메뉴 건너뛰기




Volumn 15, Issue 11, 2005, Pages 1685-1734

Mathematical modelling of cancer cell invasion of tissue: The role of the urokinase plasminogen activation system

Author keywords

Chemotaxis; Haptotaxis; Reaction diffusion; Spatio temporal heterogeneity; Tumour invasion of tissue

Indexed keywords


EID: 27644463491     PISSN: 02182025     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0218202505000947     Document Type: Article
Times cited : (307)

References (129)
  • 2
    • 0033565976 scopus 로고    scopus 로고
    • Deregulation of the signaling pathways controlling urokinase production. Its relationship with the invasive phenotype
    • J. A. Aguirre Ghiso, D. F. Alonso, E. F. Farías, D. E. Gomez and E. Bal De Kier Joffè, Deregulation of the signaling pathways controlling urokinase production. Its relationship with the invasive phenotype, Euro. J. Biochem. 263 (1999) 295-304.
    • (1999) Euro. J. Biochem. , vol.263 , pp. 295-304
    • Aguirre Ghiso, J.A.1    Alonso, D.F.2    Farías, E.F.3    Gomez, D.E.4    De Bal Kier Joffè, E.5
  • 3
    • 0002460807 scopus 로고    scopus 로고
    • Tumor dormancy induced by down-regulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling
    • J. A. Aguirre Ghiso, K. Kovalsji and L. Ossowski, Tumor dormancy induced by down-regulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling, J. Cell Biol. 147 (1999) 89-103.
    • (1999) J. Cell Biol. , vol.147 , pp. 89-103
    • Aguirre Ghiso, J.A.1    Kovalsji, K.2    Ossowski, L.3
  • 4
    • 0035172910 scopus 로고    scopus 로고
    • Urokinase receptor and fibronectin regulate the EKR MARK to p38 MARK activity ratios that determine carcinoma cell proliferation or dormancy in vivo
    • J. A. Aguirre Ghiso, D. Liu, A. Mignatti, K. Kovalski and L. Ossowski, Urokinase receptor and fibronectin regulate the EKR MARK to p38 MARK activity ratios that determine carcinoma cell proliferation or dormancy in vivo, Molecular Biology of the Cell 12 (2001) 863-879.
    • (2001) Molecular Biology of the Cell , vol.12 , pp. 863-879
    • Aguirre Ghiso, J.A.1    Liu, D.2    Mignatti, A.3    Kovalski, K.4    Ossowski, L.5
  • 6
    • 25144494216 scopus 로고    scopus 로고
    • A hybrid mathematical model of solid tumour invasion: The importance of cell adhesion
    • in press
    • A. R. A. Anderson, A hybrid mathematical model of solid tumour invasion: The importance of cell adhesion, Math. Med. Biol. (in press) (2005).
    • (2005) Math. Med. Biol.
    • Anderson, A.R.A.1
  • 8
    • 0032170064 scopus 로고    scopus 로고
    • Continuous and discrete mathematical models of tumor-induced angiogenesis
    • A. R. A. Anderson and M. A. J. Chaplain, Continuous and discrete mathematical models of tumor-induced angiogenesis, Bull. Math. Biol. 60 (1998) 857-899.
    • (1998) Bull. Math. Biol. , vol.60 , pp. 857-899
    • Anderson, A.R.A.1    Chaplain, M.A.J.2
  • 10
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • P. A. Andreasen, L. Kjøller, L. Christensen and M. J. Duffy, The urokinase-type plasminogen activator system in cancer metastasis: A review, Int. J. Cancer 72 (1997) 1-22.
    • (1997) Int. J. Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjøller, L.2    Christensen, L.3    Duffy, M.J.4
  • 11
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • P. A. Andreasen, R. Egelund and H. H. Petersen, The plasminogen activation system in tumor growth, invasion, and metastasis, Cellular and Molecular Life Sci. 57 (2000) 25-40.
    • (2000) Cellular and Molecular Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 12
    • 3843079723 scopus 로고    scopus 로고
    • A history of the study of solid tumour growth: The contribution of mathematical modelling
    • R. P. Araujo and D. L. S. McElwain, A history of the study of solid tumour growth: The contribution of mathematical modelling, Bull. Math. Biol. 66 (2004) 1039-1091.
    • (2004) Bull. Math. Biol. , vol.66 , pp. 1039-1091
    • Araujo, R.P.1    McElwain, D.L.S.2
  • 13
    • 0025237471 scopus 로고
    • Signal transduction for chemotaxis and haptotaxis by matrix molecules in tumor cells
    • S. Aznavoorian, M. L. Stracke, H. Krutzsch, E. Schiffmann and L. A. Liotta, Signal transduction for chemotaxis and haptotaxis by matrix molecules in tumor cells, J. Cell Biol. 110 (1990) 1427-1438.
    • (1990) J. Cell Biol. , vol.110 , pp. 1427-1438
    • Aznavoorian, S.1    Stracke, M.L.2    Krutzsch, H.3    Schiffmann, E.4    Liotta, L.A.5
  • 16
    • 0031983123 scopus 로고    scopus 로고
    • Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression and enhanced cellular invasion by melanoma cells
    • L. M. Bafetti, T. N. Young, Y. Itoh and S. M. Stack, Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression and enhanced cellular invasion by melanoma cells, J. Biol. Chem. 273 (1998) 143-149.
    • (1998) J. Biol. Chem. , vol.273 , pp. 143-149
    • Bafetti, L.M.1    Young, T.N.2    Itoh, Y.3    Stack, S.M.4
  • 17
    • 0037418096 scopus 로고    scopus 로고
    • The modelling of the immune competition by generalized kinetic (Boltzmann) models: Review and research perspectives
    • N. Bellomo, A. Bellouquid and E. De Angelis, The modelling of the immune competition by generalized kinetic (Boltzmann) models: Review and research perspectives, Math. Compu. Model. 37 (2003) 1131-1142.
    • (2003) Math. Compu. Model. , vol.37 , pp. 1131-1142
    • Bellomo, N.1    Bellouquid, A.2    De Angelis, E.3
  • 18
    • 0029830493 scopus 로고    scopus 로고
    • Signal transduction and the u-PA/u-PAR system
    • D. Besser, P. Verde, Y. Nagamine and F. Blasi, Signal transduction and the u-PA/u-PAR system, Fibrinolysis, 10 (1996) 215-237.
    • (1996) Fibrinolysis , vol.10 , pp. 215-237
    • Besser, D.1    Verde, P.2    Nagamine, Y.3    Blasi, F.4
  • 20
    • 0023197175 scopus 로고
    • Urokinase-type plasminogen activator: Proenzyme, receptor, and inhibitors
    • F. Blasi, J-D. Vassalli and K. Danø, Urokinase-type plasminogen activator: Proenzyme, receptor, and inhibitors, J. Cell Biol. 104 (1987) 801-804.
    • (1987) J. Cell Biol. , vol.104 , pp. 801-804
    • Blasi, F.1    Vassalli, J.-D.2    Danø, K.3
  • 21
    • 0032748523 scopus 로고    scopus 로고
    • Proteolysis, cell adhesion, chemotaxis, and invasiveness are regulated by the u-PA-uPAR-PAl-1 system
    • F. Blasi, Proteolysis, cell adhesion, chemotaxis, and invasiveness are regulated by the u-PA-uPAR-PAl-1 system, Thrombosis and Haemostasis 82 (1999) 298-304.
    • (1999) Thrombosis and Haemostasis , vol.82 , pp. 298-304
    • Blasi, F.1
  • 24
    • 0028305433 scopus 로고
    • Induction of cell migration by prourokinase binding to its receptor: Possible mechanism for signal-transduction in human epithelial cells
    • N. Busso, S. K. Masur, D. Lazega, S. Waxman and L. Ossowski, Induction of cell migration by prourokinase binding to its receptor: possible mechanism for signal-transduction in human epithelial cells, J. Cell Biol. 126 (1994) 259-270.
    • (1994) J. Cell Biol. , vol.126 , pp. 259-270
    • Busso, N.1    Masur, S.K.2    Lazega, D.3    Waxman, S.4    Ossowski, L.5
  • 27
    • 0038511363 scopus 로고    scopus 로고
    • Urokinase potentiates PDGF-induced chemotaxis of human airway smooth muscle cells
    • S. M. Carlin, M. Roth and J. L. Black, Urokinase potentiates PDGF-induced chemotaxis of human airway smooth muscle cells, Amer. J. Physiol. 284 (2003) 1020-1026.
    • (2003) Amer. J. Physiol. , vol.284 , pp. 1020-1026
    • Carlin, S.M.1    Roth, M.2    Black, J.L.3
  • 28
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • P. Carmeliet and R. K. Jain, Angiogenesis in cancer and other diseases, Nature 407 (2000) 249-256.
    • (2000) Nature , vol.407 , pp. 249-256
    • Carmeliet, P.1    Jain, R.K.2
  • 29
    • 0014212671 scopus 로고
    • Haptotaxis and the mechanism of cell motility
    • S. B. Carter, Haptotaxis and the mechanism of cell motility, Nature 213 (1967) 256-260.
    • (1967) Nature , vol.213 , pp. 256-260
    • Carter, S.B.1
  • 30
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metallo-proteinases in metastasis
    • A. F. Chambers and L. M. Matrisian, Changing views of the role of matrix metallo-proteinases in metastasis, J. Nat. Cancer Inst. 89 (1997) 1260-1270.
    • (1997) J. Nat. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 31
    • 0036674501 scopus 로고    scopus 로고
    • Dissemination and growth of cancer cells in metastatic sites
    • A. F. Chambers, A. C. Groom and I. C. MacDonald, Dissemination and growth of cancer cells in metastatic sites, Nature Rev. 2 (2002) 563-572.
    • (2002) Nature Rev. , vol.2 , pp. 563-572
    • Chambers, A.F.1    Groom, A.C.2    MacDonald, I.C.3
  • 32
    • 0029422302 scopus 로고
    • The mathematical modelling of tumour angiogenesis and invasion
    • M. A. J. Chaplain, The mathematical modelling of tumour angiogenesis and invasion, Acta Biotheor. 43 (1995) 387-402.
    • (1995) Acta Biotheor. , vol.43 , pp. 387-402
    • Chaplain, M.A.J.1
  • 33
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • H. A. Chapman, Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration, Current Opinion in Cell Biol. 9 (1997) 714-724.
    • (1997) Current Opinion in Cell Biol. , vol.9 , pp. 714-724
    • Chapman, H.A.1
  • 34
    • 0030765564 scopus 로고    scopus 로고
    • Plasmin induces the formation of multicellular spheroids of breast cancer cells
    • M. H. Chun, Plasmin induces the formation of multicellular spheroids of breast cancer cells, Cancer Lett. 117 (1997) 51-56.
    • (1997) Cancer Lett. , vol.117 , pp. 51-56
    • Chun, M.H.1
  • 37
    • 0029079407 scopus 로고
    • The urokinase/urokinase-receptor system and cancer-invasion
    • M. Conese and F. Blasi, The urokinase/urokinase-receptor system and cancer-invasion, Baillière's Clin. Haematology 8 (1995) 365-389.
    • (1995) Baillière's Clin. Haematology , vol.8 , pp. 365-389
    • Conese, M.1    Blasi, F.2
  • 38
    • 0029257171 scopus 로고
    • Urokinase/urokinase receptor system: Internalization/degradation of urokinase-serpin complexes. Mechanism and regulation
    • M. Conese and F. Blasi, Urokinase/urokinase receptor system: Internalization/degradation of urokinase-serpin complexes. Mechanism and regulation, Biol. Chem. Hoppe-Seyler 376 (1995) 143-155.
    • (1995) Biol. Chem. Hoppe-seyler , vol.376 , pp. 143-155
    • Conese, M.1    Blasi, F.2
  • 39
    • 0014598110 scopus 로고
    • The measurement of cell adhesiveness by an absolute method
    • A. S. G. Curtis, The measurement of cell adhesiveness by an absolute method, J. Embryol. Exp. Morphol. 22 (1969) 305-325.
    • (1969) J. Embryol. Exp. Morphol. , vol.22 , pp. 305-325
    • Curtis, A.S.G.1
  • 40
    • 0037416209 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins
    • R.-P. Czekay, K. Aertgeerts, S. A. Curriden and D. J. Loskutoff, Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins, J. Cell Biol 160 (2003) 781-791.
    • (2003) J. Cell Biol , vol.160 , pp. 781-791
    • Czekay, R.-P.1    Aertgeerts, K.2    Curriden, S.A.3    Loskutoff, D.J.4
  • 42
    • 0027994264 scopus 로고
    • The urokinase receptor. Protein structure and role in plasminogen activation and cancer invasion
    • K. Danø, N. Behrendt, N. Brunner, V. Ellis, M. Ploug and C. Pyke, The urokinase receptor. Protein structure and role in plasminogen activation and cancer invasion, Fibrinolysis 8 (Suppl. 1) (1994) 189-203.
    • (1994) Fibrinolysis , vol.8 , Issue.SUPPL. 1 , pp. 189-203
    • Danø, K.1    Behrendt, N.2    Brunner, N.3    Ellis, V.4    Ploug, M.5    Pyke, C.6
  • 43
    • 0035848682 scopus 로고    scopus 로고
    • 3 integrin induce chemotaxis and cytoskeleton reorganization through different signaling pathways
    • 3 integrin induce chemotaxis and cytoskeleton reorganization through different signaling pathways, Oncogens. 20 (2001) 2032-2043.
    • (2001) Oncogens. , vol.20 , pp. 2032-2043
    • Degryse, B.1    Orlando, S.2    Resnati, M.3    Rabbani, S.A.4    Blasi, F.5
  • 44
    • 0029816265 scopus 로고    scopus 로고
    • Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?
    • G. Deng, S. A. Curriden, S. Wang, S. Rosenberg and D. J. Loskutoff, Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?, J. Cell Biol. 134 (1996) 1563-1571.
    • (1996) J. Cell Biol. , vol.134 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5
  • 45
    • 0033026635 scopus 로고    scopus 로고
    • Urokinase plasminogen activator: A prognostic marker in multiple types of cancer
    • M. J. Duffy, Urokinase plasminogen activator: A prognostic marker in multiple types of cancer, J. Surg. Oncol. 71 (1999) 130-135.
    • (1999) J. Surg. Oncol. , vol.71 , pp. 130-135
    • Duffy, M.J.1
  • 46
    • 0034968363 scopus 로고    scopus 로고
    • Clinical uses of tumor markers: A critical review
    • M. J. Duffy, Clinical uses of tumor markers: A critical review, Critical Rev. Clinical Lab. Sci. 38 (2001) 225-262.
    • (2001) Critical Rev. Clinical Lab. Sci. , vol.38 , pp. 225-262
    • Duffy, M.J.1
  • 48
    • 0025883277 scopus 로고
    • Plasminogen activation by receptor-bound urokinase a kinetic study with both cell-associated and isolated receptor
    • V. Ellis and K. Danø, Plasminogen activation by receptor-bound urokinase a kinetic study with both cell-associated and isolated receptor, J. Biol. Chem. 266 (1991) 12752-12758.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12752-12758
    • Ellis, V.1    Danø, K.2
  • 49
    • 0029886219 scopus 로고    scopus 로고
    • Functional analysis of the cellular receptor for urokinase in plasminogen activation
    • V. Ellis, Functional analysis of the cellular receptor for urokinase in plasminogen activation, J. Biol. Chem. 271 (1996) 14799-14784.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14799-114784
    • Ellis, V.1
  • 50
    • 0033547790 scopus 로고    scopus 로고
    • Assembly of urokinase receptor-mediated plasminogen activation complexes involves direct, non-active-site interactions between urokinase and plasminogen
    • V. Ellis, S. A. Whawell, F. Werner and J. J. Deadman, Assembly of urokinase receptor-mediated plasminogen activation complexes involves direct, non-active-site interactions between urokinase and plasminogen, Biochem. 38 (1999) 651-659.
    • (1999) Biochem. , vol.38 , pp. 651-659
    • Ellis, V.1    Whawell, S.A.2    Werner, F.3    Deadman, J.J.4
  • 51
    • 0031463337 scopus 로고    scopus 로고
    • A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity
    • F. Fazioli, M. Resnati, N. Sidenius, Y. Higashimoto, E. Appella and F. Blasi, A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity, The EMBO J. 16 (1997) 7279-7286.
    • (1997) The EMBO J. , vol.16 , pp. 7279-7286
    • Fazioli, F.1    Resnati, M.2    Sidenius, N.3    Higashimoto, Y.4    Appella, E.5    Blasi, F.6
  • 52
    • 0026236394 scopus 로고
    • The biology of cancer metastasis or, "you cannot fix it if you do not know how it works"
    • I. J. Fidler, The biology of cancer metastasis or, "you cannot fix it if you do not know how it works", Bioessays 13 (1991) 551-554.
    • (1991) Bioessays , vol.13 , pp. 551-554
    • Fidler, I.J.1
  • 53
    • 0041769409 scopus 로고    scopus 로고
    • The pathogenesis of cancer metastasis: The "seed and soil" hypothesis revisited
    • I. J. Fidler, The pathogenesis of cancer metastasis: the "seed and soil" hypothesis revisited, Nature Rev. 3 (2002) 1-6.
    • (2002) Nature Rev. , vol.3 , pp. 1-6
    • Fidler, I.J.1
  • 54
    • 0016007951 scopus 로고
    • Tumour angiogenesis
    • J. Folkman, Tumour angiogenesis, Adv. Cancer Res. 19 (1974) 331-358.
    • (1974) Adv. Cancer Res. , vol.19 , pp. 331-358
    • Folkman, J.1
  • 55
    • 0016957980 scopus 로고
    • The vascularization of tumours
    • J. Folkman, The vascularization of tumours, Sci. Amer. 234 (1976) 58-73.
    • (1976) Sci. Amer. , vol.234 , pp. 58-73
    • Folkman, J.1
  • 56
    • 0023157363 scopus 로고
    • Angiogenic factors
    • J. Folkman and M. Klagsbrun, Angiogenic factors, Science 235 (1987) 442-447.
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsbrun, M.2
  • 58
    • 0028882787 scopus 로고
    • Models of tumour-host interaction as competing populations: Implications for tumor biology and treatment
    • R. A. Gatenby, Models of tumour-host interaction as competing populations: Implications for tumor biology and treatment, J. Theor. Biol. 176 (1995) 447-455.
    • (1995) J. Theor. Biol. , vol.176 , pp. 447-455
    • Gatenby, R.A.1
  • 59
    • 0029751950 scopus 로고    scopus 로고
    • A reaction-diffusion model of cancer invasion
    • R. A. Gatenby and E. T. Gawlinski, A reaction-diffusion model of cancer invasion, Cancer Res. 56 (1996) 5745-5753.
    • (1996) Cancer Res. , vol.56 , pp. 5745-5753
    • Gatenby, R.A.1    Gawlinski, E.T.2
  • 62
    • 0032508679 scopus 로고    scopus 로고
    • Multicellular spheroids as an in vitro model
    • G. Hamilton, Multicellular spheroids as an in vitro model, Cancer Lett. 131 (1998) 29-34.
    • (1998) Cancer Lett. , vol.131 , pp. 29-34
    • Hamilton, G.1
  • 63
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • D. Hanahan and R. A. Weinberg, The hallmarks of cancer, Cell 100 (2000) 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 65
    • 0032812916 scopus 로고    scopus 로고
    • Mathematical and experimental analysis of localization of anti-tumour anti-body-enzyme conjugates
    • T. L. Jackson, S. R. Lubkin, S. R. Siemens, N. O. Kerr, P. D. Senter and J. D. Murray, Mathematical and experimental analysis of localization of anti-tumour anti-body-enzyme conjugates, British J. Cancer 80 (1999) 1747-1753.
    • (1999) British J. Cancer , vol.80 , pp. 1747-1753
    • Jackson, T.L.1    Lubkin, S.R.2    Siemens, S.R.3    Kerr, N.O.4    Senter, P.D.5    Murray, J.D.6
  • 66
    • 0027361935 scopus 로고
    • Expression and localization of elements of the plasminogen activation system in benign breast disease and breast cancers
    • J. Jankun, H. W. Merrick and P. J. Goldblatt, Expression and localization of elements of the plasminogen activation system in benign breast disease and breast cancers, J. Cellular Biochem. 53 (1993) 135-144.
    • (1993) J. Cellular Biochem. , vol.53 , pp. 135-144
    • Jankun, J.1    Merrick, H.W.2    Goldblatt, P.J.3
  • 67
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin-binding protein on endothelial cells
    • S. M. Kanse, C. Kost, O. G. Wilhelm, P. A. Andreasen and K. T. Preissner, The urokinase receptor is a major vitronectin-binding protein on endothelial cells, Exp. Cell Res. 224 (1996) 344-353.
    • (1996) Exp. Cell Res. , vol.224 , pp. 344-353
    • Kanse, S.M.1    Kost, C.2    Wilhelm, O.G.3    Andreasen, P.A.4    Preissner, K.T.5
  • 68
    • 0020926236 scopus 로고
    • 11th R. A. Fisher memorial lecture - Kin selection and altruism
    • S. Karlin, 11th R. A. Fisher Memorial Lecture - Kin Selection and Altruism, Proc. Roy. Soc. London 219 (1983) 327-353.
    • (1983) Proc. Roy. Soc. London , vol.219 , pp. 327-353
    • Karlin, S.1
  • 70
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin-and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • L. Kjøller, S. M. Kanse, T. Kirkegaard, K. W. Rodenburg, E. Rønne, S. L. Goodmann, K. T. Preissner, L. Ossowski and P. A. Andreasen, Plasminogen activator inhibitor-1 represses integrin-and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation, Exp. Cell Res. 232 (1997) 420-429.
    • (1997) Exp. Cell Res. , vol.232 , pp. 420-429
    • Kjøller, L.1    Kanse, S.M.2    Kirkegaard, T.3    Rodenburg, K.W.4    Rønne, E.5    Goodmann, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 71
    • 0037622867 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility
    • L. Kjøller, The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility, Biol. Chem. 383 (2002) 5-19.
    • (2002) Biol. Chem. , vol.383 , pp. 5-19
    • Kjøller, L.1
  • 72
    • 0028944106 scopus 로고
    • Molecular insights into cancer invasion: Strategies for prevention and intervention
    • E. C. Kohn and L. A. Liotta, Molecular insights into cancer invasion: Strategies for prevention and intervention, Cancer Res. 51 (1995) 1856-1862.
    • (1995) Cancer Res. , vol.51 , pp. 1856-1862
    • Kohn, E.C.1    Liotta, L.A.2
  • 73
    • 27644503155 scopus 로고    scopus 로고
    • Micro and meso scales of description corresponding to a model of tissue invasion by solid tumours
    • to appear
    • L. Lachowicz, Micro and meso scales of description corresponding to a model of tissue invasion by solid tumours, Math. Mod. Meth. Appl. Sci. to appear, (2005).
    • (2005) Math. Mod. Meth. Appl. Sci.
    • Lachowicz, L.1
  • 75
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • D. A. Lauffenburger and A. F. Horwitz, Cell migration: A physically integrated molecular process, Cell 84 (1996) 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 76
    • 0022656975 scopus 로고
    • Tumour invasion and metastases: Role of the extracellular matrix
    • L. A. Liotta, Tumour invasion and metastases: role of the extracellular matrix, Cancer Res. 46 (1986) 1-7.
    • (1986) Cancer Res. , vol.46 , pp. 1-7
    • Liotta, L.A.1
  • 77
    • 0026425631 scopus 로고
    • Tumor invasion and metastasis as targets for cancer therapy
    • L. A. Liotta and W. G. Stetler-Stevenson, Tumor invasion and metastasis as targets for cancer therapy, Cancer Res. 51 (1991) 5054-5059.
    • (1991) Cancer Res. , vol.51 , pp. 5054-5059
    • Liotta, L.A.1    Stetler-Stevenson, W.G.2
  • 78
    • 0034682170 scopus 로고    scopus 로고
    • Checkpoint for invasion
    • L. A. Liotta, and T. Clair, Checkpoint for invasion, Nature 405 (2000) 287-288.
    • (2000) Nature , vol.405 , pp. 287-288
    • Liotta, L.A.1    Clair, T.2
  • 81
    • 1642348723 scopus 로고    scopus 로고
    • Mathematical modelling of the spatio-temporal response of cytotoxic T-lymphocytes to a solid tumour
    • A. Matzavinos, M. A. J. Chaplain and V. A. Kuznetsov, Mathematical modelling of the spatio-temporal response of cytotoxic T-lymphocytes to a solid tumour, Math. Med. Biol. IMA 21 (2004) 1-34.
    • (2004) Math. Med. Biol. IMA , vol.21 , pp. 1-34
    • Matzavinos, A.1    Chaplain, M.A.J.2    Kuznetsov, V.A.3
  • 82
    • 8744228986 scopus 로고    scopus 로고
    • Travelling-wave analysis of a model of the immune response to cancer
    • A. Matzavinos and M. A. J. Chaplain, Travelling-wave analysis of a model of the immune response to cancer, C.R. Biol. 327 (2004) 995-1008.
    • (2004) C.R. Biol. , vol.327 , pp. 995-1008
    • Matzavinos, A.1    Chaplain, M.A.J.2
  • 83
    • 0020588997 scopus 로고
    • Migration by haptotaxis of a Schwann cell tumor line to the basement membrane glycoprotein laminin
    • J. B. McCarthy, S. L. Palm and L. T. Furcht, Migration by haptotaxis of a Schwann cell tumor line to the basement membrane glycoprotein laminin, J. Cell Biol. 97 (1983) 772-777.
    • (1983) J. Cell Biol. , vol.97 , pp. 772-777
    • McCarthy, J.B.1    Palm, S.L.2    Furcht, L.T.3
  • 84
    • 0022650891 scopus 로고
    • Human fibronectin contains distinct adhesion- And motility-promoting domains for metastatic melanoma cells
    • J. B. McCarthy, S. T. Hagen and L. T. Furcht. Human fibronectin contains distinct adhesion- and motility-promoting domains for metastatic melanoma cells, J. Cell Biol. 102 (1986) 179-188.
    • (1986) J. Cell Biol. , vol.102 , pp. 179-188
    • McCarthy, J.B.1    Hagen, S.T.2    Furcht, L.T.3
  • 85
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • P. Mignatti and D. B. Rifkin, Biology and biochemistry of proteinases in tumor invasion, Physio. Rev. 73 (1993) 161-195.
    • (1993) Physio. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 86
    • 0033556795 scopus 로고    scopus 로고
    • Biological significance of the expression of urokinase-type plasminogen activator receptors (uPARs) in brain tumors
    • S. Mohanam, C. L. Gladson, C. N. Rao and J. S. Rao, Biological significance of the expression of urokinase-type plasminogen activator receptors (uPARs) in brain tumors, Frontiers in Biosci. 4 (1999) 178-187.
    • (1999) Frontiers in Biosci. , vol.4 , pp. 178-187
    • Mohanam, S.1    Gladson, C.L.2    Rao, C.N.3    Rao, J.S.4
  • 88
    • 0031305690 scopus 로고    scopus 로고
    • The optimal scheduling of two drugs with simple resistance for a problem in cancer chemotherapy
    • J. D. Murray, The optimal scheduling of two drugs with simple resistance for a problem in cancer chemotherapy, IMA J. Math. Appl. Med. Biol. 4 (1997) 283-303.
    • (1997) IMA J. Math. Appl. Med. Biol. , vol.4 , pp. 283-303
    • Murray, J.D.1
  • 89
    • 0027272044 scopus 로고
    • Kinetics of inactivation of α-thrombin by plasminogen activator inhibitor-1
    • M. C. Naski, D. A. Lawrence, D. F. Mosher, T. J. Podor and D. Ginsburg, Kinetics of inactivation of α-thrombin by plasminogen activator inhibitor-1, J. Biol. Chem. 268 (1993) 12367-12372.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12367-12372
    • Naski, M.C.1    Lawrence, D.A.2    Mosher, D.F.3    Podor, T.J.4    Ginsburg, D.5
  • 90
    • 0032478829 scopus 로고    scopus 로고
    • Binding of urokinase-type plasminogen activator to its receptor in MCF-7 cells activates extracellular signal-regulated kinase 1 and 2 which is required for increased cellular motility
    • D. H. D. Nguyen, I. M. Hussaini and S. L. Gonias, Binding of urokinase-type plasminogen activator to its receptor in MCF-7 cells activates extracellular signal-regulated kinase 1 and 2 which is required for increased cellular motility, J. Biol. Chem. 273 (1998) 8502-8507.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8502-8507
    • Nguyen, D.H.D.1    Hussaini, I.M.2    Gonias, S.L.3
  • 94
    • 0002670122 scopus 로고    scopus 로고
    • A mathematical model of vascular tumour growth and invasion
    • M. E. Orme and M. A. J. Chaplain, A mathematical model of vascular tumour growth and invasion, Math. Comput. Model. 23 (1996) 43-60.
    • (1996) Math. Comput. Model. , vol.23 , pp. 43-60
    • Orme, M.E.1    Chaplain, M.A.J.2
  • 95
    • 0031230846 scopus 로고    scopus 로고
    • Two-dimensional models of tumour angiogenesis and anti-angiogenesis strategies
    • M. E. Orme and M. A. J. Chaplain, Two-dimensional models of tumour angiogenesis and anti-angiogenesis strategies, IMA J. Math. Appl. Med. Biol. 14 (1997) 189-205.
    • (1997) IMA J. Math. Appl. Med. Biol. , vol.14 , pp. 189-205
    • Orme, M.E.1    Chaplain, M.A.J.2
  • 96
    • 0033824172 scopus 로고    scopus 로고
    • Urokinase receptor and integrin partnership: Coordination of signaling for cell adhesion, migration and growth
    • L. Ossowski and J. A. Aguirre-Ghiso, Urokinase receptor and integrin partnership: Coordination of signaling for cell adhesion, migration and growth, Current Opinion in Cell Biol. 124 (2000) 613-620.
    • (2000) Current Opinion in Cell Biol. , vol.124 , pp. 613-620
    • Ossowski, L.1    Aguirre-Ghiso, J.A.2
  • 99
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen aetivator-plasmin systems in angiogenesis
    • M. S. Pepper, Role of the matrix metalloproteinase and plasminogen aetivator-plasmin systems in angiogenesis, Arteriosclerosis, Thrombosis and Vascular Biol. 21 (2001) 1104-1117.
    • (2001) Arteriosclerosis, Thrombosis and Vascular Biol. , vol.21 , pp. 1104-1117
    • Pepper, M.S.1
  • 100
    • 0034923623 scopus 로고    scopus 로고
    • Extracellular proteolysis and angiogenesis
    • M. S. Pepper, Extracellular proteolysis and angiogenesis, Thrombolysis and Haemostasis, 86 (2001) 346-355.
    • (2001) Thrombolysis and Haemostasis , vol.86 , pp. 346-355
    • Pepper, M.S.1
  • 103
    • 0032767250 scopus 로고    scopus 로고
    • Extracellular matrix concentration exerts selection pressure on invasive cells
    • A. J. Perumpanani and H. M. Byrne, Extracellular matrix concentration exerts selection pressure on invasive cells, Euro. J. Cancer 35 (1999) 1274-1280.
    • (1999) Euro. J. Cancer , vol.35 , pp. 1274-1280
    • Perumpanani, A.J.1    Byrne, H.M.2
  • 105
    • 0030782196 scopus 로고    scopus 로고
    • Structure, function and expression on blood and bone marrow cells of the urokinase-type plasminogen activator receptor, uPAR
    • T. Plesner, N. Behrendt and M. Ploug, Structure, function and expression on blood and bone marrow cells of the urokinase-type plasminogen activator receptor, uPAR, STEM Cells 15 (1997) 398-408.
    • (1997) STEM Cells , vol.15 , pp. 398-408
    • Plesner, T.1    Behrendt, N.2    Ploug, M.3
  • 106
    • 0034682778 scopus 로고    scopus 로고
    • New insights into the size and stoichiometry of the plasminogen activator inhibitor type-1/vitronectin complex
    • T. J. Podor, S. G. Shaughnessy, M. N. Blackburn and C. B. Peterson, New insights into the size and stoichiometry of the plasminogen activator inhibitor type-1/vitronectin complex, J. Biol. Chem. 275 (2000) 25402-25410.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25402-25410
    • Podor, T.J.1    Shaughnessy, S.G.2    Blackburn, M.N.3    Peterson, C.B.4
  • 110
    • 85088549883 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • M. Resnati, M. Guttinger, S. Valcamonica, N. Sidenius, F. Blasi and F. Fazioli, Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect, EMBO J. 9 (1996) 467-470.
    • (1996) EMBO J. , vol.9 , pp. 467-470
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6
  • 111
    • 8044238033 scopus 로고
    • Further studies on the purification and characterization of human plasminogen and plasmin
    • K. C. Robbins, L. Summaria, D. Elwyn and G. H. Barlow, Further studies on the purification and characterization of human plasminogen and plasmin, J. Biol. Chem. 240 (1965) 541-550.
    • (1965) J. Biol. Chem. , vol.240 , pp. 541-550
    • Robbins, K.C.1    Summaria, L.2    Elwyn, D.3    Barlow, G.H.4
  • 113
    • 0026773381 scopus 로고
    • Oncogenes, anti-oncogenes and the immune response to cancer: A mathematical model
    • J. A. Sherratt and M. A. Nowak, Oncogenes, anti-oncogenes and the immune response to cancer: A mathematical model, Proc. of the. Roy. Soc. London, Ser. B 248 (1992) 261-271.
    • (1992) Proc. of The. Roy. Soc. London, Ser. B , vol.248 , pp. 261-271
    • Sherratt, J.A.1    Nowak, M.A.2
  • 114
    • 0025882274 scopus 로고
    • Migration of individual microvessel endothelial cells: Stochastic model and parameter measurement
    • C. L. Stokes, D. A. Lauffenburger and S. K. Williams, Migration of individual microvessel endothelial cells: stochastic model and parameter measurement, J. Cell Sci. 99 (1991) 419-430.
    • (1991) J. Cell Sci. , vol.99 , pp. 419-430
    • Stokes, C.L.1    Lauffenburger, D.A.2    Williams, S.K.3
  • 115
    • 0025991093 scopus 로고
    • Analysis of the roles of microvessel endothelial cell random motility and chemotaxis in angiogenesis
    • C. L. Stokes and D. Lauffenburger, Analysis of the roles of microvessel endothelial cell random motility and chemotaxis in angiogenesis, J. Theor. Biol. 152 (1991) 377-403.
    • (1991) J. Theor. Biol. , vol.152 , pp. 377-403
    • Stokes, C.L.1    Lauffenburger, D.2
  • 116
    • 0033199022 scopus 로고    scopus 로고
    • Stochastic simulation of benign avascular tumour growth using the Potts model
    • E. L. Stott, N. F. Britton, J. A. Glazier and M. Zajac, Stochastic simulation of benign avascular tumour growth using the Potts model, Math. Comput. Model. 30 (1999) 183-198.
    • (1999) Math. Comput. Model. , vol.30 , pp. 183-198
    • Stott, E.L.1    Britton, N.F.2    Glazier, J.A.3    Zajac, M.4
  • 118
    • 8744271007 scopus 로고    scopus 로고
    • Analysis of immunotherapy models in the context of cancer dynamics
    • Z. Szymańska, Analysis of immunotherapy models in the context of cancer dynamics, Appl. Math. Comput. Sci. 13 (2003) 407-418.
    • (2003) Appl. Math. Comput. Sci. , vol.13 , pp. 407-418
    • Szymańska, Z.1
  • 119
    • 0033752019 scopus 로고    scopus 로고
    • A quantitative model for differential motility of gliomas in grey and white matter
    • K. R. Swanson, E. C. Alvord and J. D. Murray, A quantitative model for differential motility of gliomas in grey and white matter, Cell Proliferation 33 (2000) 317-329.
    • (2000) Cell Proliferation , vol.33 , pp. 317-329
    • Swanson, K.R.1    Alvord, E.C.2    Murray, J.D.3
  • 120
    • 0031942989 scopus 로고    scopus 로고
    • Expression of the plasminogen activation system in kidney cancer correlates with its aggressive phenotype
    • R. Swiercz, J. D. Wolfe, A. Zaher and J. Jankun, Expression of the plasminogen activation system in kidney cancer correlates with its aggressive phenotype, Clin. Cancer Res. 4 (1998) 869-877.
    • (1998) Clin. Cancer Res. , vol.4 , pp. 869-877
    • Swiercz, R.1    Wolfe, J.D.2    Zaher, A.3    Jankun, J.4
  • 121
    • 0035830838 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor (CD87) is a ligand for integrins and mediates cell-cell interaction
    • T. Tarui, A. P. Mazar, D. B. Cines and Y. Takada, Urokinase-type plasminogen activator receptor (CD87) is a ligand for integrins and mediates cell-cell interaction, J. Biol. Chem. 276 (2001) 3983-3990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3983-3990
    • Tarui, T.1    Mazar, A.P.2    Cines, D.B.3    Takada, Y.4
  • 122
    • 0036304182 scopus 로고    scopus 로고
    • Intercellular adhesion and cancer invasion: A discrete simulation using the extended Potts model
    • S. Turner and J. A. Sherratt, intercellular adhesion and cancer invasion: A discrete simulation using the extended Potts model, J. Theor. Biol. 216 (2002) 85-100.
    • (2002) J. Theor. Biol. , vol.216 , pp. 85-100
    • Turner, S.1    Sherratt, J.A.2
  • 123
    • 0028334672 scopus 로고
    • Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
    • D. A. Waltz and H. A. Chapman, Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy, J. Biol. Chem. 269 (1994) 14746-14750.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14746-14750
    • Waltz, D.A.1    Chapman, H.A.2
  • 124
    • 0030757506 scopus 로고    scopus 로고
    • Plasmin and plasminogen activator inhibitor type 1 promote cellular motility by regulating the interaction between the urokinase receptor and vitronectin
    • D. A. Waltz, L. R. Natkin, R. M. Fujita, Y. Wei and H. A. Chapman, Plasmin and plasminogen activator inhibitor type 1 promote cellular motility by regulating the interaction between the urokinase receptor and vitronectin, J. Clin. Investigation 100 (1997) 58-67.
    • (1997) J. Clin. Investigation , vol.100 , pp. 58-67
    • Waltz, D.A.1    Natkin, L.R.2    Fujita, R.M.3    Wei, Y.4    Chapman, H.A.5
  • 125
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Y. Wei, D. A. Waltz, N. Rao, R. J. Drummond, S. Rosenberg and H. A. Chapman, Identification of the urokinase receptor as an adhesion receptor for vitronectin, J. Biol. Chem. 269 (1994) 32380-32388.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 126
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • Y. Wei, X. Yang, Q. Liu, J. A. Wilkins and H. A. Chapman, A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling, J. Cell Biol. 144 (1999) 1285-1294.
    • (1999) J. Cell Biol. , vol.144 , pp. 1285-1294
    • Wei, Y.1    Yang, X.2    Liu, Q.3    Wilkins, J.A.4    Chapman, H.A.5
  • 127
    • 0033581184 scopus 로고    scopus 로고
    • What defines a useful marker of metastasis in human cancer?
    • D. R. Welch and C. W. Rinker-Schaeffer, What defines a useful marker of metastasis in human cancer?, J. Nat. Cancer Inst. 91 (1999) 1351-1353.
    • (1999) J. Nat. Cancer Inst. , vol.91 , pp. 1351-1353
    • Welch, D.R.1    Rinker-Schaeffer, C.W.2
  • 128
    • 0033542781 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator binding to its receptor stimulates tumor cell migration by enhancing integrin-mediated signal transduction
    • M. Yebra, L. Goretzki, M. Pfeifer and B. M. Mueller, Urokinase-type plasminogen activator binding to its receptor stimulates tumor cell migration by enhancing integrin-mediated signal transduction, Exp. Cell Res. 250 (1999) 231-240.
    • (1999) Exp. Cell Res. , vol.250 , pp. 231-240
    • Yebra, M.1    Goretzki, L.2    Pfeifer, M.3    Mueller, B.M.4
  • 129
    • 0030956119 scopus 로고    scopus 로고
    • Reduction in surface urokinase receptor forces malignant cells into a protracted state of dormancy
    • W. Yu, J. Kim and L. Ossowski, Reduction in surface urokinase receptor forces malignant cells into a protracted state of dormancy, J. Cell Biol. 137 (1997) 767-777.
    • (1997) J. Cell Biol. , vol.137 , pp. 767-777
    • Yu, W.1    Kim, J.2    Ossowski, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.