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Volumn 181, Issue 6, 2012, Pages 2202-2216

TGF-β Signaling, activated stromal fibroblasts, and cysteine cathepsins B and L drive the invasive growth of human melanoma cells

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ADAM12 PROTEIN; AE BINDING PROTEIN 1; ANTINEOPLASTIC AGENT; BB 3103; BINDING PROTEIN; CATHEPSIN B; CATHEPSIN L; CATHEPSIN L INHIBITOR; COMPLEMENT FACTOR I; CYSTEINE PROTEINASE INHIBITOR; GELATINASE B; ILOMASTAT; INTERSTITIAL COLLAGENASE; MARIMASTAT; MATRIX METALLOPROTEINASE INHIBITOR; MEMBRANE METALLOENDOPEPTIDASE; MESSENGER RNA; N (3 PROPYLCARBAMOYLOXIRANE 2 CARBONYL)ISOLEUCYLPROLINE; SEPRASE; TISSUE PLASMINOGEN ACTIVATOR; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; UROKINASE;

EID: 84869193514     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2012.08.027     Document Type: Article
Times cited : (67)

References (92)
  • 2
    • 8144228952 scopus 로고    scopus 로고
    • Friends or foes: Bipolar effects of the tumour stroma in cancer
    • M.M. Mueller, N.E. Fusenig Friends or foes: bipolar effects of the tumour stroma in cancer Nat Rev Cancer 4 2004 839 849
    • (2004) Nat Rev Cancer , vol.4 , pp. 839-849
    • Mueller, M.M.1    Fusenig, N.E.2
  • 3
    • 33645739790 scopus 로고    scopus 로고
    • Tumor stroma and regulation of cancer development
    • T.D. Tlsty, L.M. Coussens Tumor stroma and regulation of cancer development Annu Rev Pathol 1 2006 119 150
    • (2006) Annu Rev Pathol , vol.1 , pp. 119-150
    • Tlsty, T.D.1    Coussens, L.M.2
  • 4
    • 58149345546 scopus 로고    scopus 로고
    • Co-evolution of tumor cells and their microenvironment
    • K. Polyak, I. Haviv, I.G. Campbell Co-evolution of tumor cells and their microenvironment Trends Genet 25 2009 30 38
    • (2009) Trends Genet , vol.25 , pp. 30-38
    • Polyak, K.1    Haviv, I.2    Campbell, I.G.3
  • 5
    • 9244227134 scopus 로고    scopus 로고
    • Stromal fibroblasts in cancer initiation and progression
    • N.A. Bhowmick, E.G. Neilson, H.L. Moses Stromal fibroblasts in cancer initiation and progression Nature 432 2004 332 337
    • (2004) Nature , vol.432 , pp. 332-337
    • Bhowmick, N.A.1    Neilson, E.G.2    Moses, H.L.3
  • 6
    • 33747859659 scopus 로고    scopus 로고
    • Stromal fibroblasts in cancer: A novel tumor-promoting cell type
    • A. Orimo, R.A. Weinberg Stromal fibroblasts in cancer: a novel tumor-promoting cell type Cell Cycle 5 2006 1597 1601
    • (2006) Cell Cycle , vol.5 , pp. 1597-1601
    • Orimo, A.1    Weinberg, R.A.2
  • 13
    • 84855460517 scopus 로고    scopus 로고
    • BRAF inhibitors for the treatment of metastatic melanoma: Clinical trials and mechanisms of resistance
    • A.M. Alcala, K.T. Flaherty BRAF inhibitors for the treatment of metastatic melanoma: clinical trials and mechanisms of resistance Clin Cancer Res 18 2012 33 39
    • (2012) Clin Cancer Res , vol.18 , pp. 33-39
    • Alcala, A.M.1    Flaherty, K.T.2
  • 15
    • 35048812952 scopus 로고    scopus 로고
    • Urinary-type plasminogen activator (uPA) and its receptor (uPAR) in squamous cell carcinoma of the oral cavity
    • Z. Shi, M.S. Stack Urinary-type plasminogen activator (uPA) and its receptor (uPAR) in squamous cell carcinoma of the oral cavity Biochem J 407 2007 153 159
    • (2007) Biochem J , vol.407 , pp. 153-159
    • Shi, Z.1    Stack, M.S.2
  • 16
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • K. Kessenbrock, V. Plaks, Z. Werb Matrix metalloproteinases: regulators of the tumor microenvironment Cell 141 2010 52 67
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 17
    • 79953163995 scopus 로고    scopus 로고
    • Proteolytic networks in cancer
    • S.D. Mason, J.A. Joyce Proteolytic networks in cancer Trends Cell Biol 21 2011 228 237
    • (2011) Trends Cell Biol , vol.21 , pp. 228-237
    • Mason, S.D.1    Joyce, J.A.2
  • 18
    • 2342551977 scopus 로고    scopus 로고
    • Cysteine cathepsins (proteases): On the main stage of cancer
    • V. Turk, J. Kos, B. Turk Cysteine cathepsins (proteases): on the main stage of cancer Cancer Cell 5 2004 409 410
    • (2004) Cancer Cell , vol.5 , pp. 409-410
    • Turk, V.1    Kos, J.2    Turk, B.3
  • 19
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • M.M. Mohamed, B.F. Sloane Cysteine cathepsins: multifunctional enzymes in cancer Nat Rev Cancer 6 2006 764 775
    • (2006) Nat Rev Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 20
    • 78651291105 scopus 로고    scopus 로고
    • Proteases in cutaneous malignant melanoma: Relevance as biomarker and therapeutic target
    • E. Frohlich Proteases in cutaneous malignant melanoma: relevance as biomarker and therapeutic target Cell Mol Life Sci 67 2010 3947 3960
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3947-3960
    • Frohlich, E.1
  • 21
    • 0001278782 scopus 로고    scopus 로고
    • The Wistar (WM) melanoma cell lines
    • J.Ma.B. Palsson, Kluwer Academic Publishers London
    • M. Hsu, D.E. Elder, M. Herlyn The Wistar (WM) melanoma cell lines J.Ma.B. Palsson, Human Cell Culture 1999 Kluwer Academic Publishers London 259 274
    • (1999) Human Cell Culture , pp. 259-274
    • Hsu, M.1    Elder, D.E.2    Herlyn, M.3
  • 23
    • 22244454745 scopus 로고    scopus 로고
    • Differential regulation of noxa in normal melanocytes and melanoma cells by proteasome inhibition: Therapeutic implications
    • Y. Fernandez, M. Verhaegen, T.P. Miller, J.L. Rush, P. Steiner, A.W. Opipari Jr, S.W. Lowe, M.S. Soengas Differential regulation of noxa in normal melanocytes and melanoma cells by proteasome inhibition: therapeutic implications Cancer Res 65 2005 6294 6304
    • (2005) Cancer Res , vol.65 , pp. 6294-6304
    • Fernandez, Y.1    Verhaegen, M.2    Miller, T.P.3    Rush, J.L.4    Steiner, P.5    Opipari, Jr.A.W.6    Lowe, S.W.7    Soengas, M.S.8
  • 25
    • 10844291804 scopus 로고    scopus 로고
    • Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts
    • K. Ravanko, K. Jarvinen, J. Helin, N. Kalkkinen, E. Holtta Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts Cancer Res 64 2004 8831 8838
    • (2004) Cancer Res , vol.64 , pp. 8831-8838
    • Ravanko, K.1    Jarvinen, K.2    Helin, J.3    Kalkkinen, N.4    Holtta, E.5
  • 27
    • 79751525323 scopus 로고    scopus 로고
    • Chaotic neovascularization induced by aggressive fibrosarcoma cells overexpressing S-adenosylmethionine decarboxylase
    • A. Paasinen-Sohns, E. Kaariainen, M. Yin, K. Jarvinen, P. Nummela, E. Holtta Chaotic neovascularization induced by aggressive fibrosarcoma cells overexpressing S-adenosylmethionine decarboxylase Int J Biochem Cell Biol 43 2011 441 454
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 441-454
    • Paasinen-Sohns, A.1    Kaariainen, E.2    Yin, M.3    Jarvinen, K.4    Nummela, P.5    Holtta, E.6
  • 28
    • 0842320996 scopus 로고    scopus 로고
    • Cooperation of the ErbB2 receptor and transforming growth factor beta in induction of migration and invasion in mammary epithelial cells
    • S.E. Seton-Rogers, Y. Lu, L.M. Hines, M. Koundinya, J. LaBaer, S.K. Muthuswamy, J.S. Brugge Cooperation of the ErbB2 receptor and transforming growth factor beta in induction of migration and invasion in mammary epithelial cells Proc Natl Acad Sci U S A 101 2004 1257 1262
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1257-1262
    • Seton-Rogers, S.E.1    Lu, Y.2    Hines, L.M.3    Koundinya, M.4    Labaer, J.5    Muthuswamy, S.K.6    Brugge, J.S.7
  • 29
    • 33750324597 scopus 로고    scopus 로고
    • HER2/Neu (ErbB2) signaling to Rac1-Pak1 is temporally and spatially modulated by transforming growth factor beta
    • S.E. Wang, I. Shin, F.Y. Wu, D.B. Friedman, C.L. Arteaga HER2/Neu (ErbB2) signaling to Rac1-Pak1 is temporally and spatially modulated by transforming growth factor beta Cancer Res 66 2006 9591 9600
    • (2006) Cancer Res , vol.66 , pp. 9591-9600
    • Wang, S.E.1    Shin, I.2    Wu, F.Y.3    Friedman, D.B.4    Arteaga, C.L.5
  • 30
    • 2542551853 scopus 로고    scopus 로고
    • Reversible regulation of the transformed phenotype of ornithine decarboxylase- and ras-overexpressing cells by dominant-negative mutants of c-Jun
    • M. Kielosto, P. Nummela, R. Katainen, V. Leaner, M.J. Birrer, E. Holtta Reversible regulation of the transformed phenotype of ornithine decarboxylase- and ras-overexpressing cells by dominant-negative mutants of c-Jun Cancer Res 64 2004 3772 3779
    • (2004) Cancer Res , vol.64 , pp. 3772-3779
    • Kielosto, M.1    Nummela, P.2    Katainen, R.3    Leaner, V.4    Birrer, M.J.5    Holtta, E.6
  • 32
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • V.G. Tusher, R. Tibshirani, G. Chu Significance analysis of microarrays applied to the ionizing radiation response Proc Natl Acad Sci U S A 98 2001 5116 5121
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 33
    • 33748491517 scopus 로고    scopus 로고
    • The MicroArray Quality Control (MAQC) project shows inter- and intraplatform reproducibility of gene expression measurements
    • MAQC Consortium
    • MAQC Consortium L. Shi, L.H. Reid, W.D. Jones, R. Shippy, J.A. Warrington The MicroArray Quality Control (MAQC) project shows inter- and intraplatform reproducibility of gene expression measurements Nat Biotechnol 24 2006 1151 1161
    • (2006) Nat Biotechnol , vol.24 , pp. 1151-1161
    • Shi, L.1    Reid, L.H.2    Jones, W.D.3    Shippy, R.4    Warrington, J.A.5
  • 34
    • 84859073482 scopus 로고    scopus 로고
    • Transforming growth factor beta-induced (TGFBI) is an anti-adhesive protein regulating the invasive growth of melanoma cells
    • P. Nummela, J. Lammi, J. Soikkeli, O. Saksela, P. Laakkonen, E. Hölttä Transforming growth factor beta-induced (TGFBI) is an anti-adhesive protein regulating the invasive growth of melanoma cells Am J Pathol 180 2012 1663 1674
    • (2012) Am J Pathol , vol.180 , pp. 1663-1674
    • Nummela, P.1    Lammi, J.2    Soikkeli, J.3    Saksela, O.4    Laakkonen, P.5    Hölttä, E.6
  • 35
    • 33749065143 scopus 로고    scopus 로고
    • Switch to an invasive growth phase in melanoma is associated with tenascin-C, fibronectin, and procollagen-I forming specific channel structures for invasion
    • E. Kaariainen, P. Nummela, J. Soikkeli, M. Yin, M. Lukk, T. Jahkola, S. Virolainen, A. Ora, E. Ukkonen, O. Saksela, E. Holtta Switch to an invasive growth phase in melanoma is associated with tenascin-C, fibronectin, and procollagen-I forming specific channel structures for invasion J Pathol 210 2006 181 191
    • (2006) J Pathol , vol.210 , pp. 181-191
    • Kaariainen, E.1    Nummela, P.2    Soikkeli, J.3    Yin, M.4    Lukk, M.5    Jahkola, T.6    Virolainen, S.7    Ora, A.8    Ukkonen, E.9    Saksela, O.10    Holtta, E.11
  • 38
    • 0346250118 scopus 로고    scopus 로고
    • Melanoma invasion in reconstructed human skin is influenced by skin cells: Investigation of the role of proteolytic enzymes
    • P. Eves, E. Katerinaki, C. Simpson, C. Layton, R. Dawson, G. Evans, S. Mac Neil Melanoma invasion in reconstructed human skin is influenced by skin cells: investigation of the role of proteolytic enzymes Clin Exp Metastasis 20 2003 685 700
    • (2003) Clin Exp Metastasis , vol.20 , pp. 685-700
    • Eves, P.1    Katerinaki, E.2    Simpson, C.3    Layton, C.4    Dawson, R.5    Evans, G.6    Mac Neil, S.7
  • 39
    • 70349252148 scopus 로고    scopus 로고
    • The invasive potential of human melanoma cell lines correlates with their ability to alter fibroblast gene expression in vitro and the stromal microenvironment in vivo
    • L. Li, B. Dragulev, P. Zigrino, C. Mauch, J.W. Fox The invasive potential of human melanoma cell lines correlates with their ability to alter fibroblast gene expression in vitro and the stromal microenvironment in vivo Int J Cancer 125 2009 1796 1804
    • (2009) Int J Cancer , vol.125 , pp. 1796-1804
    • Li, L.1    Dragulev, B.2    Zigrino, P.3    Mauch, C.4    Fox, J.W.5
  • 40
    • 66349115056 scopus 로고    scopus 로고
    • Cell tracing dyes significantly change single cell mechanics
    • V. Lulevich, Y.P. Shih, S.H. Lo, G.Y. Liu Cell tracing dyes significantly change single cell mechanics J Phys Chem B 113 2009 6511 6519
    • (2009) J Phys Chem B , vol.113 , pp. 6511-6519
    • Lulevich, V.1    Shih, Y.P.2    Lo, S.H.3    Liu, G.Y.4
  • 41
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • N.D. Rawlings, A.J. Barrett, A. Bateman MEROPS: the database of proteolytic enzymes, their substrates and inhibitors Nucleic Acids Res 40 2012 D343 D350
    • (2012) Nucleic Acids Res , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 42
    • 63649143625 scopus 로고    scopus 로고
    • Tissue biomarkers for prognosis in cutaneous melanoma: A systematic review and meta-analysis
    • B.E. Gould Rothberg, M.B. Bracken, D.L. Rimm Tissue biomarkers for prognosis in cutaneous melanoma: a systematic review and meta-analysis J Natl Cancer Inst 101 2009 452 474
    • (2009) J Natl Cancer Inst , vol.101 , pp. 452-474
    • Gould Rothberg, B.E.1    Bracken, M.B.2    Rimm, D.L.3
  • 43
    • 79960404098 scopus 로고    scopus 로고
    • A prognostic index in skin melanoma through the combination of matrix metalloproteinase-2, Ki67, and p53
    • A. Vaisanen, P. Kuvaja, M. Kallioinen, T. Turpeenniemi-Hujanen A prognostic index in skin melanoma through the combination of matrix metalloproteinase-2, Ki67, and p53 Hum Pathol 42 2011 1103 1111
    • (2011) Hum Pathol , vol.42 , pp. 1103-1111
    • Vaisanen, A.1    Kuvaja, P.2    Kallioinen, M.3    Turpeenniemi-Hujanen, T.4
  • 44
    • 0014884119 scopus 로고
    • Thickness, cross-sectional areas and depth of invasion in the prognosis of cutaneous melanoma
    • A. Breslow Thickness, cross-sectional areas and depth of invasion in the prognosis of cutaneous melanoma Ann Surg 172 1970 902 908
    • (1970) Ann Surg , vol.172 , pp. 902-908
    • Breslow, A.1
  • 49
  • 50
    • 0035870263 scopus 로고    scopus 로고
    • An intracellular form of cathepsin B contributes to invasiveness in cancer
    • A.M. Szpaderska, A. Frankfater An intracellular form of cathepsin B contributes to invasiveness in cancer Cancer Res 61 2001 3493 3500
    • (2001) Cancer Res , vol.61 , pp. 3493-3500
    • Szpaderska, A.M.1    Frankfater, A.2
  • 52
    • 0035281687 scopus 로고    scopus 로고
    • Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma
    • E. Frohlich, B. Schlagenhauff, M. Mohrle, E. Weber, C. Klessen, G. Rassner Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma Cancer 91 2001 972 982
    • (2001) Cancer , vol.91 , pp. 972-982
    • Frohlich, E.1    Schlagenhauff, B.2    Mohrle, M.3    Weber, E.4    Klessen, C.5    Rassner, G.6
  • 53
    • 0036718369 scopus 로고    scopus 로고
    • Reactive stroma in human prostate cancer: Induction of myofibroblast phenotype and extracellular matrix remodeling
    • J.A. Tuxhorn, G.E. Ayala, M.J. Smith, V.C. Smith, T.D. Dang, D.R. Rowley Reactive stroma in human prostate cancer: induction of myofibroblast phenotype and extracellular matrix remodeling Clin Cancer Res 8 2002 2912 2923
    • (2002) Clin Cancer Res , vol.8 , pp. 2912-2923
    • Tuxhorn, J.A.1    Ayala, G.E.2    Smith, M.J.3    Smith, V.C.4    Dang, T.D.5    Rowley, D.R.6
  • 55
    • 0037177886 scopus 로고    scopus 로고
    • Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B
    • M. Guo, P.A. Mathieu, B. Linebaugh, B.F. Sloane, J.J. Reiners Jr Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B J Biol Chem 277 2002 14829 14837
    • (2002) J Biol Chem , vol.277 , pp. 14829-14837
    • Guo, M.1    Mathieu, P.A.2    Linebaugh, B.3    Sloane, B.F.4    Reiners, Jr.J.J.5
  • 56
    • 77953178516 scopus 로고    scopus 로고
    • Cathepsin B is the driving force of esophageal cell invasion in a fibroblast-dependent manner
    • C.D. Andl, K.M. McCowan, G.L. Allison, A.K. Rustgi Cathepsin B is the driving force of esophageal cell invasion in a fibroblast-dependent manner Neoplasia 12 2010 485 498
    • (2010) Neoplasia , vol.12 , pp. 485-498
    • Andl, C.D.1    McCowan, K.M.2    Allison, G.L.3    Rustgi, A.K.4
  • 57
  • 58
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • J.P. Annes, J.S. Munger, D.B. Rifkin Making sense of latent TGFbeta activation J Cell Sci 116 2003 217 224
    • (2003) J Cell Sci , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 59
    • 0025765844 scopus 로고
    • A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1
    • K. Miyazono, A. Olofsson, P. Colosetti, C.H. Heldin A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1 EMBO J 10 1991 1091 1101
    • (1991) EMBO J , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.H.4
  • 60
    • 0037899253 scopus 로고    scopus 로고
    • Role of tissue stroma in cancer cell invasion
    • O. De Wever, M. Mareel Role of tissue stroma in cancer cell invasion J Pathol 200 2003 429 447
    • (2003) J Pathol , vol.200 , pp. 429-447
    • De Wever, O.1    Mareel, M.2
  • 61
    • 36749013537 scopus 로고    scopus 로고
    • Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells
    • C. Gaggioli, S. Hooper, C. Hidalgo-Carcedo, R. Grosse, J.F. Marshall, K. Harrington, E. Sahai Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells Nat Cell Biol 9 2007 1392 1400
    • (2007) Nat Cell Biol , vol.9 , pp. 1392-1400
    • Gaggioli, C.1    Hooper, S.2    Hidalgo-Carcedo, C.3    Grosse, R.4    Marshall, J.F.5    Harrington, K.6    Sahai, E.7
  • 62
    • 0025868178 scopus 로고
    • Fibroblast cell interactions with human melanoma cells affect tumor cell growth as a function of tumor progression
    • I. Cornil, D. Theodorescu, S. Man, M. Herlyn, J. Jambrosic, R.S. Kerbel Fibroblast cell interactions with human melanoma cells affect tumor cell growth as a function of tumor progression Proc Natl Acad Sci U S A 88 1991 6028 6032
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6028-6032
    • Cornil, I.1    Theodorescu, D.2    Man, S.3    Herlyn, M.4    Jambrosic, J.5    Kerbel, R.S.6
  • 63
    • 0034472617 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion and metastasis
    • I. Stamenkovic Matrix metalloproteinases in tumor invasion and metastasis Semin Cancer Biol 10 2000 415 433
    • (2000) Semin Cancer Biol , vol.10 , pp. 415-433
    • Stamenkovic, I.1
  • 64
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • L.M. Coussens, B. Fingleton, L.M. Matrisian Matrix metalloproteinase inhibitors and cancer: trials and tribulations Science 295 2002 2387 2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 65
    • 33646593786 scopus 로고    scopus 로고
    • Modifying the soil to affect the seed: Role of stromal-derived matrix metalloproteinases in cancer progression
    • S. Jodele, L. Blavier, J.M. Yoon, Y.A. DeClerck Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression Cancer Metastasis Rev 25 2006 35 43
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 35-43
    • Jodele, S.1    Blavier, L.2    Yoon, J.M.3    Declerck, Y.A.4
  • 67
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment-opinion: Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • C.M. Overall, O. Kleifeld Tumour microenvironment-opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy Nat Rev Cancer 6 2006 227 239
    • (2006) Nat Rev Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 69
    • 4744366992 scopus 로고    scopus 로고
    • CD10 protein expression in tumor and stromal cells of malignant melanoma is associated with tumor progression
    • N. Bilalovic, B. Sandstad, R. Golouh, J.M. Nesland, I. Selak, E.E. Torlakovic CD10 protein expression in tumor and stromal cells of malignant melanoma is associated with tumor progression Mod Pathol 17 2004 1251 1258
    • (2004) Mod Pathol , vol.17 , pp. 1251-1258
    • Bilalovic, N.1    Sandstad, B.2    Golouh, R.3    Nesland, J.M.4    Selak, I.5    Torlakovic, E.E.6
  • 73
    • 34547640302 scopus 로고    scopus 로고
    • Inhibition of cysteine cathepsin protease activity enhances chemotherapy regimens by decreasing tumor growth and invasiveness in a mouse model of multistage cancer
    • K.M. Bell-McGuinn, A.L. Garfall, M. Bogyo, D. Hanahan, J.A. Joyce Inhibition of cysteine cathepsin protease activity enhances chemotherapy regimens by decreasing tumor growth and invasiveness in a mouse model of multistage cancer Cancer Res 67 2007 7378 7385
    • (2007) Cancer Res , vol.67 , pp. 7378-7385
    • Bell-Mcguinn, K.M.1    Garfall, A.L.2    Bogyo, M.3    Hanahan, D.4    Joyce, J.A.5
  • 76
    • 0023462882 scopus 로고
    • The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L
    • R.W. Mason, S. Gal, M.M. Gottesman The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L Biochem J 248 1987 449 454
    • (1987) Biochem J , vol.248 , pp. 449-454
    • Mason, R.W.1    Gal, S.2    Gottesman, M.M.3
  • 77
    • 0038215389 scopus 로고    scopus 로고
    • Pericellular cathepsin B and malignant progression
    • S. Roshy, B.F. Sloane, K. Moin Pericellular cathepsin B and malignant progression Cancer Metastasis Rev 22 2003 271 286
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 271-286
    • Roshy, S.1    Sloane, B.F.2    Moin, K.3
  • 78
    • 77957855881 scopus 로고    scopus 로고
    • Specialized roles for cysteine cathepsins in health and disease
    • J. Reiser, B. Adair, T. Reinheckel Specialized roles for cysteine cathepsins in health and disease J Clin Invest 120 2010 3421 3431
    • (2010) J Clin Invest , vol.120 , pp. 3421-3431
    • Reiser, J.1    Adair, B.2    Reinheckel, T.3
  • 80
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • G. Murphy, R. Ward, J. Gavrilovic, S. Atkinson Physiological mechanisms for metalloproteinase activation Matrix Suppl 1 1992 224 230
    • (1992) Matrix Suppl , vol.1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 81
    • 0026734254 scopus 로고
    • Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B
    • H. Kobayashi, H. Ohi, M. Sugimura, H. Shinohara, T. Fujii, T. Terao Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B Cancer Res 52 1992 3610 3614
    • (1992) Cancer Res , vol.52 , pp. 3610-3614
    • Kobayashi, H.1    Ohi, H.2    Sugimura, M.3    Shinohara, H.4    Fujii, T.5    Terao, T.6
  • 84
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Y. Yasuda, Z. Li, D. Greenbaum, M. Bogyo, E. Weber, D. Bromme Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages J Biol Chem 279 2004 36761 36770
    • (2004) J Biol Chem , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6
  • 85
    • 0033082525 scopus 로고    scopus 로고
    • Independent regulation of growth and SMAD-mediated transcription by transforming growth factor beta in human melanoma cells
    • U. Rodeck, T. Nishiyama, A. Mauviel Independent regulation of growth and SMAD-mediated transcription by transforming growth factor beta in human melanoma cells Cancer Res 59 1999 547 550
    • (1999) Cancer Res , vol.59 , pp. 547-550
    • Rodeck, U.1    Nishiyama, T.2    Mauviel, A.3
  • 88
    • 43049146157 scopus 로고    scopus 로고
    • The role of proteases in transforming growth factor-beta activation
    • G. Jenkins The role of proteases in transforming growth factor-beta activation Int J Biochem Cell Biol 40 2008 1068 1078
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1068-1078
    • Jenkins, G.1
  • 90
  • 91
    • 78149358974 scopus 로고    scopus 로고
    • Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model
    • B.T. Elie, V. Gocheva, T. Shree, S.A. Dalrymple, L.J. Holsinger, J.A. Joyce Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model Biochimie 92 2010 1618 1624
    • (2010) Biochimie , vol.92 , pp. 1618-1624
    • Elie, B.T.1    Gocheva, V.2    Shree, T.3    Dalrymple, S.A.4    Holsinger, L.J.5    Joyce, J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.