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Volumn 287, Issue 22, 2012, Pages 18182-18189

Signal transducer and activator of transcription 3 (STAT3) protein suppresses adenoma-to-carcinoma transition in Apcmin/+ mice via regulation of Snail-1 (SNAI) protein stability

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; DISEASES; MAMMALS; MOLLUSCS; PROTEINS; TRANSCRIPTION;

EID: 84861567294     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.328831     Document Type: Article
Times cited : (63)

References (42)
  • 1
    • 70350500225 scopus 로고    scopus 로고
    • STATs in cancer inflammation and immunity: A leading role for STAT3
    • Yu, H., Pardoll, D., and Jove, R. (2009) STATs in cancer inflammation and immunity: a leading role for STAT3. Nat. Rev. Cancer 9, 798-809
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 798-809
    • Yu, H.1    Pardoll, D.2    Jove, R.3
  • 2
    • 0030999696 scopus 로고    scopus 로고
    • STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor
    • DOI 10.1126/science.276.5317.1418
    • Pfeffer, L. M., Mullersman, J. E., Pfeffer, S. R., Murti, A., Shi, W., and Yang, C. H. (1997) STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor. Science 276, 1418-1420 (Pubitemid 27235410)
    • (1997) Science , vol.276 , Issue.5317 , pp. 1418-1420
    • Pfeffer, L.M.1    Mullersman, J.E.2    Pfeffer, S.R.3    Murti, A.4    Shi, W.5    Yang, C.H.6
  • 3
    • 30944435466 scopus 로고    scopus 로고
    • Stat3 regulates microtubules by antagonizing the depolymerization activity of stathmin
    • DOI 10.1083/jcb.200503021
    • Ng, D. C., Lin, B. H., Lim, C. P., Huang, G., Zhang, T., Poli, V., and Cao, X. (2006) Stat3 regulates microtubules by antagonizing the depolymerization activity of stathmin. J. Cell Biol. 172, 245-257 (Pubitemid 43112971)
    • (2006) Journal of Cell Biology , vol.172 , Issue.2 , pp. 245-257
    • Ng, D.C.H.1    Bao, H.L.2    Cheh, P.L.3    Huang, G.4    Zhang, T.5    Poli, V.6    Cao, X.7
  • 6
    • 0032489508 scopus 로고    scopus 로고
    • Intestinal tumorigenesis in compound mutant mice of both Dpc4 (Smad4) and Apc genes
    • DOI 10.1016/S0092-8674(00)81132-0
    • Takaku, K., Oshima, M., Miyoshi, H., Matsui, M., Seldin, M. F., and Taketo, M. M. (1998) Intestinal tumorigenesis in compound mutant mice of both Dpc4 (Smad4) and Apc genes. Cell 92, 645-656 (Pubitemid 28141513)
    • (1998) Cell , vol.92 , Issue.5 , pp. 645-656
    • Takaku, K.1    Oshima, M.2    Miyoshi, H.3    Matsui, M.4    Seldin, M.F.5    Taketo, M.M.6
  • 8
    • 34249289041 scopus 로고    scopus 로고
    • Snail, ZEB and bHLH factors in tumour progression: An alliance against the epithelial phenotype?
    • DOI 10.1038/nrc2131, PII NRC2131
    • Peinado, H., Olmeda, D., and Cano, A. (2007) Snail, Zeb, andbHLHfactors in tumour progression: an alliance against the epithelial phenotype? Nat. Rev. Cancer 7, 415-428 (Pubitemid 46809165)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.6 , pp. 415-428
    • Peinado, H.1    Olmeda, D.2    Cano, A.3
  • 9
    • 25444439289 scopus 로고    scopus 로고
    • Inducible expression of Snail selectively increases paracellular ion permeability and differentially modulates tight junction proteins
    • DOI 10.1152/ajpcell.00175.2005
    • Carrozzino, F., Soulié, P., Huber, D., Mensi, N., Orci, L., Cano, A., Féraille, E., and Montesano, R. (2005) Inducible expression of Snail selectively increases paracellular ion permeability and differentially modulates tight junction proteins. Am. J. Physiol. Cell Physiol. 289, C1002-1014 (Pubitemid 41361654)
    • (2005) American Journal of Physiology - Cell Physiology , vol.289 , Issue.4
    • Carrozzino, F.1    Soulie, P.2    Huber, D.3    Mensi, N.4    Orci, L.5    Cano, A.6    Feraille, E.7    Montesano, R.8
  • 10
    • 0038106228 scopus 로고    scopus 로고
    • Regulation of tight junctions during the epithelium-mesenchyme transition: Direct repression of the gene expression of claudins/occludin by Snail
    • DOI 10.1242/jcs.00389
    • Ikenouchi, J., Matsuda, M., Furuse, M., and Tsukita, S. (2003) Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail. J. Cell Sci. 116, 1959-1967 (Pubitemid 36622294)
    • (2003) Journal of Cell Science , vol.116 , Issue.10 , pp. 1959-1967
    • Ikenouchi, J.1    Matsuda, M.2    Furuse, M.3    Tsukita, S.4
  • 13
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of Snail by GSK-3β-mediated phosphorylation in control of epithelial-mesenchymal transition
    • DOI 10.1038/ncb1173
    • Zhou, B. P., Deng, J., Xia, W., Xu, J., Li, Y. M., Gunduz, M., and Hung, M. C. (2004) Dual regulation of Snail by GSK-3β-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat. Cell Biol. 6, 931-940 (Pubitemid 39359846)
    • (2004) Nature Cell Biology , vol.6 , Issue.10 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6    Hung, M.-C.7
  • 14
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M., and Hemmings, B. A. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789 (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 16
    • 0033597936 scopus 로고    scopus 로고
    • Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway
    • Hartigan, J. A., and Johnson, G. V. (1999) Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway. J. Biol. Chem. 274, 21395-21401
    • (1999) J. Biol. Chem. , vol.274 , pp. 21395-21401
    • Hartigan, J.A.1    Johnson, G.V.2
  • 17
    • 0032955426 scopus 로고    scopus 로고
    • Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3β and Fyn tyrosine kinase
    • DOI 10.1046/j.1471-4159.1999.0720576.x
    • Lesort, M., Jope, R. S., and Johnson, G. V. (1999) Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3βand Fyn tyrosine kinase. J. Neurochem. 72, 576-584 (Pubitemid 29055219)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.2 , pp. 576-584
    • Lesort, M.1    Jope, R.S.2    Johnson, G.V.W.3
  • 18
    • 0037413694 scopus 로고    scopus 로고
    • Gene structure and alternative splicing of glycogen synthase kinase 3 beta (GSK-3β) in neural and non-neural tissues
    • DOI 10.1016/S0378-1119(02)01092-2
    • Schaffer, B., Wiedau-Pazos, M., and Geschwind, D. H. (2003) Gene structure and alternative splicing of glycogen synthase kinase 3β (GSK-3β) in neural and non-neural tissues. Gene 302, 73-81 (Pubitemid 36078399)
    • (2003) Gene , vol.302 , Issue.1-2 , pp. 73-81
    • Schaffer, B.1    Wiedau-Pazos, M.2    Geschwind, D.H.3
  • 19
    • 0028569010 scopus 로고
    • Phosphorylation of the Drosophila adherens junction protein Armadillo: Roles for wingless signal and zeste-white 3 kinase
    • Peifer, M., Pai, L. M., and Casey, M. (1994) Phosphorylation of the Drosophila adherens junction protein Armadillo: roles for wingless signal and zeste-white 3 kinase. Dev. Biol. 166, 543-556
    • (1994) Dev. Biol. , vol.166 , pp. 543-556
    • Peifer, M.1    Pai, L.M.2    Casey, M.3
  • 20
    • 0029683606 scopus 로고    scopus 로고
    • The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3
    • Yost, C., Torres, M., Miller, J. R., Huang, E., Kimelman, D., and Moon, R. T. (1996) The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev. 10, 1443-1454 (Pubitemid 26260702)
    • (1996) Genes and Development , vol.10 , Issue.12 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.R.3    Huang, E.4    Kimelman, D.5    Moon, R.T.6
  • 21
    • 79751489596 scopus 로고    scopus 로고
    • Molecular genetics of colorectal cancer
    • Fearon, E. R. (2011) Molecular genetics of colorectal cancer. Annu. Rev. Pathol. 6, 479-507
    • (2011) Annu. Rev. Pathol. , vol.6 , pp. 479-507
    • Fearon, E.R.1
  • 22
    • 0030265301 scopus 로고    scopus 로고
    • Manipulation of the mouse germline in the study of Min-induced neoplasia
    • DOI 10.1006/scbi.1996.0033
    • Bilger, A., Shoemaker, A. R., Gould, K. A., and Dove, W. F. (1996) Manipulation of the mouse germ line in the study of Min-induced neoplasia. Semin. Cancer Biol. 7, 249-260 (Pubitemid 27182784)
    • (1996) Seminars in Cancer Biology , vol.7 , Issue.5 , pp. 249-260
    • Bilger, A.1    Shoemaker, A.R.2    Gould, K.A.3    Dove, W.F.4
  • 23
    • 0025312728 scopus 로고
    • A genetic model for colorectal tumorigenesis
    • Fearon, E. R., and Vogelstein, B. (1990) A genetic model for colorectal tumorigenesis. Cell 61, 759-767
    • (1990) Cell , vol.61 , pp. 759-767
    • Fearon, E.R.1    Vogelstein, B.2
  • 27
    • 0037799912 scopus 로고    scopus 로고
    • Toll-like receptor-dependent production of IL-12p40 causes chronic enterocolitis in myeloid cell-specific Stat3-deficient mice
    • DOI 10.1172/JCI200317085
    • Kobayashi, M., Kweon, M. N., Kuwata, H., Schreiber, R. D., Kiyono, H., Takeda, K., and Akira, S. (2003) Toll-like receptor-dependent production of IL-12p40 causes chronic enterocolitis in myeloid cell-specific Stat3- deficient mice. J. Clin. Invest. 111, 1297-1308 (Pubitemid 36554700)
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.9 , pp. 1297-1308
    • Kobayashi, M.1    Kweon, M.-N.2    Kuwata, H.3    Schreiber, R.D.4    Kiyono, H.5    Takeda, K.6    Akira, S.7
  • 28
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock, K., Plaks, V., and Werb, Z. (2010) Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141, 52-67
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 29
    • 1242292412 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases (MMPs) in colorectal cancer
    • DOI 10.1023/A:1025867130437
    • Zucker, S., and Vacirca, J. (2004) Role of matrix metalloproteinases (MMPs) in colorectal cancer. Cancer Metastasis Rev. 23, 101-117 (Pubitemid 38221598)
    • (2004) Cancer and Metastasis Reviews , vol.23 , Issue.1-2 , pp. 101-117
    • Zucker, S.1    Vacirca, J.2
  • 30
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • DOI 10.1016/S0092-8674(03)00513-0
    • Hotary, K. B., Allen, E. D., Brooks, P. C., Datta, N. S., Long, M. W., and Weiss, S. J. (2003) Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 114, 33-45 (Pubitemid 36859839)
    • (2003) Cell , vol.114 , Issue.1 , pp. 33-45
    • Hotary, K.B.1    Allen, E.D.2    Brooks, P.C.3    Datta, N.S.4    Long, M.W.5    Weiss, S.J.6
  • 31
    • 73949087260 scopus 로고    scopus 로고
    • Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1
    • Ota, I., Li, X. Y., Hu, Y., and Weiss, S. J. (2009) Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1. Proc. Natl. Acad. Sci. U.S.A. 106, 20318-20323
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20318-20323
    • Ota, I.1    Li, X.Y.2    Hu, Y.3    Weiss, S.J.4
  • 32
    • 78650790948 scopus 로고    scopus 로고
    • Improved Phos-tag SDSPAGE under neutral pH conditions for advanced protein phosphorylation profiling
    • Kinoshita, E., and Kinoshita-Kikuta, E. (2011) Improved Phos-tag SDSPAGE under neutral pH conditions for advanced protein phosphorylation profiling. Proteomics 11, 319-323
    • (2011) Proteomics , vol.11 , pp. 319-323
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2
  • 34
    • 4944239032 scopus 로고    scopus 로고
    • Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis
    • DOI 10.1172/JCI200421032
    • Chan, K. S., Sano, S., Kiguchi, K., Anders, J., Komazawa, N., Takeda, J., and DiGiovanni, J. (2004) Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis. J. Clin. Invest. 114, 720-728 (Pubitemid 39578762)
    • (2004) Journal of Clinical Investigation , vol.114 , Issue.5 , pp. 720-728
    • Chan, K.S.1    Sano, S.2    Kiguchi, K.3    Anders, J.4    Komazawa, N.5    Takeda, J.6    DiGiovanni, J.7
  • 35
    • 20944435271 scopus 로고    scopus 로고
    • Stat3 is required for ALK-mediated lymphomagenesis and provides a possible therapeutic target
    • DOI 10.1038/nm1249
    • Chiarle, R., Simmons, W. J., Cai, H., Dhall, G., Zamo, A., Raz, R., Karras, J. G., Levy, D. E., and Inghirami, G. (2005) Stat3 is required for ALKmediated lymphomutagenesis and provides a possible therapeutic target. Nat. Med. 11, 623-629 (Pubitemid 40868302)
    • (2005) Nature Medicine , vol.11 , Issue.6 , pp. 623-629
    • Chiarle, R.1    Simmons, W.J.2    Cai, H.3    Dhall, G.4    Zamo, A.5    Raz, R.6    Karras, J.G.7    Levy, D.E.8    Inghirami, G.9
  • 37
    • 23444452377 scopus 로고    scopus 로고
    • Expression of p-STAT3 in human colorectal adenocarcinoma and adenoma; correlation with clinicopathological factors
    • DOI 10.1136/jcp.2004.023416
    • Kusaba, T., Nakayama, T., Yamazumi, K., Yakata, Y., Yoshizaki, A., Nagayasu, T., and Sekine, I. (2005) Expression of p-STAT3 in human colorectal adenocarcinoma and adenoma: correlation with clinicopathological factors. J. Clin. Pathol. 58, 833-838 (Pubitemid 41113390)
    • (2005) Journal of Clinical Pathology , vol.58 , Issue.8 , pp. 833-838
    • Kusaba, T.1    Nakayama, T.2    Yamazumi, K.3    Yakata, Y.4    Yoshizaki, A.5    Nagayasu, T.6    Sekine, I.7
  • 38
    • 54549098153 scopus 로고    scopus 로고
    • Significance of p-STAT3 expression in human colorectal adenocarcinoma
    • Park, J. K., Hong, R., Kim, K. J., Lee, T. B., and Lim, S. C. (2008) Significance of p-STAT3 expression in human colorectal adenocarcinoma. Oncol. Rep. 20, 597-604
    • (2008) Oncol. Rep. , vol.20 , pp. 597-604
    • Park, J.K.1    Hong, R.2    Kim, K.J.3    Lee, T.B.4    Lim, S.C.5
  • 39
    • 2442707740 scopus 로고    scopus 로고
    • Disruption of STAT3 signaling leads to tumor cell invasion through alterations of homotypic cell-cell adhesion complexes
    • DOI 10.1038/sj.onc.1207437
    • Rivat, C., De Wever, O., Bruyneel, E., Mareel, M., Gespach, C., and Attoub, S. (2004) Disruption of STAT3 signaling leads to tumor cell invasion through alterations of homotypic cell-cell adhesion complexes. Oncogene 23, 3317-3327 (Pubitemid 38669821)
    • (2004) Oncogene , vol.23 , Issue.19 , pp. 3317-3327
    • Rivat, C.1    De Wever, O.2    Bruyneel, E.3    Mareel, M.4    Gespach, C.5    Attoub, S.6
  • 42
    • 77549083560 scopus 로고    scopus 로고
    • Dangerous liaisons: STAT3 and NF-κB collaboration and cross-talk in cancer
    • Grivennikov, S. I., and Karin, M. (2010) Dangerous liaisons: STAT3 and NF-κB collaboration and cross-talk in cancer. Cytokine Growth Factor Rev. 21, 11-19
    • (2010) Cytokine Growth Factor Rev. , vol.21 , pp. 11-19
    • Grivennikov, S.I.1    Karin, M.2


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