAT target genes: elucidating the mechanism of STAT-mediated oncogenesis. Cancer Biol Ther 3 (2004) 1045-1050
    • (2004) Cancer Biol Ther , vol.3 , pp. 1045-1050
    • Alvarez, J.V.1    Frank, D.A.2
  • 25
    • 1042302005 scopus 로고    scopus 로고
    • The STATs of cancer-new molecular targets come of age
    • Yu H., and Jove R. The STATs of cancer-new molecular targets come of age. Nat Rev Cancer 4 (2004) 97-105
    • (2004) Nat Rev Cancer , vol.4 , pp. 97-105
    • Yu, H.1    Jove, R.2
  • 26
    • 52949096859 scopus 로고    scopus 로고
    • The function of Stat3 in tumor cells and their microenvironment
    • Groner B., Lucks P., and Borghouts C. The function of Stat3 in tumor cells and their microenvironment. Semin Cell Dev Biol 19 (2008) 341-350
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 341-350
    • Groner, B.1    Lucks, P.2    Borghouts, C.3
  • 27
    • 64849111865 scopus 로고    scopus 로고
    • Targeting STAT3 in cancer: how successful are we?
    • Yue P., and Turkson J. Targeting STAT3 in cancer: how successful are we?. Expert Opin Investig Drugs 18 (2009) 45-56
    • (2009) Expert Opin Investig Drugs , vol.18 , pp. 45-56
    • Yue, P.1    Turkson, J.2
  • 28
    • 20944435271 scopus 로고    scopus 로고
    • Stat3 is required for ALK- mediated lymphomagenesis and provides a possible therapeutic target
    • Chiarle R., Simmons W.J., Cai H., Dhall G., Zamo A., and Raz R. Stat3 is required for ALK- mediated lymphomagenesis and provides a possible therapeutic target. Nat Med 11 (2005) 623-629
    • (2005) Nat Med , vol.11 , pp. 623-629
    • Chiarle, R.1    Simmons, W.J.2    Cai, H.3    Dhall, G.4    Zamo, A.5    Raz, R.6
  • 29
    • 0035419348 scopus 로고    scopus 로고
    • Role of signal transducer and activator of transcription 5 in nucleophosmin/anaplastic lymphoma kinase-mediated malignant transformation of lymphoid cells
    • Nieborowska-Skorska M., Slupianek A., Xue L., Zhang Q., Raghunath P.N., Hoser G., et al. Role of signal transducer and activator of transcription 5 in nucleophosmin/anaplastic lymphoma kinase-mediated malignant transformation of lymphoid cells. Cancer Res 61 (2001) 6517-6523
    • (2001) Cancer Res , vol.61 , pp. 6517-6523
    • Nieborowska-Skorska, M.1    Slupianek, A.2    Xue, L.3    Zhang, Q.4    Raghunath, P.N.5    Hoser, G.6
  • 30
    • 35948966315 scopus 로고    scopus 로고
    • Stat5a is epigenetically silenced by the tyrosine kinase NPM1-ALK and acts as a tumor suppressor by reciprocally inhibiting NPM1-ALK expression
    • Zhang Q., Wang H.Y., Liu X., and Wasik M.A. Stat5a is epigenetically silenced by the tyrosine kinase NPM1-ALK and acts as a tumor suppressor by reciprocally inhibiting NPM1-ALK expression. Nature Med 13 (2007) 1341-1348
    • (2007) Nature Med , vol.13 , pp. 1341-1348
    • Zhang, Q.1    Wang, H.Y.2    Liu, X.3    Wasik, M.A.4
  • 32
    • 0031433362 scopus 로고    scopus 로고
    • An indirect effect of STAT5A in IL-2-induced proliferation: a critical role for STAT5A in IL-2-mediated IL-2 receptor alpha chain induction
    • Nakajima H., Liu X.W., Wynshaw-Boris A., Rosenthal L.A., Imada K., Finbloom D.S., et al. An indirect effect of STAT5A in IL-2-induced proliferation: a critical role for STAT5A in IL-2-mediated IL-2 receptor alpha chain induction. Immunity 7 (1997) 691-701
    • (1997) Immunity , vol.7 , pp. 691-701
    • Nakajima, H.1    Liu, X.W.2    Wynshaw-Boris, A.3    Rosenthal, L.A.4    Imada, K.5    Finbloom, D.S.6
  • 33
    • 0033544884 scopus 로고    scopus 로고
    • STAT5B-deficient mice are growth hormone pulse-resistant. Role of STAT5B in sex-specific liver p450 expression
    • Davey H.W., Park S.H., Grattan D.R., McLachlan M.J., and Waxman D.J. STAT5B-deficient mice are growth hormone pulse-resistant. Role of STAT5B in sex-specific liver p450 expression. J Biol Chem 274 (1999) 35331-35336
    • (1999) J Biol Chem , vol.274 , pp. 35331-35336
    • Davey, H.W.1    Park, S.H.2    Grattan, D.R.3    McLachlan, M.J.4    Waxman, D.J.5
  • 34
    • 0031774896 scopus 로고    scopus 로고
    • STAT5B is essential for natural killer cell-mediated proliferation and cytolytic activity
    • Imada K., Bloom E.T., Nakajima H., Horvath-Arcidiacono J.A., Udy G.B., Davey H.W., et al. STAT5B is essential for natural killer cell-mediated proliferation and cytolytic activity. J Exp Med 188 (1998) 2067-2274
    • (1998) J Exp Med , vol.188 , pp. 2067-2274
    • Imada, K.1    Bloom, E.T.2    Nakajima, H.3    Horvath-Arcidiacono, J.A.4    Udy, G.B.5    Davey, H.W.6
  • 35
    • 33846951463 scopus 로고    scopus 로고
    • Oncogenic tyrosine kinase NPM/ALK induces activation of the MEK/ERK signaling pathway independently of c-Raf
    • Marzec M., Kasprzycka M., Liu X., Raghunath P.N., Wlodarski P., and Wasik M.A. Oncogenic tyrosine kinase NPM/ALK induces activation of the MEK/ERK signaling pathway independently of c-Raf. Oncogene 26 (2007) 813-821
    • (2007) Oncogene , vol.26 , pp. 813-821
    • Marzec, M.1    Kasprzycka, M.2    Liu, X.3    Raghunath, P.N.4    Wlodarski, P.5    Wasik, M.A.6
  • 36
    • 33747819801 scopus 로고    scopus 로고
    • mTOR and cancer: insights into a complex relationship
    • Sabatini D.M. mTOR and cancer: insights into a complex relationship. Nat Rev Cancer 6 (2006) 729-734
    • (2006) Nat Rev Cancer , vol.6 , pp. 729-734
    • Sabatini, D.M.1
  • 38
    • 33750058023 scopus 로고    scopus 로고
    • Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?
    • Corradettia M.N., and Guan K.L. Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?. Oncogene 25 (2006) 6347-6360
    • (2006) Oncogene , vol.25 , pp. 6347-6360
    • Corradettia, M.N.1    Guan, K.L.2
  • 39
    • 34547935219 scopus 로고    scopus 로고
    • Oncogenic tyrosine kinase NPM/ALK induces activation of the rapamycin-sensitive mTOR signaling pathway
    • Marzec M., Kasprzycka M., Liu X., El-Salem M., Halasa K., Raghunath P.N., et al. Oncogenic tyrosine kinase NPM/ALK induces activation of the rapamycin-sensitive mTOR signaling pathway. Oncogene 26 (2007) 5606-5614
    • (2007) Oncogene , vol.26 , pp. 5606-5614
    • Marzec, M.1    Kasprzycka, M.2    Liu, X.3    El-Salem, M.4    Halasa, K.5    Raghunath, P.N.6
  • 40
    • 33746118057 scopus 로고    scopus 로고
    • Activation of mammalian target of rapamycin signaling pathway contributes to tumor cell survival in anaplastic lymphoma kinase-positive anaplastic large cell lymphoma
    • Vega F., Medeiros L.J., Leventaki V., Atwell C., Cho-Vega J.H., Tian L., et al. Activation of mammalian target of rapamycin signaling pathway contributes to tumor cell survival in anaplastic lymphoma kinase-positive anaplastic large cell lymphoma. Cancer Res 66 (2006) 6589-6597
    • (2006) Cancer Res , vol.66 , pp. 6589-6597
    • Vega, F.1    Medeiros, L.J.2    Leventaki, V.3    Atwell, C.4    Cho-Vega, J.H.5    Tian, L.6
  • 41
    • 33745587303 scopus 로고    scopus 로고
    • NPM/ALK oncoprotein induces T regulatory cell phenotype by activating STAT3
    • Kasprzycka M., Marzec M., Liu X., Zhang Q., and Wasik M.A. NPM/ALK oncoprotein induces T regulatory cell phenotype by activating STAT3. Proc Natl Acad Sci U S A 103 (2006) 9964-9969
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9964-9969
    • Kasprzycka, M.1    Marzec, M.2    Liu, X.3    Zhang, Q.4    Wasik, M.A.5
  • 42
    • 58549102319 scopus 로고    scopus 로고
    • Oncogenic kinase NPM/ALK induces through STAT3 expression of immunosuppressive protein CD274 (PD-L1, B7-H1)
    • Marzec M., Zhang Q., Goradia A., Raghunath P.N., Liu X., Paessler M., et al. Oncogenic kinase NPM/ALK induces through STAT3 expression of immunosuppressive protein CD274 (PD-L1, B7-H1). Proc Natl Acad Sci U S A 105 (2008) 20852-20857
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20852-20857
    • Marzec, M.1    Zhang, Q.2    Goradia, A.3    Raghunath, P.N.4    Liu, X.5    Paessler, M.6
  • 43
    • 53149136629 scopus 로고    scopus 로고
    • Gamma c-signaling cytokines induce a regulatory T cell (Treg) phenotype in malignant CD4+ T lymphocytes
    • Kasprzycka M., Zhang Q., Witkiewicz A., Marzec M., Potoczek M., Liu X., et al. Gamma c-signaling cytokines induce a regulatory T cell (Treg) phenotype in malignant CD4+ T lymphocytes. J Immunol 181 (2008) 2506-2512
    • (2008) J Immunol , vol.181 , pp. 2506-2512
    • Kasprzycka, M.1    Zhang, Q.2    Witkiewicz, A.3    Marzec, M.4    Potoczek, M.5    Liu, X.6
  • 44
    • 34547794178 scopus 로고    scopus 로고
    • PD-1 and PD-1 ligands: from discovery to clinical application
    • Okazaki T., and Honjo T. PD-1 and PD-1 ligands: from discovery to clinical application. Intern Immunol 19 (2007) 813-824
    • (2007) Intern Immunol , vol.19 , pp. 813-824
    • Okazaki, T.1    Honjo, T.2
  • 46
    • 4944239032 scopus 로고    scopus 로고
    • Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis
    • Chan K.S., Sano S., Kiguchi K., Anders J., Komazawa N., Takeda J., et al. Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis. J Clin Invest 114 (2004) 720-728
    • (2004) J Clin Invest , vol.114 , pp. 720-728
    • Chan, K.S.1    Sano, S.2    Kiguchi, K.3    Anders, J.4    Komazawa, N.5    Takeda, J.6
  • 47
    • 16844368861 scopus 로고    scopus 로고
    • Knockdown of STAT3 expression by RNA interference inhibits the induction of breast tumors in immunocompetent mice
    • Ling X., and Arlinghaus R.B. Knockdown of STAT3 expression by RNA interference inhibits the induction of breast tumors in immunocompetent mice. Cancer Res 65 (2005) 2532-2536
    • (2005) Cancer Res , vol.65 , pp. 2532-2536
    • Ling, X.1    Arlinghaus, R.B.2
  • 48
    • 20944435271 scopus 로고    scopus 로고
    • Stat3 is required for ALK-mediated lymphomagenesis and provides a possible therapeutic target
    • Chiarle R., Simmons W.J., Cai H., Dhall G., Zamo A., Raz R., et al. Stat3 is required for ALK-mediated lymphomagenesis and provides a possible therapeutic target. Nat Med 11 (2005) 623-629
    • (2005) Nat Med , vol.11 , pp. 623-629
    • Chiarle, R.1    Simmons, W.J.2    Cai, H.3    Dhall, G.4    Zamo, A.5    Raz, R.6
  • 49
    • 11144357779 scopus 로고    scopus 로고
    • Regulation of the innate and adaptive immune responses by Stat-3 signaling in tumor cells
    • Wang T., Niu G., Kortylewski M., Burdelya L., Shain K., Zhang S., et al. Regulation of the innate and adaptive immune responses by Stat-3 signaling in tumor cells. Nat Med 10 (2004) 48-54
    • (2004) Nat Med , vol.10 , pp. 48-54
    • Wang, T.1    Niu, G.2    Kortylewski, M.3    Burdelya, L.4    Shain, K.5    Zhang, S.6
  • 51
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones P.A., and Baylin S.B. The epigenomics of cancer. Cell 128 (2007) 683-692
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 52
    • 56749183895 scopus 로고    scopus 로고
    • Epigenetic mechanisms in health and disease
    • van der Maarel S.M. Epigenetic mechanisms in health and disease. Ann Rheum Dis 67 Suppl 3 (2008) iii97-iii100
    • (2008) Ann Rheum Dis , vol.67 , Issue.SUPPL. 3
    • van der Maarel, S.M.1
  • 53
    • 0037434930 scopus 로고    scopus 로고
    • The function of the protein tyrosine phosphatase SHP-1 in cancer
    • Wu C., Sun M., Liu L., and Zhou G.W. The function of the protein tyrosine phosphatase SHP-1 in cancer. Gene 306 (2003) 1-12
    • (2003) Gene , vol.306 , pp. 1-12
    • Wu, C.1    Sun, M.2    Liu, L.3    Zhou, G.W.4
  • 54
    • 0030764557 scopus 로고    scopus 로고
    • Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency
    • Shultz L.D., Rajan T.V., and Greiner D.L. Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency. Trends Biotech 15 (1997) 302-307
    • (1997) Trends Biotech , vol.15 , pp. 302-307
    • Shultz, L.D.1    Rajan, T.V.2    Greiner, D.L.3
  • 55
    • 0033809993 scopus 로고    scopus 로고
    • Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T cells results from methylation of the SHP-1 promoter
    • Zhang Q., Raghunath P.N., Vonderheid E., Odum N., and Wasik M.A. Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T cells results from methylation of the SHP-1 promoter. Am J Pathol 157 (2000) 1137-1146
    • (2000) Am J Pathol , vol.157 , pp. 1137-1146
    • Zhang, Q.1    Raghunath, P.N.2    Vonderheid, E.3    Odum, N.4    Wasik, M.A.5
  • 56
    • 0037112439 scopus 로고    scopus 로고
    • Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant methylation in leukemias/lymphomas
    • Oka T., Ouchida M., Koyama M., Ogama Y., Takada S., Nakatani Y., et al. Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant methylation in leukemias/lymphomas. Cancer Res 62 (2002) 6390-6394
    • (2002) Cancer Res , vol.62 , pp. 6390-6394
    • Oka, T.1    Ouchida, M.2    Koyama, M.3    Ogama, Y.4    Takada, S.5    Nakatani, Y.6
  • 57
    • 4444257905 scopus 로고    scopus 로고
    • Methylation of SHP1 gene and loss of SHP1 protein expression are frequent in systemic anaplastic large cell lymphoma
    • Khoury J.D., Rassidakis G.Z., Medeiros L.J., Amin H.M., and Lai R. Methylation of SHP1 gene and loss of SHP1 protein expression are frequent in systemic anaplastic large cell lymphoma. Blood 104 (2004) 1580-1581
    • (2004) Blood , vol.104 , pp. 1580-1581
    • Khoury, J.D.1    Rassidakis, G.Z.2    Medeiros, L.J.3    Amin, H.M.4    Lai, R.5
  • 58
    • 33646540436 scopus 로고    scopus 로고
    • SHP1 tyrosine phosphatase negatively regulates NPM- ALK tyrosine kinase signaling
    • Honorat J.F., Ragab A., and Lamant L. SHP1 tyrosine phosphatase negatively regulates NPM- ALK tyrosine kinase signaling. Blood 107 (2006) 4130-4138
    • (2006) Blood , vol.107 , pp. 4130-4138
    • Honorat, J.F.1    Ragab, A.2    Lamant, L.3
  • 59
    • 18744395503 scopus 로고    scopus 로고
    • STAT3- and DNMT1-mediated epigenetic silencing of SHP-1 tyrosine phosphatase tumor suppressor gene in malignant T lymphocytes
    • Zhang Q., Wang H.Y., Marzec M., Raghunath P.N., Nagasawa T., and Wasik M.A. STAT3- and DNMT1-mediated epigenetic silencing of SHP-1 tyrosine phosphatase tumor suppressor gene in malignant T lymphocytes. Proc Natl Acad Sci U S A 102 (2005) 6948-6953
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6948-6953
    • Zhang, Q.1    Wang, H.Y.2    Marzec, M.3    Raghunath, P.N.4    Nagasawa, T.5    Wasik, M.A.6
  • 60
    • 33746651038 scopus 로고    scopus 로고
    • STAT3 induces transcription of the DNA methyltransferase 1 (DNMT1) gene in malignant T- lymphocytes
    • Zhang Q., Wang H.Y., Woetmann A., Raghunath P.N., Odum N., and Wasik M.A. STAT3 induces transcription of the DNA methyltransferase 1 (DNMT1) gene in malignant T- lymphocytes. Blood 108 (2006) 1058-1064
    • (2006) Blood , vol.108 , pp. 1058-1064
    • Zhang, Q.1    Wang, H.Y.2    Woetmann, A.3    Raghunath, P.N.4    Odum, N.5    Wasik, M.A.6
  • 61
    • 21744462480 scopus 로고    scopus 로고
    • Chronic myeloid leukemia: a model for oncology
    • Hehlmann R., Berger U., and Hochhaus A. Chronic myeloid leukemia: a model for oncology. Ann Hematol 84 (2005) 487-497
    • (2005) Ann Hematol , vol.84 , pp. 487-497
    • Hehlmann, R.1    Berger, U.2    Hochhaus, A.3
  • 62
    • 0036154836 scopus 로고    scopus 로고
    • Model of inhibition of the NPM-ALK kinase activity by Herbimycin A
    • Turturro F., Arnold M.D., Frist A.Y., and Pulford K. Model of inhibition of the NPM-ALK kinase activity by Herbimycin A. Clin Cancer Res 8 (2002) 240-245
    • (2002) Clin Cancer Res , vol.8 , pp. 240-245
    • Turturro, F.1    Arnold, M.D.2    Frist, A.Y.3    Pulford, K.4
  • 63
    • 0034888811 scopus 로고    scopus 로고
    • Inhibition of tyrosine kinase activity induces caspase-dependent apoptosis in anaplastic large cell lymphoma with NPM-ALK (p80) fusion protein
    • Ergin M., Denning M.F., Izban K.F., Amin H.M., Martinez R.L., Saeed S., et al. Inhibition of tyrosine kinase activity induces caspase-dependent apoptosis in anaplastic large cell lymphoma with NPM-ALK (p80) fusion protein. Exp Hematol 29 (2001) 1082-1090
    • (2001) Exp Hematol , vol.29 , pp. 1082-1090
    • Ergin, M.1    Denning, M.F.2    Izban, K.F.3    Amin, H.M.4    Martinez, R.L.5    Saeed, S.6
  • 64
    • 27944485366 scopus 로고    scopus 로고
    • Inhibition of ALK enzymatic activity in T-cell lymphoma cells induces apoptosis and suppresses proliferation and STAT3 phosphorylation independently of Jak3
    • Marzec M., Kasprzycka M., Ptasznik A., Wlodarski P., Zhang Q., Odum N., et al. Inhibition of ALK enzymatic activity in T-cell lymphoma cells induces apoptosis and suppresses proliferation and STAT3 phosphorylation independently of Jak3. Lab Invest 85 (2005) 1544-1554
    • (2005) Lab Invest , vol.85 , pp. 1544-1554
    • Marzec, M.1    Kasprzycka, M.2    Ptasznik, A.3    Wlodarski, P.4    Zhang, Q.5    Odum, N.6
  • 65
    • 32644442671 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase activity is essential for the proliferation and survival of anaplastic large-cell lymphoma cells
    • Wan W., Albom M.S., Lu L., Quail M.R., Becknell N.C., Weinberg L.R., et al. Anaplastic lymphoma kinase activity is essential for the proliferation and survival of anaplastic large-cell lymphoma cells. Blood 107 (2006) 1617-1623
    • (2006) Blood , vol.107 , pp. 1617-1623
    • Wan, W.1    Albom, M.S.2    Lu, L.3    Quail, M.R.4    Becknell, N.C.5    Weinberg, L.R.6
  • 66
    • 33846110366 scopus 로고    scopus 로고
    • Identification of NVP-TAE684: a potent, selective and efficacious inhibitor of NPM-ALK
    • Galkin A.V., Melnick J.S., Kim S., Hood T.L., Li N., Li L., et al. Identification of NVP-TAE684: a potent, selective and efficacious inhibitor of NPM-ALK. Proc Natl Acad Sci U S A 104 (2007) 270-275
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 270-275
    • Galkin, A.V.1    Melnick, J.S.2    Kim, S.3    Hood, T.L.4    Li, N.5    Li, L.6
  • 67
    • 42549119526 scopus 로고    scopus 로고
    • Development of anaplastic lymphoma kinase (ALK) small-molecule inhibitors for cancer therapy
    • Li R., and Morris S.W. Development of anaplastic lymphoma kinase (ALK) small-molecule inhibitors for cancer therapy. Med Res Rev 28 (2008) 372-412
    • (2008) Med Res Rev , vol.28 , pp. 372-412
    • Li, R.1    Morris, S.W.2
  • 68
    • 0242624636 scopus 로고    scopus 로고
    • Epigenetic targets in hematopoietic malignancies
    • Claus R., and Lübbert M. Epigenetic targets in hematopoietic malignancies. Oncogene 22 (2003) 6489-6496
    • (2003) Oncogene , vol.22 , pp. 6489-6496
    • Claus, R.1    Lübbert, M.2
  • 69
    • 21844466446 scopus 로고    scopus 로고
    • Pharmacology of 5-aza-2′-deoxycytidine (decitabine)
    • Momparler R.L. Pharmacology of 5-aza-2′-deoxycytidine (decitabine). Semin Hematol 42 Suppl (2005) S9-S16
    • (2005) Semin Hematol , vol.42 , Issue.SUPPL
    • Momparler, R.L.1
  • 70
    • 25844465921 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer with 5-aza-2′-deoxycytidine (decitabine)
    • Momparler R.L. Epigenetic therapy of cancer with 5-aza-2′-deoxycytidine (decitabine). Semin Oncol 32 (2005) 443-451
    • (2005) Semin Oncol , vol.32 , pp. 443-451
    • Momparler, R.L.1
  • 71
    • 34249779568 scopus 로고    scopus 로고
    • Global ARCC Trial. Temsirolimus, interferon alfa, or both for advanced renal-cell carcinoma
    • Hudes G., Carducci M., Tomczak P., Dutcher J., Figlin R., Kapoor A., et al. Global ARCC Trial. Temsirolimus, interferon alfa, or both for advanced renal-cell carcinoma. N Engl J Med 356 (2007) 2271-2281
    • (2007) N Engl J Med , vol.356 , pp. 2271-2281
    • Hudes, G.1    Carducci, M.2    Tomczak, P.3    Dutcher, J.4    Figlin, R.5    Kapoor, A.6
  • 72
    • 13944250650 scopus 로고    scopus 로고
    • In vivo antitumor efficacy of STAT3 blockade using a transcription factor decoy approach: implications for cancer therapy
    • Xi S., Gooding W.E., and Grandis J.R. In vivo antitumor efficacy of STAT3 blockade using a transcription factor decoy approach: implications for cancer therapy. Oncogene 24 (2004) 970-979
    • (2004) Oncogene , vol.24 , pp. 970-979
    • Xi, S.1    Gooding, W.E.2    Grandis, J.R.3
  • 73
    • 16844368861 scopus 로고    scopus 로고
    • Knockdown of STAT3 expression by RNA interference inhibits the induction of breast tumors in immunocompetent mice
    • Ling X., and Arlinghaus R.B. Knockdown of STAT3 expression by RNA interference inhibits the induction of breast tumors in immunocompetent mice. Cancer Res 65 (2005) 2532-2536
    • (2005) Cancer Res , vol.65 , pp. 2532-2536
    • Ling, X.1    Arlinghaus, R.B.2
  • 74
    • 3543055012 scopus 로고    scopus 로고
    • Novel peptidomimetic inhibitors of signal transducer and activator of transcription 3 dimerization and biological activity
    • Turkson J., Kim J.S., Zhang S., Yuan J., Huang M., Glenn M., et al. Novel peptidomimetic inhibitors of signal transducer and activator of transcription 3 dimerization and biological activity. Mol Cancer Ther 3 (2004) 261-269
    • (2004) Mol Cancer Ther , vol.3 , pp. 261-269
    • Turkson, J.1    Kim, J.S.2    Zhang, S.3    Yuan, J.4    Huang, M.5    Glenn, M.6
  • 75
    • 0034663414 scopus 로고    scopus 로고
    • Immune response to the ALK oncogenic tyrosine kinase in patients with anaplastic large-cell lymphoma
    • Pulford K., Falini B., Banham A.H., Codrington D., Roberton H., Hatton C., et al. Immune response to the ALK oncogenic tyrosine kinase in patients with anaplastic large-cell lymphoma. Blood 96 (2000) 1605-1607
    • (2000) Blood , vol.96 , pp. 1605-1607
    • Pulford, K.1    Falini, B.2    Banham, A.H.3    Codrington, D.4    Roberton, H.5    Hatton, C.6
  • 76
    • 0037085808 scopus 로고    scopus 로고
    • ALK as a novel lymphoma-associated tumor antigen: identification of 2 HLA-A2.1-restricted CD8+ T-cell epitopes
    • Passoni L., Scardino A., Bertazzoli C., Gallo B., Coluccia A.M., Lemonnier F.A., et al. ALK as a novel lymphoma-associated tumor antigen: identification of 2 HLA-A2.1-restricted CD8+ T-cell epitopes. Blood 99 (2002) 2100-2106
    • (2002) Blood , vol.99 , pp. 2100-2106
    • Passoni, L.1    Scardino, A.2    Bertazzoli, C.3    Gallo, B.4    Coluccia, A.M.5    Lemonnier, F.A.6
  • 77
    • 44949166624 scopus 로고    scopus 로고
    • The anaplastic lymphoma kinase is an effective oncoantigen for lymphoma vaccination
    • Chiarle R., Martinengo C., Mastini C., Ambrogio C., D'Escamard V., Forni G., et al. The anaplastic lymphoma kinase is an effective oncoantigen for lymphoma vaccination. Nat Med 14 (2008) 676-680
    • (2008) Nat Med , vol.14 , pp. 676-680
    • Chiarle, R.1    Martinengo, C.2    Mastini, C.3    Ambrogio, C.4    D'Escamard, V.5    Forni, G.6
  • 78
    • 38449107219 scopus 로고    scopus 로고
    • Targeting molecular and cellular inhibitory mechanisms for improvement of antitumor memory responses reactivated by tumor cell vaccine
    • Webster W.S., Thompson R.H., Harris K.J., Frigola X., Kuntz S., Inman B.A., et al. Targeting molecular and cellular inhibitory mechanisms for improvement of antitumor memory responses reactivated by tumor cell vaccine. J Immunol 179 (2007) 2860-2869
    • (2007) J Immunol , vol.179 , pp. 2860-2869
    • Webster, W.S.1    Thompson, R.H.2    Harris, K.J.3    Frigola, X.4    Kuntz, S.5    Inman, B.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.