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Volumn 87, Issue 3-4 SPEC. ISS., 2005, Pages 321-328

Tumor-stroma interactions: Their role in the control of tumor cell invasion

Author keywords

Proteases; Receptors; Stroma; Tumor

Indexed keywords

COLLAGENASE 3; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; TISSUE INHIBITOR OF METALLOPROTEINASE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; VERY LATE ACTIVATION ANTIGEN 2;

EID: 15244348665     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.10.025     Document Type: Short Survey
Times cited : (100)

References (95)
  • 1
    • 0141988559 scopus 로고    scopus 로고
    • Molecular mechanisms of tumor invasion and metastasis: An integrated view
    • R.A. Cairns, R. Khokha, and R.P. Hill Molecular mechanisms of tumor invasion and metastasis: an integrated view Curr Mol Med 3 2003 659 671
    • (2003) Curr Mol Med , vol.3 , pp. 659-671
    • Cairns, R.A.1    Khokha, R.2    Hill, R.P.3
  • 2
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • L.M. Coussens, and Z. Werb Inflammation and cancer Nature 420 2002 860 867
    • (2002) Nature , vol.420 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 3
    • 0028334894 scopus 로고
    • E-cadherin is the major mediator of human melanocyte adhesion to keratinocytes in vitro
    • A. Tang, M.S. Eller, M. Hara, M. Yaar, S. Hirohashi, and B.A. Gilchrest E-cadherin is the major mediator of human melanocyte adhesion to keratinocytes in vitro J. Cell Sci. 107 1994 983 992
    • (1994) J. Cell Sci. , vol.107 , pp. 983-992
    • Tang, A.1    Eller, M.S.2    Hara, M.3    Yaar, M.4    Hirohashi, S.5    Gilchrest, B.A.6
  • 4
    • 0034025433 scopus 로고    scopus 로고
    • Cadherin repertoire determines partner-specific gap junctional communication during melanoma progression
    • M. Hsu, T. Andl, G. Li, J.L. Meinkoth, and M. Herlyn Cadherin repertoire determines partner-specific gap junctional communication during melanoma progression J. Cell Sci. 113 2000 1535 1542
    • (2000) J. Cell Sci. , vol.113 , pp. 1535-1542
    • Hsu, M.1    Andl, T.2    Li, G.3    Meinkoth, J.L.4    Herlyn, M.5
  • 5
    • 0007936466 scopus 로고    scopus 로고
    • Alterations in cadherin and catenin expression during the biological progression of melanocytic tumours
    • D.S. Sanders, K. Blessing, G.A. Hassan, R. Bruton, J.R. Marsden, and J. Jankowski Alterations in cadherin and catenin expression during the biological progression of melanocytic tumours Mol. Pathol. 52 1999 151 157
    • (1999) Mol. Pathol. , vol.52 , pp. 151-157
    • Sanders, D.S.1    Blessing, K.2    Hassan, G.A.3    Bruton, R.4    Marsden, J.R.5    Jankowski, J.6
  • 6
    • 0030470184 scopus 로고    scopus 로고
    • Expression of N-cadherin by human squamous carcinoma cells induces a scattered fibroblastic phenotype with disrupted cell-cell adhesion
    • S. Islam, T.E. Carey, G.T. Wolf, M.J. Wheelock, and K.R. Johnson Expression of N-cadherin by human squamous carcinoma cells induces a scattered fibroblastic phenotype with disrupted cell-cell adhesion J. Cell Biol. 135 1996 1643 1654
    • (1996) J. Cell Biol. , vol.135 , pp. 1643-1654
    • Islam, S.1    Carey, T.E.2    Wolf, G.T.3    Wheelock, M.J.4    Johnson, K.R.5
  • 8
    • 0029873133 scopus 로고    scopus 로고
    • Biology of tumor cell invasion: Interplay of cell adhesion and matrix degradation
    • J. Heino Biology of tumor cell invasion: interplay of cell adhesion and matrix degradation Int. J. Cancer 65 1996 717 722
    • (1996) Int. J. Cancer , vol.65 , pp. 717-722
    • Heino, J.1
  • 9
    • 0032030656 scopus 로고    scopus 로고
    • Integrins and GTPases in tumour cell growth, motility and invasion
    • P. Keely, L. Parise, and R. Juliano Integrins and GTPases in tumour cell growth, motility and invasion Trends Cell Biol. 8 1998 101 106
    • (1998) Trends Cell Biol. , vol.8 , pp. 101-106
    • Keely, P.1    Parise, L.2    Juliano, R.3
  • 10
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • E. Ruoslahti, and M.D. Pierschbacher New perspectives in cell adhesion: RGD and integrins Science 238 1987 491 497
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 11
    • 0022508987 scopus 로고
    • A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells
    • M.J. Humphries, K. Olden, and K.M. Yamada A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells Science 233 1986 467 470
    • (1986) Science , vol.233 , pp. 467-470
    • Humphries, M.J.1    Olden, K.2    Yamada, K.M.3
  • 12
    • 0024401619 scopus 로고
    • Antimetastatic effects of synthetic polypeptides containing repeated structures of the cell adhesive Arg-Gly-Asp (RGD) and Tyr-Ile-Gly-Ser-Arg (YIGSR) sequences
    • I. Saiki, J. Murata, J. Iida, T. Sakurai, N. Nishi, and K. Matsuno Antimetastatic effects of synthetic polypeptides containing repeated structures of the cell adhesive Arg-Gly-Asp (RGD) and Tyr-Ile-Gly-Ser-Arg (YIGSR) sequences Br. J. Cancer 60 1989 722 728
    • (1989) Br. J. Cancer , vol.60 , pp. 722-728
    • Saiki, I.1    Murata, J.2    Iida, J.3    Sakurai, T.4    Nishi, N.5    Matsuno, K.6
  • 13
    • 0037728975 scopus 로고    scopus 로고
    • Alphavbeta3 integrin antagonist S247 decreases colon cancer metastasis and angiogenesis and improves survival in mice
    • N. Reinmuth, W. Liu, S.A. Ahmad, F. Fan, O. Stoeltzing, and A.A. Parikh Alphavbeta3 integrin antagonist S247 decreases colon cancer metastasis and angiogenesis and improves survival in mice Cancer Res. 63 2003 2079 2087
    • (2003) Cancer Res. , vol.63 , pp. 2079-2087
    • Reinmuth, N.1    Liu, W.2    Ahmad, S.A.3    Fan, F.4    Stoeltzing, O.5    Parikh, A.A.6
  • 15
  • 16
    • 0027157861 scopus 로고
    • Integrin expression in cutaneous malignant melanoma: Association of the alpha 3/beta 1 heterodimer with tumor progression
    • P.G. Natali, M.R. Nicotra, A. Bartolazzi, R. Cavaliere, and A. Bigotti Integrin expression in cutaneous malignant melanoma: association of the alpha 3/beta 1 heterodimer with tumor progression Int. J. Cancer 54 1993 68 72
    • (1993) Int. J. Cancer , vol.54 , pp. 68-72
    • Natali, P.G.1    Nicotra, M.R.2    Bartolazzi, A.3    Cavaliere, R.4    Bigotti, A.5
  • 17
    • 0025880917 scopus 로고
    • Integrin alpha 2 beta 1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils
    • C.E. Klein, D. Dressel, T. Steinmayer, C. Mauch, B. Eckes, and T. Krieg Integrin alpha 2 beta 1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils J. Cell Biol. 115 1991 1427 1436
    • (1991) J. Cell Biol. , vol.115 , pp. 1427-1436
    • Klein, C.E.1    Dressel, D.2    Steinmayer, T.3    Mauch, C.4    Eckes, B.5    Krieg, T.6
  • 18
    • 0033597728 scopus 로고    scopus 로고
    • Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines
    • P. Kurschat, P. Zigrino, R. Nischt, K. Breitkopf, P. Steurer, and C.E. Klein Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines J. Biol. Chem. 274 1999 21056 21062
    • (1999) J. Biol. Chem. , vol.274 , pp. 21056-21062
    • Kurschat, P.1    Zigrino, P.2    Nischt, R.3    Breitkopf, K.4    Steurer, P.5    Klein, C.E.6
  • 19
    • 0031816911 scopus 로고    scopus 로고
    • The disintegrin eristostatin interferes with integrin alpha 4 beta 1 function and with experimental metastasis of human melanoma cells
    • E.H. Danen, C. Marcinkiewicz, I.M. Cornelissen, A.A. Van:Kraats, J.A. Pachter, and D.J. Ruiter The disintegrin eristostatin interferes with integrin alpha 4 beta 1 function and with experimental metastasis of human melanoma cells Exp. Cell Res. 238 1998 188 196
    • (1998) Exp. Cell Res. , vol.238 , pp. 188-196
    • Danen, E.H.1    Marcinkiewicz, C.2    Cornelissen, I.M.3    Van4    Kraats, A.A.5    Pachter, J.A.6    Ruiter, D.J.7
  • 20
    • 0028841186 scopus 로고
    • Mitogenic activity of laminin on human melanoma and melanocytes: Different signal requirements and role of beta 1 integrins
    • R. Mortarini, A. Gismondi, A. Maggioni, A. Santoni, M. Herlyn, and A. Anichini Mitogenic activity of laminin on human melanoma and melanocytes: different signal requirements and role of beta 1 integrins Cancer Res. 55 1995 4702 4710
    • (1995) Cancer Res. , vol.55 , pp. 4702-4710
    • Mortarini, R.1    Gismondi, A.2    Maggioni, A.3    Santoni, A.4    Herlyn, M.5    Anichini, A.6
  • 21
    • 0028970987 scopus 로고
    • Integrin alpha 6 expression in human prostate carcinoma cells is associated with a migratory and invasive phenotype in vitro and in vivo
    • I. Rabinovitz, R.B. Nagle, and A.E. Cress Integrin alpha 6 expression in human prostate carcinoma cells is associated with a migratory and invasive phenotype in vitro and in vivo Clin. Exp. Metastasis 13 1995 481 491
    • (1995) Clin. Exp. Metastasis , vol.13 , pp. 481-491
    • Rabinovitz, I.1    Nagle, R.B.2    Cress, A.E.3
  • 22
    • 0022966376 scopus 로고
    • Purification of melanoma growth stimulatory activity
    • A. Richmond, and H.G. Thomas Purification of melanoma growth stimulatory activity J. Cell. Physiol. 129 1986 375 384
    • (1986) J. Cell. Physiol. , vol.129 , pp. 375-384
    • Richmond, A.1    Thomas, H.G.2
  • 23
    • 0036093865 scopus 로고    scopus 로고
    • Inflammation and the development of pancreatic cancer
    • B. Farrow, and B.M. Evers Inflammation and the development of pancreatic cancer Surg. Oncol. 10 2002 153 169
    • (2002) Surg. Oncol. , vol.10 , pp. 153-169
    • Farrow, B.1    Evers, B.M.2
  • 24
    • 0023104031 scopus 로고
    • Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
    • A.E. Postlethwaite, J. Keski-Oja, H.L. Moses, and A.H. Kang Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta J. Exp. Med. 165 1987 251 256
    • (1987) J. Exp. Med. , vol.165 , pp. 251-256
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Moses, H.L.3    Kang, A.H.4
  • 25
    • 0026600577 scopus 로고
    • Transforming growth factor-beta 1 overproduction in prostate cancer: Effects on growth in vivo and in vitro
    • M.S. Steiner, and E.R. Barrack Transforming growth factor-beta 1 overproduction in prostate cancer: effects on growth in vivo and in vitro Mol. Endocrinol. 6 1992 15 25
    • (1992) Mol. Endocrinol. , vol.6 , pp. 15-25
    • Steiner, M.S.1    Barrack, E.R.2
  • 26
    • 0842288323 scopus 로고    scopus 로고
    • TGF-beta signaling in fibroblasts modulates the oncogenic potential of adjacent epithelia
    • N.A. Bhowmick, A. Chytil, D. Plieth, A.E. Gorska, N. Dumont, and S. Shappell TGF-beta signaling in fibroblasts modulates the oncogenic potential of adjacent epithelia Science 303 2004 848 851
    • (2004) Science , vol.303 , pp. 848-851
    • Bhowmick, N.A.1    Chytil, A.2    Plieth, D.3    Gorska, A.E.4    Dumont, N.5    Shappell, S.6
  • 27
    • 0034644472 scopus 로고    scopus 로고
    • TGFbeta signaling in growth control, cancer, and heritable disorders
    • J. Massague, S.W. Blain, and R.S. Lo TGFbeta signaling in growth control, cancer, and heritable disorders Cell 103 2000 295 309
    • (2000) Cell , vol.103 , pp. 295-309
    • Massague, J.1    Blain, S.W.2    Lo, R.S.3
  • 28
    • 0033818034 scopus 로고    scopus 로고
    • Lessons from melanocyte development for understanding the biological events in naevus and melanoma formation
    • M. Herlyn, C. Berking, G. Li, and K. Satyamoorthy Lessons from melanocyte development for understanding the biological events in naevus and melanoma formation Melanoma Res. 10 2000 303 312
    • (2000) Melanoma Res. , vol.10 , pp. 303-312
    • Herlyn, M.1    Berking, C.2    Li, G.3    Satyamoorthy, K.4
  • 29
    • 1242271205 scopus 로고    scopus 로고
    • Endothelin B receptor blockade inhibits dynamics of cell interactions and communications in melanoma cell progression
    • A. Bagnato, L. Rosano, F. Spinella, V. Di:Castro, R. Tecce, and P.G. Natali Endothelin B receptor blockade inhibits dynamics of cell interactions and communications in melanoma cell progression Cancer Res. 64 2004 1436 1443
    • (2004) Cancer Res. , vol.64 , pp. 1436-1443
    • Bagnato, A.1    Rosano, L.2    Spinella, F.3    Di4    Castro, V.5    Tecce, R.6    Natali, P.G.7
  • 30
    • 10744228941 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 but not Mel-CAM and/or beta3 integrin promotes progression of melanocytes to melanoma
    • F. Meier, U. Caroli, K. Satyamoorthy, B. Schittek, J. Bauer, and C. Berking Fibroblast growth factor-2 but not Mel-CAM and/or beta3 integrin promotes progression of melanocytes to melanoma Exp. Dermatol. 12 2003 296 306
    • (2003) Exp. Dermatol. , vol.12 , pp. 296-306
    • Meier, F.1    Caroli, U.2    Satyamoorthy, K.3    Schittek, B.4    Bauer, J.5    Berking, C.6
  • 31
    • 0035101043 scopus 로고    scopus 로고
    • Basic fibroblast growth factor and ultraviolet B transform melanocytes in human skin
    • C. Berking, R. Takemoto, K. Satyamoorthy, R. Elenitsas, and M. Herlyn Basic fibroblast growth factor and ultraviolet B transform melanocytes in human skin Am. J. Pathol. 158 2001 943 953
    • (2001) Am. J. Pathol. , vol.158 , pp. 943-953
    • Berking, C.1    Takemoto, R.2    Satyamoorthy, K.3    Elenitsas, R.4    Herlyn, M.5
  • 33
    • 0033067863 scopus 로고    scopus 로고
    • Matrix-degrading proteases and angiogenesis during development and tumor formation
    • Z. Werb, T.H. Vu, J.L. Rinkenberger, and L.M. Coussens Matrix-degrading proteases and angiogenesis during development and tumor formation APMIS 107 1999 11 18
    • (1999) APMIS , vol.107 , pp. 11-18
    • Werb, Z.1    Vu, T.H.2    Rinkenberger, J.L.3    Coussens, L.M.4
  • 34
    • 0030293598 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the development of cancer
    • L.M. Coussens, and Z. Werb Matrix metalloproteinases and the development of cancer Chem. Biol. 3 1996 895 904
    • (1996) Chem. Biol. , vol.3 , pp. 895-904
    • Coussens, L.M.1    Werb, Z.2
  • 35
    • 0025641098 scopus 로고
    • A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas
    • P. Basset, J.P. Bellocq, C. Wolf, I. Stoll, P. Hutin, and J.M. Limacher A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas Nature 348 1990 699 704
    • (1990) Nature , vol.348 , pp. 699-704
    • Basset, P.1    Bellocq, J.P.2    Wolf, C.3    Stoll, I.4    Hutin, P.5    Limacher, J.M.6
  • 36
    • 0033752213 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase-mediated progelatinase a activation in non-tumorigenic and tumorigenic human keratinocytes
    • P. Baumann, P. Zigrino, C. Mauch, D. Breitkreutz, and R. Nischt Membrane-type 1 matrix metalloproteinase-mediated progelatinase A activation in non-tumorigenic and tumorigenic human keratinocytes Br. J. Cancer 83 2000 1387 1393
    • (2000) Br. J. Cancer , vol.83 , pp. 1387-1393
    • Baumann, P.1    Zigrino, P.2    Mauch, C.3    Breitkreutz, D.4    Nischt, R.5
  • 37
    • 0036262509 scopus 로고    scopus 로고
    • Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography
    • P. Kurschat, C. Wickenhauser, W. Groth, T. Krieg, and C. Mauch Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography J. Pathol. 197 2002 179 187
    • (2002) J. Pathol. , vol.197 , pp. 179-187
    • Kurschat, P.1    Wickenhauser, C.2    Groth, W.3    Krieg, T.4    Mauch, C.5
  • 38
    • 0036417284 scopus 로고    scopus 로고
    • In vivo glioma growth requires host-derived matrix metalloproteinase 2 for maintenance of angioarchitecture
    • M. Takahashi, S. Fukami, N. Iwata, K. Inoue, S. Itohara, and H. Itoh In vivo glioma growth requires host-derived matrix metalloproteinase 2 for maintenance of angioarchitecture Pharmacol. Res. 46 2002 155 163
    • (2002) Pharmacol. Res. , vol.46 , pp. 155-163
    • Takahashi, M.1    Fukami, S.2    Iwata, N.3    Inoue, K.4    Itohara, S.5    Itoh, H.6
  • 40
    • 0033923006 scopus 로고    scopus 로고
    • Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type 1 matrix metalloproteinase (MT1-MMP) correlate with melanoma progression
    • U.B. Hofmann, J.R. Westphal, A.J. Zendman, J.C. Becker, D.J. Ruiter, and G.N. Van:Muijen Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type 1 matrix metalloproteinase (MT1-MMP) correlate with melanoma progression J. Pathol. 191 2000 245 256
    • (2000) J. Pathol. , vol.191 , pp. 245-256
    • Hofmann, U.B.1    Westphal, J.R.2    Zendman, A.J.3    Becker, J.C.4    Ruiter, D.J.5    Van6    Muijen, G.N.7
  • 41
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • A. Okada, J.P. Bellocq, N. Rouyer, M.P. Chenard, M.C. Rio, and P. Chambon Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas Proc. Natl. Acad. Sci. USA 92 1995 2730 2734
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.P.2    Rouyer, N.3    Chenard, M.P.4    Rio, M.C.5    Chambon, P.6
  • 42
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • N. Koshikawa, G. Giannelli, V. Cirulli, K. Miyazaki, and V. Quaranta Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5 J. Cell Biol. 148 2000 615 624
    • (2000) J. Cell Biol. , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 43
    • 0035892362 scopus 로고    scopus 로고
    • Laminin-5 in the progression of carcinomas
    • J. Lohi Laminin-5 in the progression of carcinomas Int. J. Cancer 94 2001 763 767
    • (2001) Int. J. Cancer , vol.94 , pp. 763-767
    • Lohi, J.1
  • 44
    • 0035988822 scopus 로고    scopus 로고
    • Laminin isoforms in tumor invasion, angiogenesis and metastasis
    • M. Patarroyo, K. Tryggvason, and I. Virtanen Laminin isoforms in tumor invasion, angiogenesis and metastasis Semin. Cancer Biol. 12 2002 197 207
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 197-207
    • Patarroyo, M.1    Tryggvason, K.2    Virtanen, I.3
  • 45
    • 0035417897 scopus 로고    scopus 로고
    • Cooperative interactions of laminin 5 gamma2 chain, matrix metalloproteinase-2, and membrane type-1-matrix/metalloproteinase are required for mimicry of embryonic vasculogenesis by aggressive melanoma
    • R.E. Seftor, E.A. Seftor, N. Koshikawa, P.S. Meltzer, L.M. Gardner, and M. Bilban Cooperative interactions of laminin 5 gamma2 chain, matrix metalloproteinase-2, and membrane type-1-matrix/metalloproteinase are required for mimicry of embryonic vasculogenesis by aggressive melanoma Cancer Res. 61 2001 6322 6327
    • (2001) Cancer Res. , vol.61 , pp. 6322-6327
    • Seftor, R.E.1    Seftor, E.A.2    Koshikawa, N.3    Meltzer, P.S.4    Gardner, L.M.5    Bilban, M.6
  • 46
    • 0343415583 scopus 로고    scopus 로고
    • Fibroblasts surrounding melanoma express elevated levels of matrix metalloproteinase-1 (MMP-1) and intercellular adhesion molecule-1 (ICAM-1) in vitro
    • E. Wandel, A. Grasshoff, M. Mittag, U.F. Haustein, and A. Saalbach Fibroblasts surrounding melanoma express elevated levels of matrix metalloproteinase-1 (MMP-1) and intercellular adhesion molecule-1 (ICAM-1) in vitro Exp. Dermatol. 9 2000 34 41
    • (2000) Exp. Dermatol. , vol.9 , pp. 34-41
    • Wandel, E.1    Grasshoff, A.2    Mittag, M.3    Haustein, U.F.4    Saalbach, A.5
  • 47
    • 0027328322 scopus 로고
    • Tumor cell-derived collagenase-stimulatory factor increases expression of interstitial collagenase, stromelysin, and 72-kDa gelatinase
    • H. Kataoka, R. DeCastro, S. Zucker, and C. Biswas Tumor cell-derived collagenase-stimulatory factor increases expression of interstitial collagenase, stromelysin, and 72-kDa gelatinase Cancer Res. 53 1993 3154 3158
    • (1993) Cancer Res. , vol.53 , pp. 3154-3158
    • Kataoka, H.1    Decastro, R.2    Zucker, S.3    Biswas, C.4
  • 48
    • 0344844479 scopus 로고    scopus 로고
    • Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells
    • S. Menashi, M. Serova, L. Ma, S. Vignot, S. Mourah, and F. Calvo Regulation of extracellular matrix metalloproteinase inducer and matrix metalloproteinase expression by amphiregulin in transformed human breast epithelial cells Cancer Res. 63 2003 7575 7580
    • (2003) Cancer Res. , vol.63 , pp. 7575-7580
    • Menashi, S.1    Serova, M.2    Ma, L.3    Vignot, S.4    Mourah, S.5    Calvo, F.6
  • 49
    • 0034976637 scopus 로고    scopus 로고
    • Tumorigenic potential of extracellular matrix metalloproteinase inducer
    • S. Zucker, M. Hymowitz, E.E. Rollo, R. Mann, C.E. Conner, and J. Cao Tumorigenic potential of extracellular matrix metalloproteinase inducer Am. J. Pathol. 158 2001 1921 1928
    • (2001) Am. J. Pathol. , vol.158 , pp. 1921-1928
    • Zucker, S.1    Hymowitz, M.2    Rollo, E.E.3    Mann, R.4    Conner, C.E.5    Cao, J.6
  • 51
    • 0036605095 scopus 로고    scopus 로고
    • Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts
    • T. Kanekura, X. Chen, and T. Kanzaki Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts Int. J. Cancer 99 2002 520 528
    • (2002) Int. J. Cancer , vol.99 , pp. 520-528
    • Kanekura, T.1    Chen, X.2    Kanzaki, T.3
  • 52
    • 0034652586 scopus 로고    scopus 로고
    • EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface
    • H. Guo, R. Li, S. Zucker, and B.P. Toole EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface Cancer Res. 60 2000 888 891
    • (2000) Cancer Res. , vol.60 , pp. 888-891
    • Guo, H.1    Li, R.2    Zucker, S.3    Toole, B.P.4
  • 53
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    • P.C. Brooks, S. Stromblad, L.C. Sanders, T.L. Von Schalscha, R.T. Aimes, and W.G. Stetler-Stevenson Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3 Cell 85 1996 683 693
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3    Von Schalscha, T.L.4    Aimes, R.T.5    Stetler-Stevenson, W.G.6
  • 54
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells
    • E.I. Deryugina, B. Ratnikov, E. Monosov, T.I. Postnova, R. DiScipio, and J.W. Smith MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells Exp. Cell Res. 263 2001 209 223
    • (2001) Exp. Cell Res. , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, B.2    Monosov, E.3    Postnova, T.I.4    Discipio, R.5    Smith, J.W.6
  • 55
  • 56
    • 0031426654 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells
    • A. Lochter, S. Galosy, J. Muschler, N. Freedman, Z. Werb, and M.J. Bissell Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells J. Cell Biol. 139 1997 1861 1872
    • (1997) J. Cell Biol. , vol.139 , pp. 1861-1872
    • Lochter, A.1    Galosy, S.2    Muschler, J.3    Freedman, N.4    Werb, Z.5    Bissell, M.J.6
  • 57
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • M. Kajita, Y. Itoh, T. Chiba, H. Mori, A. Okada, and H. Kinoh Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration J. Cell Biol. 153 2001 893 904
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6
  • 58
    • 0842347494 scopus 로고    scopus 로고
    • Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-type 1 matrix metalloproteinase
    • H. Nakamura, N. Suenaga, K. Taniwaki, H. Matsuki, K. Yonezawa, and M. Fujii Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-type 1 matrix metalloproteinase Cancer Res. 64 2004 876 882
    • (2004) Cancer Res. , vol.64 , pp. 876-882
    • Nakamura, H.1    Suenaga, N.2    Taniwaki, K.3    Matsuki, H.4    Yonezawa, K.5    Fujii, M.6
  • 59
    • 0029943568 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases in angiogenesis
    • P. Mignatti, and D.B. Rifkin Plasminogen activators and matrix metalloproteinases in angiogenesis Enzyme Protein 49 1996 117 137
    • (1996) Enzyme Protein , vol.49 , pp. 117-137
    • Mignatti, P.1    Rifkin, D.B.2
  • 60
    • 0024261420 scopus 로고
    • Plasminogen activation: Biochemistry, physiology, and therapeutics
    • T.C. Wun Plasminogen activation: biochemistry, physiology, and therapeutics Crit. Rev. Biotechnol. 8 1988 131 148
    • (1988) Crit. Rev. Biotechnol. , vol.8 , pp. 131-148
    • Wun, T.C.1
  • 61
    • 0029682495 scopus 로고    scopus 로고
    • Induction of primary cutaneous melanocytic neoplasms in urokinase-type plasminogen activator (uPA)-deficient and wild-type mice: Cellular blue nevi invade but do not progress to malignant melanoma in uPA-deficient animals
    • R.L. Shapiro, J.G. Duquette, D.F. Roses, I. Nunes, M.N. Harris, and H. Kamino Induction of primary cutaneous melanocytic neoplasms in urokinase-type plasminogen activator (uPA)-deficient and wild-type mice: cellular blue nevi invade but do not progress to malignant melanoma in uPA-deficient animals Cancer Res. 56 1996 3597 3604
    • (1996) Cancer Res. , vol.56 , pp. 3597-3604
    • Shapiro, R.L.1    Duquette, J.G.2    Roses, D.F.3    Nunes, I.4    Harris, M.N.5    Kamino, H.6
  • 62
    • 0029892448 scopus 로고    scopus 로고
    • Expression of plasminogen activators in basal cell carcinoma
    • E.M. Spiers, G.S. Lazarus, and B. Lyons-Giordano Expression of plasminogen activators in basal cell carcinoma J. Pathol. 178 1996 290 296
    • (1996) J. Pathol. , vol.178 , pp. 290-296
    • Spiers, E.M.1    Lazarus, G.S.2    Lyons-Giordano, B.3
  • 63
    • 0030931986 scopus 로고    scopus 로고
    • Localization of plasminogen activators and their inhibitor in squamous cell carcinomas of the head and neck
    • T. Yasuda, Y. Sakata, K. Kitamura, M. Morita, and T. Ishida Localization of plasminogen activators and their inhibitor in squamous cell carcinomas of the head and neck Head Neck 19 1997 611 616
    • (1997) Head Neck , vol.19 , pp. 611-616
    • Yasuda, T.1    Sakata, Y.2    Kitamura, K.3    Morita, M.4    Ishida, T.5
  • 65
    • 0038505666 scopus 로고    scopus 로고
    • Invasion of melanoma cells into dermal connective tissue in vitro: Evidence for an important role of cysteine proteases
    • R. Dennhofer, P. Kurschat, P. Zigrino, A. Klose, A. Bosserhoff, and G. Van:Muijen Invasion of melanoma cells into dermal connective tissue in vitro: evidence for an important role of cysteine proteases Int. J. Cancer 106 2003 316 323
    • (2003) Int. J. Cancer , vol.106 , pp. 316-323
    • Dennhofer, R.1    Kurschat, P.2    Zigrino, P.3    Klose, A.4    Bosserhoff, A.5    Van6    Muijen, G.7
  • 66
    • 0024246445 scopus 로고
    • Immunohistochemical and biochemical study of a cathepsin B-like proteinase in human colonic cancers
    • D. Keppler, M.C. Fondaneche, V. Dalet-Fumeron, M. Pagano, and P. Burtin Immunohistochemical and biochemical study of a cathepsin B-like proteinase in human colonic cancers Cancer Res. 48 1988 6855 6862
    • (1988) Cancer Res. , vol.48 , pp. 6855-6862
    • Keppler, D.1    Fondaneche, M.C.2    Dalet-Fumeron, V.3    Pagano, M.4    Burtin, P.5
  • 67
    • 0031882125 scopus 로고    scopus 로고
    • Increased activity of cathepsin B in fibroblasts isolated from primary melanoma in comparison to fibroblasts from normal skin
    • A. Ulmer, V. Korber, H. Schmid, and G. Fierlbeck Increased activity of cathepsin B in fibroblasts isolated from primary melanoma in comparison to fibroblasts from normal skin Exp. Dermatol. 7 1998 14 17
    • (1998) Exp. Dermatol. , vol.7 , pp. 14-17
    • Ulmer, A.1    Korber, V.2    Schmid, H.3    Fierlbeck, G.4
  • 69
    • 0030032540 scopus 로고    scopus 로고
    • A cysteine proteinase, which cleaves human C3, the third component of complement, is involved in tumorigenicity and metastasis of human melanoma
    • D. Jean, M. Bar-Eli, S. Huang, K. Xie, F. Rodrigues-Lima, and J. Hermann A cysteine proteinase, which cleaves human C3, the third component of complement, is involved in tumorigenicity and metastasis of human melanoma Cancer Res. 56 1996 254 258
    • (1996) Cancer Res. , vol.56 , pp. 254-258
    • Jean, D.1    Bar-Eli, M.2    Huang, S.3    Xie, K.4    Rodrigues-Lima, F.5    Hermann, J.6
  • 70
    • 0028929438 scopus 로고
    • Biochemical and immunohistochemical analysis of cathepsins B, H, L and D in human melanocytic tumours
    • T. Kageshita, A. Yoshii, T. Kimura, K. Maruo, T. Ono, and M. Himeno Biochemical and immunohistochemical analysis of cathepsins B, H, L and D in human melanocytic tumours Arch. Dermatol. Res. 287 1995 266 272
    • (1995) Arch. Dermatol. Res. , vol.287 , pp. 266-272
    • Kageshita, T.1    Yoshii, A.2    Kimura, T.3    Maruo, K.4    Ono, T.5    Himeno, M.6
  • 71
    • 0036657788 scopus 로고    scopus 로고
    • Correlation between laminin and cathepsin D expressions in breast carcinoma
    • W.Q. Zheng, L.M. Looi, and P.L. Cheah Correlation between laminin and cathepsin D expressions in breast carcinoma Tumori 88 2002 296 299
    • (2002) Tumori , vol.88 , pp. 296-299
    • Zheng, W.Q.1    Looi, L.M.2    Cheah, P.L.3
  • 72
    • 0030071483 scopus 로고    scopus 로고
    • Immunohistochemical localization of cathepsins D and e in human gastric cancer: A possible correlation with local invasive and metastatic activities of carcinoma cells
    • K. Matsuo, I. Kobayashi, T. Tsukuba, T. Kiyoshima, Y. Ishibashi, and A. Miyoshi Immunohistochemical localization of cathepsins D and E in human gastric cancer: a possible correlation with local invasive and metastatic activities of carcinoma cells Hum. Pathol. 27 1996 184 190
    • (1996) Hum. Pathol. , vol.27 , pp. 184-190
    • Matsuo, K.1    Kobayashi, I.2    Tsukuba, T.3    Kiyoshima, T.4    Ishibashi, Y.5    Miyoshi, A.6
  • 73
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Y. Izumi, M. Hirata, H. Hasuwa, R. Iwamoto, T. Umata, and K. Miyado A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor EMBO J. 17 1998 7260 7272
    • (1998) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6
  • 74
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • R.A. Black, and J.M. White ADAMs: focus on the protease domain Curr. Opin. Cell Biol. 10 1998 654 659
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 75
    • 0037391956 scopus 로고    scopus 로고
    • The ADAMs family of proteins: From basic studies to potential clinical applications
    • M.J. Duffy, D.J. Lynn, A.T. Lloyd, and C.M. O'Shea The ADAMs family of proteins: from basic studies to potential clinical applications Thromb. Haemost. 89 2003 622 631
    • (2003) Thromb. Haemost. , vol.89 , pp. 622-631
    • Duffy, M.J.1    Lynn, D.J.2    Lloyd, A.T.3    O'Shea, C.M.4
  • 78
    • 0032908446 scopus 로고    scopus 로고
    • Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion
    • K. Iba, R. Albrechtsen, B.J. Gilpin, F. Loechel, and U.M. Wewer Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion Am. J. Pathol. 154 1999 1489 1501
    • (1999) Am. J. Pathol. , vol.154 , pp. 1489-1501
    • Iba, K.1    Albrechtsen, R.2    Gilpin, B.J.3    Loechel, F.4    Wewer, U.M.5
  • 79
    • 0031801882 scopus 로고    scopus 로고
    • Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia
    • R. Yavari, C. Adida, P. Bray-Ward, M. Brines, and T. Xu Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia Hum. Mol. Genet. 7 1998 1161 1167
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1161-1167
    • Yavari, R.1    Adida, C.2    Bray-Ward, P.3    Brines, M.4    Xu, T.5
  • 80
    • 0030273873 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
    • L.G. Jia, K. Shimokawa, J.B. Bjarnason, and J.W. Fox Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins Toxicon 34 1996 1269 1276
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L.G.1    Shimokawa, K.2    Bjarnason, J.B.3    Fox, J.W.4
  • 81
    • 0028168017 scopus 로고
    • Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets
    • M.A. McLane, M.A. Kowalska, L. Silver, S.J. Shattil, and S. Niewiarowski Interaction of disintegrins with the alpha IIb beta 3 receptor on resting and activated human platelets Biochem. J. 301 1994 429 436
    • (1994) Biochem. J. , vol.301 , pp. 429-436
    • McLane, M.A.1    Kowalska, M.A.2    Silver, L.3    Shattil, S.J.4    Niewiarowski, S.5
  • 82
    • 0029032192 scopus 로고
    • Effect of four disintegrins on the adhesive and metastatic properties of B16F10 melanoma cells in a murine model
    • L. Beviglia, G.J. Stewart, and S. Niewiarowski Effect of four disintegrins on the adhesive and metastatic properties of B16F10 melanoma cells in a murine model Oncol. Res. 7 1995 7 20
    • (1995) Oncol. Res. , vol.7 , pp. 7-20
    • Beviglia, L.1    Stewart, G.J.2    Niewiarowski, S.3
  • 85
    • 0032559821 scopus 로고    scopus 로고
    • In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy
    • R. Masson, O. Lefebvre, A. Noel, M.E. Fahime, M.P. Chenard, and C. Wendling In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy J. Cell Biol. 140 1998 1535 1541
    • (1998) J. Cell Biol. , vol.140 , pp. 1535-1541
    • Masson, R.1    Lefebvre, O.2    Noel, A.3    Fahime, M.E.4    Chenard, M.P.5    Wendling, C.6
  • 86
    • 1642268124 scopus 로고    scopus 로고
    • Altered metastatic behavior of human breast cancer cells after experimental manipulation of matrix metalloproteinase 8 gene expression
    • V. Montel, J. Kleeman, D. Agarwal, D. Spinella, K. Kawai, and D. Tarin Altered metastatic behavior of human breast cancer cells after experimental manipulation of matrix metalloproteinase 8 gene expression Cancer Res. 64 2004 1687 1694
    • (2004) Cancer Res. , vol.64 , pp. 1687-1694
    • Montel, V.1    Kleeman, J.2    Agarwal, D.3    Spinella, D.4    Kawai, K.5    Tarin, D.6
  • 88
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • G. Bergers, R. Brekken, G. McMahon, T.H. Vu, T. Itoh, and K. Tamaki Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis Nat. Cell Biol. 2 2000 737 744
    • (2000) Nat. Cell Biol. , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    McMahon, G.3    Vu, T.H.4    Itoh, T.5    Tamaki, K.6
  • 89
    • 10744223801 scopus 로고    scopus 로고
    • Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin
    • Y. Hamano, M. Zeisberg, H. Sugimoto, J.C. Lively, Y. Maeshima, and C. Yang Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin Cancer Cell 3 2003 589 601
    • (2003) Cancer Cell , vol.3 , pp. 589-601
    • Hamano, Y.1    Zeisberg, M.2    Sugimoto, H.3    Lively, J.C.4    Maeshima, Y.5    Yang, C.6
  • 90
    • 0034721666 scopus 로고    scopus 로고
    • MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis
    • L.M. Coussens, C.L. Tinkle, D. Hanahan, and Z. Werb MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis Cell 103 2000 481 490
    • (2000) Cell , vol.103 , pp. 481-490
    • Coussens, L.M.1    Tinkle, C.L.2    Hanahan, D.3    Werb, Z.4
  • 91
    • 1642535587 scopus 로고    scopus 로고
    • Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment
    • N. Rousselet, L. Mills, D. Jean, C. Tellez, M. Bar-Eli, and R. Frade Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment Cancer Res. 64 2004 146 151
    • (2004) Cancer Res. , vol.64 , pp. 146-151
    • Rousselet, N.1    Mills, L.2    Jean, D.3    Tellez, C.4    Bar-Eli, M.5    Frade, R.6
  • 92
    • 0041426722 scopus 로고    scopus 로고
    • Immortalized mammary epithelial cells overexpressing protein kinase C gamma acquire a malignant phenotype and become tumorigenic in vivo
    • E. Mazzoni, A. Adam, E. Bal:de:Kier:Joffe, and J.A. Aguirre-Ghiso Immortalized mammary epithelial cells overexpressing protein kinase C gamma acquire a malignant phenotype and become tumorigenic in vivo Mol. Cancer Res. 1 2003 776 787
    • (2003) Mol. Cancer Res. , vol.1 , pp. 776-787
    • Mazzoni, E.1    Adam, A.2    Bal3    De4    Kier5    Joffe, E.6    Aguirre-Ghiso, J.A.7
  • 93
    • 0032510494 scopus 로고    scopus 로고
    • A causal role for E-cadherin in the transition from adenoma to carcinoma
    • A.K. Perl, P. Wilgenbus, U. Dahl, H. Semb, and G. Christofori A causal role for E-cadherin in the transition from adenoma to carcinoma Nature 392 1998 190 193
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2    Dahl, U.3    Semb, H.4    Christofori, G.5
  • 94
    • 0036152857 scopus 로고    scopus 로고
    • Enhanced pathological angiogenesis in mice lacking beta3 integrin or beta3 and beta5 integrins
    • L.E. Reynolds, L. Wyder, J.C. Lively, D. Taverna, S.D. Robinson, and X. Huang Enhanced pathological angiogenesis in mice lacking beta3 integrin or beta3 and beta5 integrins Nat. Med. 8 2002 27 34
    • (2002) Nat. Med. , vol.8 , pp. 27-34
    • Reynolds, L.E.1    Wyder, L.2    Lively, J.C.3    Taverna, D.4    Robinson, S.D.5    Huang, X.6
  • 95


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