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Volumn 6, Issue 7, 2006, Pages 506-520

Tumour microenvironment - TGFΒ: The molecular Jekyll and Hyde of cancer

Author keywords

[No Author keywords available]

Indexed keywords

4 [4 (1,3 BENZODIOXOL 5 YL) 5 (2 PYRIDINYL) 1H IMIDAZOL 2 YL]BENZAMIDE; A 8001; ACTIVIN; AP 11014; AP 12009; BONE MORPHOGENETIC PROTEIN RECEPTOR; DAXX PROTEIN; FAS LIGAND; GELATINASE A; GELATINASE B; KERATIN; LERDELIMUMAB; LORICRIN; LY 364947; LY 550410; LY 566578; LY 580276; MAJOR HISTOCOMPATIBILITY ANTIGEN; METELIMUMAB; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE 1; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1D11; MONOCLONAL ANTIBODY 2G7; MONOCLONAL ANTIBODY GC 1008; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN CDC42; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SB 208; SB 505124; SD 093; SMAD ANCHOR FOR RECEPTOR ACTIVATION; SMAD1 PROTEIN; SMAD2 PROTEIN; SMAD3 PROTEIN; SMAD4 PROTEIN; SMAD5 PROTEIN; SMAD8 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33745515023     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1926     Document Type: Review
Times cited : (1146)

References (157)
  • 1
    • 0242499448 scopus 로고    scopus 로고
    • Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
    • Siegel, P. M. & Massague, J. Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer. Nature Rev. Cancer 3, 807-821 (2003).
    • (2003) Nature Rev. Cancer , vol.3 , pp. 807-821
    • Siegel, P.M.1    Massague, J.2
  • 2
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-β family signalling
    • Derynck, R. & Zhang, Y. E. Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 425, 577-584 (2003).
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 4
    • 0026537831 scopus 로고
    • Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase
    • Lin, H. Y., Wang, X. F., Ng-Eaton, E., Weinberg, R. A. & Lodish, H. F. Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase. Cell 68, 775-785 (1992). Describes the initial cloning and characterization of the type II TGFβ receptor. The binding affinity of TGFβ1 and TGFβ2 was shown, along with an analysis of this receptor as a functional serine and threonine kinase.
    • (1992) Cell , vol.68 , pp. 775-785
    • Lin, H.Y.1    Wang, X.F.2    Ng-Eaton, E.3    Weinberg, R.A.4    Lodish, H.F.5
  • 5
    • 0025989562 scopus 로고
    • Expression cloning and characterization of the TGF-β type III receptor
    • Wang, X. F. et al. Expression cloning and characterization of the TGF-β type III receptor. Cell 67, 797-805 (1991). Describes the initial cloning and characterization of a type III TGFβ receptor. It was shown that the cloned type III receptor was able to bind TGFβ1 and increase the ligand affinity for the type II TGFβ receptor.
    • (1991) Cell , vol.67 , pp. 797-805
    • Wang, X.F.1
  • 6
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis
    • Yu, Q. & Stamenkovic, I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev. 14, 163-176 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 7
    • 0033524949 scopus 로고    scopus 로고
    • The integrin-α ν β 6 binds and activates latent TGF β 1: A mechanism for regulating pulmonary inflammation and fibrosis
    • Munger, J. S. et al. The integrin-α ν β 6 binds and activates latent TGF β 1: a mechanism for regulating pulmonary inflammation and fibrosis. Cell 96, 319-328 (1999).
    • (1999) Cell , vol.96 , pp. 319-328
    • Munger, J.S.1
  • 8
    • 0028878041 scopus 로고
    • The soluble exoplasmic domain of the type II transforming growth factor (TGF)-β receptor. a heterogeneously glycosylated protein with high affinity and selectivity for TGF-β ligands
    • Lin, H. Y. et al. The soluble exoplasmic domain of the type II transforming growth factor (TGF)-β receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-β ligands. J. Biol. Chem. 270, 2747-2754 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2747-2754
    • Lin, H.Y.1
  • 9
    • 12344320716 scopus 로고    scopus 로고
    • Thrombospondin-1 is a major activator of TGF-β1 in vivo
    • Crawford, S. E. et al. Thrombospondin-1 is a major activator of TGF-β1 in vivo. Cell 93, 1159-1170 (1998).
    • (1998) Cell , vol.93 , pp. 1159-1170
    • Crawford, S.E.1
  • 10
    • 0027490673 scopus 로고
    • The transforming growth factor-β receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
    • Moustakas, A. et al. The transforming growth factor-β receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand. J. Biol. Chem. 268, 22215-22218 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22215-22218
    • Moustakas, A.1
  • 11
    • 0032559594 scopus 로고    scopus 로고
    • Oligomeric structure of type I and type II transforming growth factor-β receptors: Homodimers form in the ER and persist at the plasma membrane
    • Gilboa, L., Wells, R. G., Lodish, H. F. & Henis, Y. I. Oligomeric structure of type I and type II transforming growth factor-β receptors: homodimers form in the ER and persist at the plasma membrane. J. Cell. Biol. 140, 767-777 (1998).
    • (1998) J. Cell. Biol. , vol.140 , pp. 767-777
    • Gilboa, L.1    Wells, R.G.2    Lodish, H.F.3    Henis, Y.I.4
  • 12
    • 0242330126 scopus 로고    scopus 로고
    • Activin receptor-like kinase (ALK)1 is an antagonistic mediator of lateral TGFβ/ALK5 signaling
    • Goumans, M. J. et al. Activin receptor-like kinase (ALK)1 is an antagonistic mediator of lateral TGFβ/ALK5 signaling. Mol. Cell 12, 817-828 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 817-828
    • Goumans, M.J.1
  • 13
    • 0026496172 scopus 로고
    • TGF β signals through a heteromeric protein kinase receptor complex
    • Wrana, J. L. et al. TGF β signals through a heteromeric protein kinase receptor complex. Cell 71, 1003-1014 (1992).
    • (1992) Cell , vol.71 , pp. 1003-1014
    • Wrana, J.L.1
  • 14
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction
    • Luo, K. & Lodish, H. F. Signaling by chimeric erythropoietin-TGF- β receptors: homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J. 15, 4485-4496 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, H.F.2
  • 15
    • 17544376741 scopus 로고    scopus 로고
    • Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors
    • Feng, X. H. & Derynck, R. Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors. J. Biol. Chem. 271, 13123-13129 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 13123-13129
    • Feng, X.H.1    Derynck, R.2
  • 16
    • 33644989417 scopus 로고    scopus 로고
    • Transforming growth factor-β stimulates epithelial-mesenchymal transformation in the proepicardium
    • Olivey, H. E., Mundell, N. A., Austin, A. F. & Barnett, J. V. Transforming growth factor-β stimulates epithelial-mesenchymal transformation in the proepicardium. Dev. Dyn. 235, 50-59 (2006).
    • (2006) Dev. Dyn. , vol.235 , pp. 50-59
    • Olivey, H.E.1    Mundell, N.A.2    Austin, A.F.3    Barnett, J.V.4
  • 17
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y. & Massague, J. Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113, 685-700 (2003).
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 18
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-β signals
    • Moustakas, A. & Heldin, C. H. Non-Smad TGF-β signals. J. Cell Sci. 118, 3573-3584 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 19
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodiles, M. et al. High-throughput mapping of a dynamic signaling network in mammalian cells. Science 307, 1621-1625 (2005). The TGFβ pathway has been targeted for interactome mapping. This paper and supplementary material outlines the results from approximately 12,000 individual experimental reactions that resulted in the identification of a large number of new interactions.
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodiles, M.1
  • 20
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in tgf-β signaling through Smads
    • Feng, X. H. & Derynck, R. Specificity and versatility in tgf-β signaling through Smads. Annu. Rev. Cell Dev. Biol. 21, 659-693 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 21
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-β signals
    • Massague, J. How cells read TGF-β signals. Nature Rev. Mol. Cell Biol. 1, 169-178 (2000).
    • (2000) Nature Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massague, J.1
  • 22
    • 0035501062 scopus 로고    scopus 로고
    • TGF-β signaling in cancer-a double-edged sword
    • Akhurst, R. J. & Derynck, R. TGF-β signaling in cancer-a double-edged sword. Trends Cell Biol. 11, S44-S51 (2001).
    • (2001) Trends Cell Biol. , vol.11
    • Akhurst, R.J.1    Derynck, R.2
  • 23
    • 0034785348 scopus 로고    scopus 로고
    • TGF-β signaling in tumor suppression and cancer progression
    • Derynck, R., Akhurst, R. J. & Balmain, A. TGF-β signaling in tumor suppression and cancer progression. Nature Genet. 29, 117-129 (2001).
    • (2001) Nature Genet. , vol.29 , pp. 117-129
    • Derynck, R.1    Akhurst, R.J.2    Balmain, A.3
  • 24
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • Lin, H. K., Bergmann, S. & Pandolfi, P. P. Cytoplasmic PML function in TGF-β signalling. Nature 431, 205-211 (2004).
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 25
    • 0042237016 scopus 로고    scopus 로고
    • A role for MEK kinase 1 in TGF-β/activin-induced epithelium movement and embryonic eyelid closure
    • Zhang, L. et al. A role for MEK kinase 1 in TGF-β/activin-induced epithelium movement and embryonic eyelid closure. EMBO J. 22, 4443-4454 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4443-4454
    • Zhang, L.1
  • 26
    • 0035461303 scopus 로고    scopus 로고
    • TGF-β-induced p38 activation is mediated by Rac1-regulated generation of reactive oxygen species in cultured human keratinocytes
    • Chiu, C. et al. TGF-β-induced p38 activation is mediated by Rac1-regulated generation of reactive oxygen species in cultured human keratinocytes. Int. J. Mol. Med. 8, 251-255 (2001).
    • (2001) Int. J. Mol. Med. , vol.8 , pp. 251-255
    • Chiu, C.1
  • 27
    • 2342436038 scopus 로고    scopus 로고
    • Smad7 is required for TGF-β-induced activation of the small GTPase Cdc42
    • Edlund, S., Landstrom, M., Heldin, C. H. & Aspenstrom, P. Smad7 is required for TGF-β-induced activation of the small GTPase Cdc42. J. Cell Sci. 117, 1835-1847 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1835-1847
    • Edlund, S.1    Landstrom, M.2    Heldin, C.H.3    Aspenstrom, P.4
  • 28
    • 0034906821 scopus 로고    scopus 로고
    • TGF-β-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation
    • Perlman, R., Schiemann, W. P., Brooks, M. W., Lodish, H. F. & Weinberg, R. A. TGF-β-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. Nature Cell Biol. 3, 708-714 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 708-714
    • Perlman, R.1    Schiemann, W.P.2    Brooks, M.W.3    Lodish, H.F.4    Weinberg, R.A.5
  • 29
    • 0242721599 scopus 로고    scopus 로고
    • Cell-type-specific activation of PAK2 by transforming growth factor-β independent of Smad2 and Smad3
    • Wilkes, M. C., Murphy, S. J., Garamszegi, N. & Leof, E. B. Cell-type-specific activation of PAK2 by transforming growth factor-β independent of Smad2 and Smad3. Mol. Cell Biol. 23, 8878-8889 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 8878-8889
    • Wilkes, M.C.1    Murphy, S.J.2    Garamszegi, N.3    Leof, E.B.4
  • 30
    • 0026612306 scopus 로고
    • Activation of p21 ras by transforming growth factor-β in epithelial cells
    • Mulder, K. M. & Morris, S. L. Activation of p21 ras by transforming growth factor-β in epithelial cells. J. Biol. Chem. 267, 5029-5031 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 5029-5031
    • Mulder, K.M.1    Morris, S.L.2
  • 31
    • 15444372825 scopus 로고    scopus 로고
    • Type I transforming growth factor-β receptor binds to and activates phosphatidylinositol 3-kinase
    • Yi, J. Y., Shin, I. & Arteaga, C. L. Type I transforming growth factor-β receptor binds to and activates phosphatidylinositol 3-kinase. J. Biol. Chem. 280, 10870-10876 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 10870-10876
    • Yi, J.Y.1    Shin, I.2    Arteaga, C.L.3
  • 32
    • 14844364701 scopus 로고    scopus 로고
    • Regulation of the polarity protein Par6 by TGFβ receptors controls epithelial cell plasticity
    • Ozdamar, B. et al. Regulation of the polarity protein Par6 by TGFβ receptors controls epithelial cell plasticity. Science 307, 1603-1609 (2005).
    • (2005) Science , vol.307 , pp. 1603-1609
    • Ozdamar, B.1
  • 33
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-β1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick, N. A. et al. Transforming growth factor-β1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell 12, 27-36 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1
  • 34
    • 0029940355 scopus 로고    scopus 로고
    • TAB1: An activator of the TAK1 MAPKKK in TGF-β signal transduction
    • Shibuya, H. et al. TAB1: an activator of the TAK1 MAPKKK in TGF-β signal transduction. Science 272, 1179-1182 (1996).
    • (1996) Science , vol.272 , pp. 1179-1182
    • Shibuya, H.1
  • 35
    • 0029551805 scopus 로고
    • Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction
    • Yamaguchi, K. et al. Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction. Science 270, 2008-2011 (1995).
    • (1995) Science , vol.270 , pp. 2008-2011
    • Yamaguchi, K.1
  • 36
    • 0034671578 scopus 로고    scopus 로고
    • TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G(1) arrest
    • Petritsch, C., Beug, H., Balmain, A. & Oft, M. TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G(1) arrest. Genes Dev. 14, 3093-3101 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 3093-3101
    • Petritsch, C.1    Beug, H.2    Balmain, A.3    Oft, M.4
  • 37
    • 30944444113 scopus 로고    scopus 로고
    • Alterations in components of the TGF-β superfamily signaling pathways in human cancer
    • Levy, L. & Hill, C. S. Alterations in components of the TGF-β superfamily signaling pathways in human cancer. Cytokine Growth Factor Rev. 17, 41-58 (2006).
    • (2006) Cytokine Growth Factor Rev. , vol.17 , pp. 41-58
    • Levy, L.1    Hill, C.S.2
  • 38
    • 0029066689 scopus 로고
    • Inactivation of the type II TGF-β receptor in colon cancer cells with microsatellite instability
    • Markowitz, S. et al. Inactivation of the type II TGF-β receptor in colon cancer cells with microsatellite instability. Science 268, 1336-1338 (1995). This is the first conclusive study that links inactivation of the type II TGFβ receptor to cancer.
    • (1995) Science , vol.268 , pp. 1336-1338
    • Markowitz, S.1
  • 39
    • 1242292420 scopus 로고    scopus 로고
    • Genomic instability and colon cancer
    • Grady, W. M. Genomic instability and colon cancer. Cancer Metastasis Rev. 23, 11-27 (2004).
    • (2004) Cancer Metastasis Rev. , vol.23 , pp. 11-27
    • Grady, W.M.1
  • 40
    • 0035153463 scopus 로고    scopus 로고
    • Role of transforming growth factor-β in cancer
    • Pasche, B. Role of transforming growth factor-β in cancer. J. Cell. Physiol. 186, 153-168 (2001).
    • (2001) J. Cell. Physiol. , vol.186 , pp. 153-168
    • Pasche, B.1
  • 41
    • 0035829653 scopus 로고    scopus 로고
    • Mutation frequency in coding and non-coding repeat sequences in mismatch repair deficient cells derived from normal human tissue
    • Bacon, A. L., Farrington, S. M. & Dunlop, M. G. Mutation frequency in coding and non-coding repeat sequences in mismatch repair deficient cells derived from normal human tissue. Oncogene 20, 7464-7471 (2001).
    • (2001) Oncogene , vol.20 , pp. 7464-7471
    • Bacon, A.L.1    Farrington, S.M.2    Dunlop, M.G.3
  • 42
    • 0034027480 scopus 로고    scopus 로고
    • Molecular mechanisms of inactivation of TGF-β receptors during carcinogenesis
    • Kim, S. J., Im, Y. H., Markowitz, S. D. & Bang, Y. J. Molecular mechanisms of inactivation of TGF-β receptors during carcinogenesis. Cytokine Growth Factor Rev. 11, 159-168 (2000).
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 159-168
    • Kim, S.J.1    Im, Y.H.2    Markowitz, S.D.3    Bang, Y.J.4
  • 43
    • 0000031048 scopus 로고    scopus 로고
    • Transcriptional repression of the transforming growth factor-β type I receptor gene by DNA methylation results in the development of TGF-β resistance in human gastric cancer
    • Kang, S. H. et al. Transcriptional repression of the transforming growth factor-β type I receptor gene by DNA methylation results in the development of TGF-β resistance in human gastric cancer. Oncogene 18, 7280-7286 (1999).
    • (1999) Oncogene , vol.18 , pp. 7280-7286
    • Kang, S.H.1
  • 45
    • 4644327904 scopus 로고    scopus 로고
    • Genetic models for transforming growth factor-β superfamily signaling in ovarian follicle development
    • Pangas, S. A. & Matzuk, M. M. Genetic models for transforming growth factor-β superfamily signaling in ovarian follicle development. Mol. Cell. Endocrinol. 225, 83-91 (2004).
    • (2004) Mol. Cell. Endocrinol. , vol.225 , pp. 83-91
    • Pangas, S.A.1    Matzuk, M.M.2
  • 46
    • 0026472124 scopus 로고
    • Expression of the neu proto-oncogene in the mammary epithelium of transgenic mice induces metastatic disease
    • Guy, C. T. et al. Expression of the neu proto-oncogene in the mammary epithelium of transgenic mice induces metastatic disease. Proc. Natl Acad. Sci. USA 89, 10578-10582 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10578-10582
    • Guy, C.T.1
  • 47
    • 0026587657 scopus 로고
    • Induction of mammary tumors by expression of polyomavirus middle T oncogene: A transgenic mouse model for metastatic disease
    • Guy, C. T., Cardiff, R. D. & Muller, W. J. Induction of mammary tumors by expression of polyomavirus middle T oncogene: a transgenic mouse model for metastatic disease. Mol. Cell Biol. 12, 954-961 (1992).
    • (1992) Mol. Cell Biol. , vol.12 , pp. 954-961
    • Guy, C.T.1    Cardiff, R.D.2    Muller, W.J.3
  • 48
    • 0025372023 scopus 로고
    • Development of mammary hyperplasia and neoplasia in MMTV-TGF-α transgenic mice
    • Matsui, Y., Halter, S. A., Holt, J. T., Hogan, B. L. & Coffey, R. J. Development of mammary hyperplasia and neoplasia in MMTV-TGF-α transgenic mice. Cell 61, 1147-1155 (1990).
    • (1990) Cell , vol.61 , pp. 1147-1155
    • Matsui, Y.1    Halter, S.A.2    Holt, J.T.3    Hogan, B.L.4    Coffey, R.J.5
  • 50
    • 30144433093 scopus 로고    scopus 로고
    • Generation of a functional mammary gland from a single stem cell
    • Shackleton, M. et al. Generation of a functional mammary gland from a single stem cell. Nature 439, 84-88 (2006). Although it is not directly related to TGFβ signalling in cancer, this high-impact paper outlines a new method whereby a single mammary stem cell can be isolated that is able to produce myoepithelium, ductal and alveolar epithelium. A single cell from this population was able to reconstitute all the epithelial and myoepithelial cell types necessary to reconstitute a functional mammary gland when transplanted into a cleared mammary fat pad.
    • (2006) Nature , vol.439 , pp. 84-88
    • Shackleton, M.1
  • 51
    • 0032910954 scopus 로고    scopus 로고
    • Overexpression of a kinase-deficient transforming growth factor-β type II receptor in mouse mammary stroma results in increased epithelial branching
    • Joseph, H., Gorska, A. E., Sohn, P., Moses, H. L. & Serra, R. Overexpression of a kinase-deficient transforming growth factor-β type II receptor in mouse mammary stroma results in increased epithelial branching. Mol. Biol. Cell 10, 1221-1234 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1221-1234
    • Joseph, H.1    Gorska, A.E.2    Sohn, P.3    Moses, H.L.4    Serra, R.5
  • 52
    • 0033858512 scopus 로고    scopus 로고
    • Transforming growth factor β3 induces cell death during the first stage of mammary gland involution
    • Nguyen, A. V. & Pollard, J. W. Transforming growth factor β3 induces cell death during the first stage of mammary gland involution. Development 127, 3107-3118 (2000).
    • (2000) Development , vol.127 , pp. 3107-3118
    • Nguyen, A.V.1    Pollard, J.W.2
  • 53
    • 0027136742 scopus 로고
    • Inhibition of mammary duct development but not alveolar outgrowth during pregnancy in transgenic mice expressing active TGF-β 1
    • Pierce, D. F., Jr. et al. Inhibition of mammary duct development but not alveolar outgrowth during pregnancy in transgenic mice expressing active TGF-β 1. Genes Dev. 7, 2308-2317 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 2308-2317
    • Pierce Jr., D.F.1
  • 54
    • 0035953393 scopus 로고    scopus 로고
    • Reducing mammary cancer risk through premature stem cell senescence
    • Boulanger, C. A. & Smith, G. H. Reducing mammary cancer risk through premature stem cell senescence. Oncogene 20, 2264-2272 (2001).
    • (2001) Oncogene , vol.20 , pp. 2264-2272
    • Boulanger, C.A.1    Smith, G.H.2
  • 55
    • 13244273440 scopus 로고    scopus 로고
    • Parity-induced mouse mammary epithelial cells are pluripotent, self-renewing and sensitive to TGF-β1 expression
    • Boulanger, C. A., Wagner, K. U. & Smith, G. H. Parity-induced mouse mammary epithelial cells are pluripotent, self-renewing and sensitive to TGF-β1 expression. Oncogene 24, 552-560 (2005).
    • (2005) Oncogene , vol.24 , pp. 552-560
    • Boulanger, C.A.1    Wagner, K.U.2    Smith, G.H.3
  • 56
    • 0027286692 scopus 로고
    • Targeting expression of a transforming growth factor β 1 transgene to the pregnant mammary gland inhibits alveolar development and lactation
    • Jhappan, C. et al. Targeting expression of a transforming growth factor β 1 transgene to the pregnant mammary gland inhibits alveolar development and lactation. EMBO J. 12, 1835-1845 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1835-1845
    • Jhappan, C.1
  • 57
    • 0028986768 scopus 로고
    • Ectopic TGF-β1 expression in the secretory mammary epithelium induces early senescence of the epithelial stem cell population
    • Kordon, E. C. et al. Ectopic TGF-β1 expression in the secretory mammary epithelium induces early senescence of the epithelial stem cell population. Dev. Biol. 168, 47-61 (1995).
    • (1995) Dev. Biol. , vol.168 , pp. 47-61
    • Kordon, E.C.1
  • 58
    • 0029010734 scopus 로고
    • Mammary tumor suppression by transforming growth factor-β1 transgene expression
    • Pierce, D. F., Jr. et al. Mammary tumor suppression by transforming growth factor-β1 transgene expression. Proc. Natl Acad. Sci. USA 92, 4254-4258 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4254-4258
    • Pierce Jr., D.F.1
  • 59
    • 0242552529 scopus 로고    scopus 로고
    • Increased malignancy of Neu-induced mammary tumors overexpressing active transforming growth factor β1
    • Muraoka, R. S. et al. Increased malignancy of Neu-induced mammary tumors overexpressing active transforming growth factor β1. Mol. Cell. Biol. 23, 8691-8703 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8691-8703
    • Muraoka, R.S.1
  • 60
    • 10844224603 scopus 로고    scopus 로고
    • Conditional overex press ion of active transforming growth factor β1 in vivo accelerates metastases of transgenic mammary tumors
    • Muraoka-Cook, R. S. et al. Conditional overex press ion of active transforming growth factor β1 in vivo accelerates metastases of transgenic mammary tumors. Cancer Res. 64, 9002-9011 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 9002-9011
    • Muraoka-Cook, R.S.1
  • 61
    • 0141537150 scopus 로고    scopus 로고
    • Transgenic mice expressing a dominant-negative mutant type II transforming growth factor-β receptor exhibit impaired mammary development and enhanced mammary tumor formation
    • Gorska, A. E. et al. Transgenic mice expressing a dominant-negative mutant type II transforming growth factor-β receptor exhibit impaired mammary development and enhanced mammary tumor formation. Am. J. Pathol. 163, 1539-1549 (2003).
    • (2003) Am. J. Pathol. , vol.163 , pp. 1539-1549
    • Gorska, A.E.1
  • 62
    • 0242594006 scopus 로고    scopus 로고
    • Expression of TGF-β type II receptor antisense RNA impairs TGF-β signaling in vitro and promotes mammary gland differentiation in vivo
    • Lenferink, A. E., Magoon, J., Pepin, M. C., Guimond, A. & O'Connor-McCourt, M. D. Expression of TGF-β type II receptor antisense RNA impairs TGF-β signaling in vitro and promotes mammary gland differentiation in vivo. Int. J. Cancer 107, 919-928 (2003).
    • (2003) Int. J. Cancer , vol.107 , pp. 919-928
    • Lenferink, A.E.1    Magoon, J.2    Pepin, M.C.3    Guimond, A.4    O'Connor-McCourt, M.D.5
  • 63
    • 0036086409 scopus 로고    scopus 로고
    • Blockade of TGF-β inhibits mammary tumor cell viability, migration, and metastases
    • Muraoka, R. S. et al. Blockade of TGF-β inhibits mammary tumor cell viability, migration, and metastases. J. Clin. Invest. 109, 1551-1559 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 1551-1559
    • Muraoka, R.S.1
  • 64
    • 16844373628 scopus 로고    scopus 로고
    • Effect of conditional knockout of the type II TGF-β receptor gene in mammary epithelia on mammary gland development and polyomavirus middle T antigen induced tumor formation and metastasis
    • Forrester, E. et al. Effect of conditional knockout of the type II TGF-β receptor gene in mammary epithelia on mammary gland development and polyomavirus middle T antigen induced tumor formation and metastasis. Cancer Res. 65, 2296-2302 (2005). Outlined for the first time the effect of complete conditional type II TGFβ receptor ablation in the context of mammary development and tumourigenesis.
    • (2005) Cancer Res. , vol.65 , pp. 2296-2302
    • Forrester, E.1
  • 65
    • 0036081239 scopus 로고    scopus 로고
    • Latent transforming growth factor-β activation in mammary gland: Regulation by ovarian hormones affects ductal and alveolar proliferation
    • Ewan, K. B. et al. Latent transforming growth factor-β activation in mammary gland: regulation by ovarian hormones affects ductal and alveolar proliferation. Am. J. Pathol. 160, 2081-2093 (2002).
    • (2002) Am. J. Pathol. , vol.160 , pp. 2081-2093
    • Ewan, K.B.1
  • 66
    • 25144457206 scopus 로고    scopus 로고
    • Proliferation of estrogen receptor-α-positive mammary epithelial cells is restrained by transforming growth factor-β1 in adult mice
    • Ewan, K. B. et al. Proliferation of estrogen receptor-α-positive mammary epithelial cells is restrained by transforming growth factor-β1 in adult mice. Am. J. Pathol. 167, 409-417 (2005).
    • (2005) Am. J. Pathol. , vol.167 , pp. 409-417
    • Ewan, K.B.1
  • 67
    • 0242285692 scopus 로고    scopus 로고
    • TGF-β switches from tumor suppressor to prometastatic factor in a model of breast cancer progression
    • Tang, B. et al. TGF-β switches from tumor suppressor to prometastatic factor in a model of breast cancer progression. J. Clin. Invest. 112, 1116-1124 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 1116-1124
    • Tang, B.1
  • 68
    • 30644461349 scopus 로고    scopus 로고
    • Activated type I TGFβ receptor kinase enhances the survival of mammary epithelial cells and accelerates tumor progression
    • Muraoka-Cook, R. S. et al. Activated type I TGFβ receptor kinase enhances the survival of mammary epithelial cells and accelerates tumor progression. Oncogene (2005).
    • (2005) Oncogene
    • Muraoka-Cook, R.S.1
  • 69
    • 0032547895 scopus 로고    scopus 로고
    • TGFβ signaling is necessary for carcinoma cell invasiveness and metastasis
    • Oft, M., Heider, K. H. & Beug, H. TGFβ signaling is necessary for carcinoma cell invasiveness and metastasis. Curr. Biol. 8, 1243-1252 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1243-1252
    • Oft, M.1    Heider, K.H.2    Beug, H.3
  • 70
    • 0037816160 scopus 로고    scopus 로고
    • Transforming growth factor β signaling impairs Neu-induced mammary tumorigenesis while promoting pulmonary metastasis
    • Siegel, P. M., Shu, W., Cardiff, R. D., Muller, W. J. & Massague, J. Transforming growth factor β signaling impairs Neu-induced mammary tumorigenesis while promoting pulmonary metastasis. Proc. Natl Acad. Sci. USA 100, 8430-8435 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8430-8435
    • Siegel, P.M.1    Shu, W.2    Cardiff, R.D.3    Muller, W.J.4    Massague, J.5
  • 71
    • 33644534795 scopus 로고    scopus 로고
    • The tumor suppressor Smad4 is required for transforming growth factor-β-induced epithelial to mesenchymal transition and bone metastasis of breast cancer cells
    • Deckers, M. et al. The tumor suppressor Smad4 is required for transforming growth factor-β-induced epithelial to mesenchymal transition and bone metastasis of breast cancer cells. Cancer Res. 66, 2202-2209 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 2202-2209
    • Deckers, M.1
  • 72
    • 0030598681 scopus 로고    scopus 로고
    • TGFβ1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice
    • Cui, W. et al. TGFβ1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice. Cell 86, 531-542 (1996).
    • (1996) Cell , vol.86 , pp. 531-542
    • Cui, W.1
  • 73
    • 0029802491 scopus 로고    scopus 로고
    • Altered epidermal cell growth control in vivo by inducible expression of transforming growth factor β 1 in the skin of transgenic mice
    • Fowlis, D. J., Cui, W., Johnson, S. A., Balmain, A. & Akhurst, R. J. Altered epidermal cell growth control in vivo by inducible expression of transforming growth factor β 1 in the skin of transgenic mice. Cell Growth Differ. 7, 679-687 (1996).
    • (1996) Cell Growth Differ. , vol.7 , pp. 679-687
    • Fowlis, D.J.1    Cui, W.2    Johnson, S.A.3    Balmain, A.4    Akhurst, R.J.5
  • 74
    • 0028986244 scopus 로고
    • Concerted action of TGF-β1 and its type II receptor in control of epidermal homeostasis in transgenic mice
    • Cui, W. et al. Concerted action of TGF-β1 and its type II receptor in control of epidermal homeostasis in transgenic mice. Genes Dev. 9, 945-955 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 945-955
    • Cui, W.1
  • 75
    • 0032500010 scopus 로고    scopus 로고
    • Expression of a dominant negative type II TGF-β receptor in mouse skin results in an increase in carcinoma incidence and an acceleration of carcinoma development
    • Amendt, C., Schirmacher, P., Weber, H. & Blessing, M. Expression of a dominant negative type II TGF-β receptor in mouse skin results in an increase in carcinoma incidence and an acceleration of carcinoma development. Oncogene 17, 25-34 (1998).
    • (1998) Oncogene , vol.17 , pp. 25-34
    • Amendt, C.1    Schirmacher, P.2    Weber, H.3    Blessing, M.4
  • 76
    • 0034721099 scopus 로고    scopus 로고
    • Aberrant cell cycle progression contributes to the early-stage accelerated carcinogenesis in transgenic epidermis expressing the dominant negative TGFβRII
    • Go, C. et al. Aberrant cell cycle progression contributes to the early-stage accelerated carcinogenesis in transgenic epidermis expressing the dominant negative TGFβRII. Oncogene 19, 3623-3631 (2000).
    • (2000) Oncogene , vol.19 , pp. 3623-3631
    • Go, C.1
  • 77
    • 0033564547 scopus 로고    scopus 로고
    • Blocking transforming growth factor-β signaling in transgenic epidermis accelerates chemical carcinogenesis: A mechanism associated with increased angiogenesis
    • Go, C., Li, P. & Wang, X. J. Blocking transforming growth factor-β signaling in transgenic epidermis accelerates chemical carcinogenesis: a mechanism associated with increased angiogenesis. Cancer Res. 59, 2861-2868 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 2861-2868
    • Go, C.1    Li, P.2    Wang, X.J.3
  • 78
    • 0033587687 scopus 로고    scopus 로고
    • Development of gene-switch transgenic mice that inducibly express transforming growth factor β1 in the epidermis
    • Wang, X. J., Liefer, K. M., Tsai, S., O'Malley, B. W. & Roop, D. R. Development of gene-switch transgenic mice that inducibly express transforming growth factor β1 in the epidermis. Proc. Natl Acad. Sci. USA 96, 8483-8488 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8483-8488
    • Wang, X.J.1    Liefer, K.M.2    Tsai, S.3    O'Malley, B.W.4    Roop, D.R.5
  • 79
    • 0035887461 scopus 로고    scopus 로고
    • Inducible expression of transforming growth factor β1 in papillomas causes rapid metastasis
    • Weeks, B. H., He, W., Olson, K. L. & Wang, X. J. Inducible expression of transforming growth factor β1 in papillomas causes rapid metastasis. Cancer Res. 61, 7435-7443 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 7435-7443
    • Weeks, B.H.1    He, W.2    Olson, K.L.3    Wang, X.J.4
  • 80
    • 22144490495 scopus 로고    scopus 로고
    • Distinct mechanisms of TGF-β1-mediated epithelial-to-mesenchymal transition and metastasis during skin carcinogenesis
    • Han, G. et al. Distinct mechanisms of TGF-β1-mediated epithelial-to-mesenchymal transition and metastasis during skin carcinogenesis. J. Clin. Invest. 115, 1714-1723 (2005). Showed the effect of increased TGFβ expression with the concurrent expression of a dominant-negative type II receptor in the skin epithelium during carcinogenesis. The data show that the expression of TGFβ with a reduction in the tumour-cell-autonomous response to this pathway promotes progression to metastasis.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1714-1723
    • Han, G.1
  • 81
    • 0030953639 scopus 로고    scopus 로고
    • Expression of a dominant-negative type II transforming growth factor-β (TGF-β) receptor in the epidermis of transgenic mice blocks TGF-β-mediated growth inhibition
    • Wang, X. J. et al. Expression of a dominant-negative type II transforming growth factor-β (TGF-β) receptor in the epidermis of transgenic mice blocks TGF-β-mediated growth inhibition. Proc. Natl Acad. Sci. USA 94, 2386-2391 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2386-2391
    • Wang, X.J.1
  • 82
    • 0842288323 scopus 로고    scopus 로고
    • TGF-β signaling in fibroblasts modulates the oncogenic potential of adjacent epithelia
    • Bhowmick, N. A. et al. TGF-β signaling in fibroblasts modulates the oncogenic potential of adjacent epithelia. Science 303, 848-851 (2004). Showed that TGFβ signalling in some fibroblast subpopulations can regulate the initiation of carcinoma in adjacent epithelia.
    • (2004) Science , vol.303 , pp. 848-851
    • Bhowmick, N.A.1
  • 83
    • 23744452875 scopus 로고    scopus 로고
    • Loss of TGF-β type II receptor in fibroblasts promotes mammary carcinoma growth and invasion through upregulation of TGF-α-, MSP- And HGF-mediated signaling networks
    • Cheng, N. et al. Loss of TGF-β type II receptor in fibroblasts promotes mammary carcinoma growth and invasion through upregulation of TGF-α-, MSP- and HGF-mediated signaling networks. Oncogene 24, 5053-5068 (2005). Showed that TGFβ signalling in fibroblasts can regulate tumour progression in adjacent epithelium through distinct molecular mechanisms.
    • (2005) Oncogene , vol.24 , pp. 5053-5068
    • Cheng, N.1
  • 84
    • 0035890799 scopus 로고    scopus 로고
    • Malignant transformation in a nontumorigenic human prostatic epithelial cell line
    • Hayward, S. W. et al. Malignant transformation in a nontumorigenic human prostatic epithelial cell line. Cancer Res. 61, 8135-8142 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 8135-8142
    • Hayward, S.W.1
  • 85
    • 0034161922 scopus 로고    scopus 로고
    • Irradiated mammary gland stroma promotes the expression of tumorigenic potential by unirradiated epithelial cells
    • Barcellos-Hoff, M. H. & Ravani, S. A. Irradiated mammary gland stroma promotes the expression of tumorigenic potential by unirradiated epithelial cells. Cancer Res. 60, 1254-1260 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 1254-1260
    • Barcellos-Hoff, M.H.1    Ravani, S.A.2
  • 86
    • 0036790977 scopus 로고    scopus 로고
    • Diversity, topographic differentiation, and positional memory in human fibroblasts
    • Chang, H. Y. et al. Diversity, topographic differentiation, and positional memory in human fibroblasts. Proc. Natl Acad. Sci. USA 99, 12877-12882 (2002). Showed that fibroblasts isolated from different parts of the body have distinct molecular profiles. The unique molecular identity of each fibroblast subpopulation was used to accurately identify the tissue from which it was derived.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12877-12882
    • Chang, H.Y.1
  • 87
    • 33745536920 scopus 로고    scopus 로고
    • TGF-β regulates differentially the proliferation of fetal and adult human skin fibroblasts via the activation of PKA and the autocrine action of FGF-2
    • Dec epub ahead of print
    • Giannouli, C. C. & Kletsas, D. TGF-β regulates differentially the proliferation of fetal and adult human skin fibroblasts via the activation of PKA and the autocrine action of FGF-2. Cell. Signal. 14 Dec 2005 [epub ahead of print].
    • (2005) Cell. Signal. , vol.14
    • Giannouli, C.C.1    Kletsas, D.2
  • 88
  • 89
    • 0032868805 scopus 로고    scopus 로고
    • Effects of TGF-β on the immune system: Implications for cancer immunotherapy
    • de Visser, K. E. & Kast, W. M. Effects of TGF-β on the immune system: implications for cancer immunotherapy. Leukemia 13, 1188-1199 (1999).
    • (1999) Leukemia , vol.13 , pp. 1188-1199
    • De Visser, K.E.1    Kast, W.M.2
  • 90
    • 0036372440 scopus 로고    scopus 로고
    • Transforming growth factor-β in T-cell biology
    • Gorelik, L. & Flavell, R. A. Transforming growth factor-β in T-cell biology. Nature Rev. Immunol. 2, 46-53 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 46-53
    • Gorelik, L.1    Flavell, R.A.2
  • 91
    • 3042703866 scopus 로고    scopus 로고
    • TGF-β: The perpetrator of immune suppression by regulatory T cells and suicidal T cells
    • Wahl, S. M., Swisher, J., McCartney-Francis, N. & Chen, W. TGF-β: the perpetrator of immune suppression by regulatory T cells and suicidal T cells. J. Leukoc. Biol. 76, 15-24 (2004).
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 15-24
    • Wahl, S.M.1    Swisher, J.2    McCartney-Francis, N.3    Chen, W.4
  • 92
    • 0141428794 scopus 로고    scopus 로고
    • Controlling the angiogenic switch: A balance between two distinct TGF-β receptor signaling pathways
    • Goumans, M. J., Lebrin, F. & Valdimarsdottir, G. Controlling the angiogenic switch: a balance between two distinct TGF-β receptor signaling pathways. Trends Cardiovasc. Med. 13, 301-307 (2003).
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 301-307
    • Goumans, M.J.1    Lebrin, F.2    Valdimarsdottir, G.3
  • 93
    • 12144258900 scopus 로고    scopus 로고
    • Dual role of transforming growth factor β in mammary tumorigenesis and metastatic progression
    • Muraoka-Cook, R. S., Dumont, N. & Arteaga, C. L. Dual role of transforming growth factor β in mammary tumorigenesis and metastatic progression. Clin. Cancer Res. 11, 937s-943s (2005).
    • (2005) Clin. Cancer Res. , vol.11
    • Muraoka-Cook, R.S.1    Dumont, N.2    Arteaga, C.L.3
  • 94
    • 0034131557 scopus 로고    scopus 로고
    • Abrogation of TGFβ signaling in T cells leads to spontaneous T cell differentiation and autoimmune disease
    • Gorelik, L. & Flavell, R. A. Abrogation of TGFβ signaling in T cells leads to spontaneous T cell differentiation and autoimmune disease. Immunity 12, 171-181 (2000).
    • (2000) Immunity , vol.12 , pp. 171-181
    • Gorelik, L.1    Flavell, R.A.2
  • 95
    • 0027531528 scopus 로고
    • Transforming growth factor-β1 null mutation in mice causes excessive inflammatory response and early death
    • Kulkarni, A. B. et al. Transforming growth factor-β1 null mutation in mice causes excessive inflammatory response and early death. Proc. Natl Acad. Sci. USA 90, 770-774 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 770-774
    • Kulkarni, A.B.1
  • 96
    • 0037100520 scopus 로고    scopus 로고
    • Induced disruption of the transforming growth factor-β type II receptor gene in mice causes a lethal inflammatory disorder that is transplantable
    • Leveen, P. et al. Induced disruption of the transforming growth factor-β type II receptor gene in mice causes a lethal inflammatory disorder that is transplantable. Blood 100, 560-568 (2002).
    • (2002) Blood , vol.100 , pp. 560-568
    • Leveen, P.1
  • 97
    • 0026799402 scopus 로고
    • Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease
    • Shull, M. M. et al. Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease. Nature 359, 693-699 (1992).
    • (1992) Nature , vol.359 , pp. 693-699
    • Shull, M.M.1
  • 98
    • 0037570729 scopus 로고    scopus 로고
    • Minimal effects on immune parameters following chronic anti-TGF-β monoclonal antibody administration to normal mice
    • Ruzek, M. C. et al. Minimal effects on immune parameters following chronic anti-TGF-β monoclonal antibody administration to normal mice. Immunopharmacol. Immunotoxicol. 25, 235-257 (2003).
    • (2003) Immunopharmacol. Immunotoxicol. , vol.25 , pp. 235-257
    • Ruzek, M.C.1
  • 99
    • 0036087521 scopus 로고    scopus 로고
    • Lifetime exposure to a soluble TGF-β antagonist protects mice against metastasis without adverse side effects
    • Yang, Y. A. et al. Lifetime exposure to a soluble TGF-β antagonist protects mice against metastasis without adverse side effects. J. Clin. Invest. 109, 1607-1615 (2002). Before this study it was not known if the systemic inhibition of TGFβ signalling would be a viable strategy for administration over a sustained duration in vivo. However, this report indicates that in mice, a sustained systemic inhibition of TGFβ does not result in any observed adverse effects.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1607-1615
    • Yang, Y.A.1
  • 100
    • 10444261212 scopus 로고    scopus 로고
    • Development of TGF-β signalling inhibitors for cancer therapy
    • Yingling, J. M., Blanchard, K. L. & Sawyer, J. S. Development of TGF-β signalling inhibitors for cancer therapy. Nature Rev. Drug Discov. 3, 1011-1022 (2004).
    • (2004) Nature Rev. Drug Discov. , vol.3 , pp. 1011-1022
    • Yingling, J.M.1    Blanchard, K.L.2    Sawyer, J.S.3
  • 101
    • 31144468294 scopus 로고    scopus 로고
    • + T regulatory cells suppress NK cell-mediated immunotherapy of cancer
    • + T regulatory cells suppress NK cell-mediated immunotherapy of cancer. J. Immunol. 176, 1582-1587 (2006).
    • (2006) J. Immunol. , vol.176 , pp. 1582-1587
    • Smyth, M.J.1
  • 103
    • 0025930443 scopus 로고
    • Expression of TGF-β2 in human glioblastoma: A role in resistance to immune rejection?
    • Fontana, A., Bodmer, S., Frei, K., Malipiero, U. & Siepl, C. Expression of TGF-β2 in human glioblastoma: a role in resistance to immune rejection? Ciba Found. Symp. 157, 232-238; discussion 238-241 (1991).
    • (1991) Ciba Found. Symp. , vol.157 , pp. 232-238
    • Fontana, A.1    Bodmer, S.2    Frei, K.3    Malipiero, U.4    Siepl, C.5
  • 104
    • 0034770605 scopus 로고    scopus 로고
    • Immune-mediated eradication of tumors through the blockade of transforming growth factor-β signaling in T cells
    • Gorelik, L. & Flavell, R. A. Immune-mediated eradication of tumors through the blockade of transforming growth factor-β signaling in T cells. Nature Med. 7, 1118-1122 (2001). Blockade of TGFβ signalling in T cells resulted in a marked resistance to cancer when mice were challenged with live tumour cells. The resistance was shown to be the result of an efficient eradication of tumour cells owing to a robust immune response after the attenuation of TGFβ signalling in T cells.
    • (2001) Nature Med. , vol.7 , pp. 1118-1122
    • Gorelik, L.1    Flavell, R.A.2
  • 105
    • 27644457376 scopus 로고    scopus 로고
    • TGF-β directly targets cytotoxic T cell functions during tumor evasion of immune surveillance
    • Thomas, D. A. & Massague, J. TGF-β directly targets cytotoxic T cell functions during tumor evasion of immune surveillance. Cancer Cell 8, 369-380 (2005).
    • (2005) Cancer Cell , vol.8 , pp. 369-380
    • Thomas, D.A.1    Massague, J.2
  • 106
    • 20144387943 scopus 로고    scopus 로고
    • + T cells: Eradication of autologous mouse prostate cancer
    • + T cells: eradication of autologous mouse prostate cancer. Cancer Res. 65, 1761-1769 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 1761-1769
    • Zhang, Q.1
  • 107
    • 20044375562 scopus 로고    scopus 로고
    • Kinetic characterization of novel pyrazole TGF-β receptor I kinase inhibitors and their blockade of the epithelial-mesenchymal transition
    • Peng, S. B. et al. Kinetic characterization of novel pyrazole TGF-β receptor I kinase inhibitors and their blockade of the epithelial-mesenchymal transition. Biochemistry 44, 2293-2304 (2005).
    • (2005) Biochemistry , vol.44 , pp. 2293-2304
    • Peng, S.B.1
  • 108
    • 29644443725 scopus 로고    scopus 로고
    • The ALK-5 inhibitor A-83-01 inhibits Smad signaling and epithelial-to-mesenchymal transition by transforming growth factor-β
    • Tojo, M. et al. The ALK-5 inhibitor A-83-01 inhibits Smad signaling and epithelial-to-mesenchymal transition by transforming growth factor-β. Cancer Sci. 96, 791-800 (2005).
    • (2005) Cancer Sci. , vol.96 , pp. 791-800
    • Tojo, M.1
  • 109
    • 2942536310 scopus 로고    scopus 로고
    • Selective inhibitors of type I receptor kinase block cellular transforming growth factor-β signaling
    • Ge, R. et al. Selective inhibitors of type I receptor kinase block cellular transforming growth factor-β signaling. Biochem. Pharmacol. 68, 41-50 (2004).
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 41-50
    • Ge, R.1
  • 110
    • 1342265719 scopus 로고    scopus 로고
    • SB-505124 is a selective inhibitor of transforming growth factor-β type I receptors ALK4, ALK5, and ALK7
    • DaCosta Byfield, S., Major, C., Laping, N. J. & Roberts, A. B. SB-505124 is a selective inhibitor of transforming growth factor-β type I receptors ALK4, ALK5, and ALK7. Mol. Pharmacol. 65, 744-752 (2004).
    • (2004) Mol. Pharmacol. , vol.65 , pp. 744-752
    • Dacosta Byfield, S.1    Major, C.2    Laping, N.J.3    Roberts, A.B.4
  • 111
    • 7444226411 scopus 로고    scopus 로고
    • SD-208, a novel transforming growth factor-β receptor I kinase inhibitor, inhibits growth and invasiveness and enhances immunogenicity of murine and human glioma cells in vitro and in vivo
    • Uhl, M. et al. SD-208, a novel transforming growth factor-β receptor I kinase inhibitor, inhibits growth and invasiveness and enhances immunogenicity of murine and human glioma cells in vitro and in vivo. Cancer Res. 64, 7954-7961 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 7954-7961
    • Uhl, M.1
  • 112
    • 0036085920 scopus 로고    scopus 로고
    • SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7
    • Inman, G. J. et al. SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol. Pharmacol. 62, 65-74 (2002).
    • (2002) Mol. Pharmacol. , vol.62 , pp. 65-74
    • Inman, G.J.1
  • 113
    • 23444434936 scopus 로고    scopus 로고
    • Gene expression profiling of cancer progression reveals intrinsic regulation of transforming growth factor-β signaling in ErbB2/Neu-induced tumors from transgenic mice
    • Landis, M. D., Seachrist, D. D., Montanez-Wiscovich, M. E., Danielpour, D. & Keri, R. A. Gene expression profiling of cancer progression reveals intrinsic regulation of transforming growth factor-β signaling in ErbB2/Neu-induced tumors from transgenic mice. Oncogene 24, 5173-5190 (2005).
    • (2005) Oncogene , vol.24 , pp. 5173-5190
    • Landis, M.D.1    Seachrist, D.D.2    Montanez-Wiscovich, M.E.3    Danielpour, D.4    Keri, R.A.5
  • 114
    • 1842847888 scopus 로고    scopus 로고
    • Clinical significance of the expression of activin a in esophageal carcinoma
    • Yoshinaga, K. et al. Clinical significance of the expression of activin A in esophageal carcinoma. Int. J. Oncol. 22, 75-80 (2003).
    • (2003) Int. J. Oncol. , vol.22 , pp. 75-80
    • Yoshinaga, K.1
  • 115
    • 3442894138 scopus 로고    scopus 로고
    • Targeting endogenous transforming growth factor-β receptor signaling in SMAD4-deficient human pancreatic carcinoma cells inhibits their invasive phenotype1
    • Subramanian, G. et al. Targeting endogenous transforming growth factor-β receptor signaling in SMAD4-deficient human pancreatic carcinoma cells inhibits their invasive phenotype1. Cancer Res. 64, 5200-5211 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 5200-5211
    • Subramanian, G.1
  • 116
    • 0033623532 scopus 로고    scopus 로고
    • Integrin α1β1 and transforming growth factor-β1 play distinct roles in alport glomerular pathogenesis and serve as dual targets for metabolic therapy
    • Cosgrove, D. et al. Integrin α1β1 and transforming growth factor-β1 play distinct roles in alport glomerular pathogenesis and serve as dual targets for metabolic therapy. Am. J. Pathol. 157, 1649-1659 (2000).
    • (2000) Am. J. Pathol. , vol.157 , pp. 1649-1659
    • Cosgrove, D.1
  • 117
    • 0033215194 scopus 로고    scopus 로고
    • A soluble transforming growth factor β type III receptor suppresses tumorigenicity and metastasis of human breast cancer MDA-MB-231 cells
    • Bandyopadhyay, A. et al. A soluble transforming growth factor β type III receptor suppresses tumorigenicity and metastasis of human breast cancer MDA-MB-231 cells. Cancer Res. 59, 5041-5046 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 5041-5046
    • Bandyopadhyay, A.1
  • 118
    • 0037102289 scopus 로고    scopus 로고
    • Antitumor activity of a recombinant soluble betaglycan in human breast cancer xenograft
    • Bandyopadhyay, A. et al. Antitumor activity of a recombinant soluble betaglycan in human breast cancer xenograft. Cancer Res. 62, 4690-4695 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 4690-4695
    • Bandyopadhyay, A.1
  • 119
    • 0024553650 scopus 로고
    • Monoclonal antibodies recognizing transforming growth factor-β. Bioactivity neutralization and transforming growth factor-β 2 affinity purification
    • Dasch, J. R., Pace, D. R., Waegell, W., Inenaga, D. & Ellingsworth, L. Monoclonal antibodies recognizing transforming growth factor-β. Bioactivity neutralization and transforming growth factor-β 2 affinity purification. J. Immunol. 142, 1536-1541 (1989).
    • (1989) J. Immunol. , vol.142 , pp. 1536-1541
    • Dasch, J.R.1    Pace, D.R.2    Waegell, W.3    Inenaga, D.4    Ellingsworth, L.5
  • 120
    • 0032821129 scopus 로고    scopus 로고
    • Human anti-transforming growth factor-β2 antibody: A new glaucoma anti-scarring agent
    • Cordeiro, M. F., Gay, J. A. & Khaw, P. T. Human anti-transforming growth factor-β2 antibody: a new glaucoma anti-scarring agent. Invest. Ophthalmol. Vis. Sci. 40, 2225-2234 (1999).
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2225-2234
    • Cordeiro, M.F.1    Gay, J.A.2    Khaw, P.T.3
  • 121
    • 0032867293 scopus 로고    scopus 로고
    • A fully human antibody neutralising biologically active human TGFβ2 for use in therapy
    • Thompson, J. E. et al. A fully human antibody neutralising biologically active human TGFβ2 for use in therapy. J. Immunol. Methods 227, 17-29 (1999).
    • (1999) J. Immunol. Methods , vol.227 , pp. 17-29
    • Thompson, J.E.1
  • 122
    • 0025179010 scopus 로고
    • The autocrine production of transforming growth factor-β1 during lymphocyte activation. A study with a monoclonal antibody-based ELISA
    • Lucas, C. et al. The autocrine production of transforming growth factor-β1 during lymphocyte activation. A study with a monoclonal antibody-based ELISA. J. Immunol. 145, 1415-1422 (1990).
    • (1990) J. Immunol. , vol.145 , pp. 1415-1422
    • Lucas, C.1
  • 123
    • 0027569092 scopus 로고
    • Transforming growth factor β1 can induce estrogen-independent tumorigenicity of human breast cancer cells in athymic mice
    • Arteaga, C. L., Carty-Dugger, T., Moses, H. L., Hurd, S. D. & Pietenpol, J. A. Transforming growth factor β1 can induce estrogen-independent tumorigenicity of human breast cancer cells in athymic mice. Cell Growth Differ. 4, 193-201 (1993).
    • (1993) Cell Growth Differ. , vol.4 , pp. 193-201
    • Arteaga, C.L.1    Carty-Dugger, T.2    Moses, H.L.3    Hurd, S.D.4    Pietenpol, J.A.5
  • 124
    • 0027793115 scopus 로고
    • Evidence for a positive role of transforming growth factor-β in human breast cancer cell tumorigenesis
    • Arteaga, C. L., Dugger, T. C., Winnier, A. R. & Forbes, J. T. Evidence for a positive role of transforming growth factor-β in human breast cancer cell tumorigenesis. J. Cell. Biochem. Suppl. 17G, 187-193 (1993).
    • (1993) J. Cell. Biochem. Suppl. , vol.17 , pp. 187-193
    • Arteaga, C.L.1    Dugger, T.C.2    Winnier, A.R.3    Forbes, J.T.4
  • 125
    • 0027137485 scopus 로고
    • Anti-transforming growth factor (TGF)-β antibodies inhibit breast cancer cell tumorigenicity and increase mouse spleen natural killer cell activity. Implications for a possible role of tumor cell/host TGF-β interactions in human breast cancer progression
    • Arteaga, C. L. et al. Anti-transforming growth factor (TGF)-β antibodies inhibit breast cancer cell tumorigenicity and increase mouse spleen natural killer cell activity. Implications for a possible role of tumor cell/host TGF-β interactions in human breast cancer progression. J. Clin. Invest. 92, 2569-2576 (1993).
    • (1993) J. Clin. Invest. , vol.92 , pp. 2569-2576
    • Arteaga, C.L.1
  • 126
    • 0029865486 scopus 로고    scopus 로고
    • Eradication of established intracranial rat gliomas by transforming growth factor-β antisense gene therapy
    • Fakhrai, H. et al. Eradication of established intracranial rat gliomas by transforming growth factor-β antisense gene therapy. Proc. Natl Acad. Sci. USA 93, 2909-2914 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2909-2914
    • Fakhrai, H.1
  • 127
    • 0031698247 scopus 로고    scopus 로고
    • Prolonged survival of rats with intracranial C6 gliomas by treatment with TGF-β antisense gene
    • Liau, L. M., Fakhrai, H. & Black, K. L. Prolonged survival of rats with intracranial C6 gliomas by treatment with TGF-β antisense gene. Neurol. Res. 20, 742-747 (1998).
    • (1998) Neurol. Res. , vol.20 , pp. 742-747
    • Liau, L.M.1    Fakhrai, H.2    Black, K.L.3
  • 128
    • 33745515298 scopus 로고    scopus 로고
    • Targeted tumor therapy with the TGF-β2 antisense compound AP 12009
    • Schlingensiepen, K. H. et al. Targeted tumor therapy with the TGF-β2 antisense compound AP 12009. Cytokine Growth Factor Rev. 17, 729-139 (2005).
    • (2005) Cytokine Growth Factor Rev. , vol.17 , pp. 729-1139
    • Schlingensiepen, K.H.1
  • 129
    • 22044456529 scopus 로고    scopus 로고
    • Intracerebral and intrathecal infusion of the TGF-β2-specific antisense phosphorothioate oligonucleotide AP 12009 in rabbits and primates: Toxicology and safety
    • Schlingensiepen, R. et al. Intracerebral and intrathecal infusion of the TGF-β2-specific antisense phosphorothioate oligonucleotide AP 12009 in rabbits and primates: toxicology and safety. Oligonucleotides 15, 94-104 (2005).
    • (2005) Oligonucleotides , vol.15 , pp. 94-104
    • Schlingensiepen, R.1
  • 131
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein, B. & Kinzler, K. W. Cancer genes and the pathways they control. Nature Med. 10, 789-799 (2004).
    • (2004) Nature Med. , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 132
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D. & Weinberg, R. A. The hallmarks of cancer. Cell 100, 57-70 (2000).
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 133
    • 28944432805 scopus 로고    scopus 로고
    • Selective evolution of stromal mesenchyme with p53 loss in response to epithelial tumorigenesis
    • Hill, R., Song, Y., Cardiff, R. D. & Van Dyke, T. Selective evolution of stromal mesenchyme with p53 loss in response to epithelial tumorigenesis. Cell 123, 1001-1011 (2005).
    • (2005) Cell , vol.123 , pp. 1001-1011
    • Hill, R.1    Song, Y.2    Cardiff, R.D.3    Van Dyke, T.4
  • 134
    • 14844293126 scopus 로고    scopus 로고
    • Activin receptor-like kinase 2 and Smad6 regulate epithelial-mesenchymal transformation during cardiac valve formation
    • Desgrosellier, J. S., Mundell, N. A., McDonnell, M. A., Moses, H. L. & Barnett, J. V. Activin receptor-like kinase 2 and Smad6 regulate epithelial-mesenchymal transformation during cardiac valve formation. Dev. Biol. 280, 201-210 (2005).
    • (2005) Dev. Biol. , vol.280 , pp. 201-210
    • Desgrosellier, J.S.1    Mundell, N.A.2    McDonnell, M.A.3    Moses, H.L.4    Barnett, J.V.5
  • 135
    • 0034213609 scopus 로고    scopus 로고
    • Activin receptor-like kinase 2 can mediate atrioventricular cushion transformation
    • Lai, Y. T. et al. Activin receptor-like kinase 2 can mediate atrioventricular cushion transformation. Dev. Biol. 222, 1-11 (2000).
    • (2000) Dev. Biol. , vol.222 , pp. 1-11
    • Lai, Y.T.1
  • 136
    • 0028603343 scopus 로고
    • TGF-β induced transdifferentiation of mammary epithelial cells to mesenchymal cells: Involvement of type I receptors
    • Miettinen, P. J., Ebner, R., Lopez, A. R. & Derynck, R. TGF-β induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors. J. Cell Biol. 127, 2021-2036 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 2021-2036
    • Miettinen, P.J.1    Ebner, R.2    Lopez, A.R.3    Derynck, R.4
  • 137
    • 0025873571 scopus 로고
    • Transforming growth factor-β induces human T lymphocyte migration in vitro
    • Adams, D. H. et al. Transforming growth factor-β induces human T lymphocyte migration in vitro. J. Immunol. 147, 609-6012 (1991).
    • (1991) J. Immunol. , vol.147 , pp. 609-6012
    • Adams, D.H.1
  • 138
    • 17844402285 scopus 로고    scopus 로고
    • TGF-β1 attenuates the acquisition and expression of effector function by tumor antigen-specific human memory CD8 T cells
    • Ahmadzadeh, M. & Rosenberg, S. A. TGF-β1 attenuates the acquisition and expression of effector function by tumor antigen-specific human memory CD8 T cells. J. Immunol. 174, 5215-5223 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 5215-5223
    • Ahmadzadeh, M.1    Rosenberg, S.A.2
  • 139
    • 0027248910 scopus 로고
    • Modulation of macrophage function by transforming growth factor β, interleukin-4, and interleukin-10
    • Bogdan, C. & Nathan, C. Modulation of macrophage function by transforming growth factor β, interleukin-4, and interleukin-10. Ann. NY Acad. Sci. 685, 713-739 (1993).
    • (1993) Ann. NY Acad. Sci. , vol.685 , pp. 713-739
    • Bogdan, C.1    Nathan, C.2
  • 140
    • 0023946378 scopus 로고
    • Transforming growth factor-β is a potent immunosuppressive agent that inhibits IL-1-dependent lymphocyte proliferation
    • Wahl, S. M. et al. Transforming growth factor-β is a potent immunosuppressive agent that inhibits IL-1-dependent lymphocyte proliferation. J. Immunol. 140, 3026-3032 (1988).
    • (1988) J. Immunol. , vol.140 , pp. 3026-3032
    • Wahl, S.M.1
  • 141
    • 0026793418 scopus 로고
    • TGF-β inhibits proliferation of and promotes differentiation of human promonocytic leukemia cells
    • Bombara, C. & Ignotz, R. A. TGF-β inhibits proliferation of and promotes differentiation of human promonocytic leukemia cells. J. Cell. Physiol. 153, 30-37 (1992).
    • (1992) J. Cell. Physiol. , vol.153 , pp. 30-37
    • Bombara, C.1    Ignotz, R.A.2
  • 142
    • 0031204379 scopus 로고    scopus 로고
    • Identification of an inhibitor targeting macrophage production of monocyte chemoattractant protein-1 as TGF-β 1
    • Kitamura, M. Identification of an inhibitor targeting macrophage production of monocyte chemoattractant protein-1 as TGF-β 1. J. Immunol. 159, 1404-1411 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 1404-1411
    • Kitamura, M.1
  • 143
    • 12144289322 scopus 로고    scopus 로고
    • Essential role for Smad3 in regulating MCP-1 expression and vascular inflammation
    • Feinberg, M. W. et al. Essential role for Smad3 in regulating MCP-1 expression and vascular inflammation. Circ. Res. 94, 601-608 (2004).
    • (2004) Circ. Res. , vol.94 , pp. 601-608
    • Feinberg, M.W.1
  • 144
    • 0032519925 scopus 로고    scopus 로고
    • Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-β, PGE2, and PAF
    • Fadok, V. A. et al. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-β, PGE2, and PAF. J. Clin. Invest. 101, 890-898 (1998).
    • (1998) J. Clin. Invest. , vol.101 , pp. 890-898
    • Fadok, V.A.1
  • 145
    • 0033485401 scopus 로고    scopus 로고
    • Transcriptional and translational regulation of inflammatory mediator production by endogenous TGF-β in macrophages that have ingested apoptotic cells
    • McDonald, P. P., Fadok, V. A., Bratton, D. & Henson, P. M. Transcriptional and translational regulation of inflammatory mediator production by endogenous TGF-β in macrophages that have ingested apoptotic cells. J. Immunol. 163, 6164-6172 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 6164-6172
    • McDonald, P.P.1    Fadok, V.A.2    Bratton, D.3    Henson, P.M.4
  • 146
    • 0037177841 scopus 로고    scopus 로고
    • Cross-talk between ERK and p38 MAPK mediates selective suppression of proinflammatory cytokines by transforming growth factor-β
    • Xiao, Y. Q. et al. Cross-talk between ERK and p38 MAPK mediates selective suppression of proinflammatory cytokines by transforming growth factor-β. J. Biol. Chem. 277, 14884-14893 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 14884-14893
    • Xiao, Y.Q.1
  • 147
    • 0035966002 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in ligand-independent sequestration of CXCR4 in human primary monocytes-macrophages
    • Wang, J. et al. Role of tyrosine phosphorylation in ligand-independent sequestration of CXCR4 in human primary monocytes-macrophages. J. Biol. Chem. 276, 49236-49243 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 49236-49243
    • Wang, J.1
  • 148
    • 0036006717 scopus 로고    scopus 로고
    • TGF-β1 enhances SDF-1α-induced chemotaxis and homing of naive T cells by up-regulating CXCR4 expression and downstream cytoskeletal effector molecules
    • Franitza, S. et al. TGF-β1 enhances SDF-1α-induced chemotaxis and homing of naive T cells by up-regulating CXCR4 expression and downstream cytoskeletal effector molecules. Eur. J. Immunol. 32, 193-202 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 193-202
    • Franitza, S.1
  • 149
    • 18844428327 scopus 로고    scopus 로고
    • Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion
    • Orimo, A. et al. Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion. Cell 121, 335-348 (2005).
    • (2005) Cell , vol.121 , pp. 335-348
    • Orimo, A.1
  • 150
    • 0027500836 scopus 로고
    • Transforming growth factor β1 (TGF-β1) controls expression of major histocompatibility genes in the postnatal mouse: Aberrant histocompatibility antigen expression in the pathogenesis of the TGF-β1 null mouse phenotype
    • Geiser, A. G. et al. Transforming growth factor β1 (TGF-β1) controls expression of major histocompatibility genes in the postnatal mouse: aberrant histocompatibility antigen expression in the pathogenesis of the TGF-β1 null mouse phenotype. Proc. Natl Acad. Sci. USA 90, 9944-9948 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9944-9948
    • Geiser, A.G.1
  • 151
    • 0031093495 scopus 로고    scopus 로고
    • TGF-β suppresses IFN-γ induction of class II MHC gene expression by inhibiting class II transactivator messenger RNA expression
    • Lee, Y. J. et al. TGF-β suppresses IFN-γ induction of class II MHC gene expression by inhibiting class II transactivator messenger RNA expression. J. Immunol. 158, 2065-2075 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 2065-2075
    • Lee, Y.J.1
  • 152
    • 0026656952 scopus 로고
    • Transforming growth factor-β 1 differentially regulates proliferation and MHC class-II antigen expression in forebrain and brainstem astrocyte primary cultures
    • Johns, L. D. et al. Transforming growth factor-β 1 differentially regulates proliferation and MHC class-II antigen expression in forebrain and brainstem astrocyte primary cultures. Brain Res. 585, 229-236 (1992).
    • (1992) Brain Res. , vol.585 , pp. 229-236
    • Johns, L.D.1
  • 153
    • 0028971393 scopus 로고
    • Transforming growth factor-β down-regulates major histocompatibility complex class I antigen expression and increases the susceptibility of uveal melanoma cells to natural killer cell-mediated cytolysis
    • Ma, D. & Niederkorn, J. Y. Transforming growth factor-β down-regulates major histocompatibility complex class I antigen expression and increases the susceptibility of uveal melanoma cells to natural killer cell-mediated cytolysis. Immunology 86, 263-269 (1995).
    • (1995) Immunology , vol.86 , pp. 263-269
    • Ma, D.1    Niederkorn, J.Y.2
  • 154
    • 0043065313 scopus 로고    scopus 로고
    • Expression of a soluble transforming growth factor-β (TGFβ) receptor reduces tumorigenicity by regulating natural killer (NK) cell activity against 9L gliosarcoma in vivo
    • Witham, T. F. et al. Expression of a soluble transforming growth factor-β (TGFβ) receptor reduces tumorigenicity by regulating natural killer (NK) cell activity against 9L gliosarcoma in vivo. J. Neurooncol. 64, 63-69 (2003).
    • (2003) J. Neurooncol. , vol.64 , pp. 63-69
    • Witham, T.F.1
  • 155
    • 0025953719 scopus 로고
    • Transforming growth factor β1, a potent chemoattractant for human neutrophils, bypasses classic signal-transduction pathways
    • Reibman, J. et al. Transforming growth factor β1, a potent chemoattractant for human neutrophils, bypasses classic signal-transduction pathways. Proc. Natl Acad. Sci. USA 88, 6805-6809 ( 1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6805-6809
    • Reibman, J.1
  • 156
    • 0032573581 scopus 로고    scopus 로고
    • Regulation of the proinflammatory effects of Fas ligand (CD95L)
    • Chen, J. J., Sun, Y. & Nabel, G. J. Regulation of the proinflammatory effects of Fas ligand (CD95L). Science 282, 1714-1717 (1998).
    • (1998) Science , vol.282 , pp. 1714-1717
    • Chen, J.J.1    Sun, Y.2    Nabel, G.J.3
  • 157
    • 10544232277 scopus 로고    scopus 로고
    • Melanoma cell expression of Fas(Apo-1/CD95) ligand: Implications for tumor immune escape
    • Hahne, M. et al. Melanoma cell expression of Fas(Apo-1/CD95) ligand: implications for tumor immune escape. Science 274, 1363-1366 (1996).
    • (1996) Science , vol.274 , pp. 1363-1366
    • Hahne, M.1


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