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Volumn 3 APR, Issue , 2013, Pages

Mathematical modeling of cancer invasion: The role of membrane-bound matrix metalloproteinases

Author keywords

Cancer invasion; Extracellular matrix; Mathematical model; Membrane bound MMPs; Metalloproteinases

Indexed keywords

COLLAGEN; MATRIX METALLOPROTEINASE; PROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 84890653380     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2013.00070     Document Type: Article
Times cited : (53)

References (43)
  • 2
    • 3843079723 scopus 로고    scopus 로고
    • A history of the study of solid tumour growth: the contribution of mathematical modelling
    • Araujo, R. P., and McElwain, D. L. S. (2004). A history of the study of solid tumour growth: the contribution of mathematical modelling. Bull. Math. Biol. 66, 1039-1091.
    • (2004) Bull. Math. Biol. , vol.66 , pp. 1039-1091
    • Araujo, R.P.1    McElwain, D.L.S.2
  • 3
    • 0013916715 scopus 로고
    • Rate of growth of solid tumours as a problem of diffusion
    • Burton, A. C. (1966). Rate of growth of solid tumours as a problem of diffusion. Growth 30, 157-176.
    • (1966) Growth , vol.30 , pp. 157-176
    • Burton, A.C.1
  • 4
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A: a kinetic study
    • Butler, G. S., Butler, M. J., Atkinson, S. J., Will, H., Tamura, T., Schade van Westrum, S., et al. (1998). The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A: a kinetic study. J. Biol. Chem. 273, 871-880.
    • (1998) J. Biol. Chem. , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3    Will, H.4    Tamura, T.5    Schade van Westrum, S.6
  • 5
    • 80052344220 scopus 로고    scopus 로고
    • Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface-collagen substratum interface
    • doi:10.1371/journal.pone.0024029
    • Collier, I. E., Legant, W., Marmer, B., Lubman, O., Saffarian, S., Wakatsuki, T., et al. (2011). Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface-collagen substratum interface. PLoS ONE 6:e24029. doi:10.1371/journal.pone.0024029
    • (2011) PLoS ONE , vol.6
    • Collier, I.E.1    Legant, W.2    Marmer, B.3    Lubman, O.4    Saffarian, S.5    Wakatsuki, T.6
  • 6
    • 80053190203 scopus 로고    scopus 로고
    • Robustness analysis and behavior discrimination in enzymatic reaction networks
    • doi:10.1371/journal.pone.0024246
    • Donzé, A., Fanchon, E., Gattepaille, L. M., Maler, O., and Tracqui, P. (2011). Robustness analysis and behavior discrimination in enzymatic reaction networks. PLoS ONE 6:e24246. doi:10.1371/journal.pone.0024246
    • (2011) PLoS ONE , vol.6
    • Donzé, A.1    Fanchon, E.2    Gattepaille, L.M.3    Maler, O.4    Tracqui, P.5
  • 7
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • d'Ortho, M. P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., et al. (1997). Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250, 751.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 751
    • d'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6
  • 8
    • 0035834666 scopus 로고    scopus 로고
    • Characterization of the role of the 'MT-loop': an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases
    • English, W. R., Holtz, B., Vogt, G., Knauper, V., and Murphy, G. (2001). Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases. J. Biol. Chem. 276, 42018-42026.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42018-42026
    • English, W.R.1    Holtz, B.2    Vogt, G.3    Knauper, V.4    Murphy, G.5
  • 9
    • 1542495339 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic migration of tumour cells and leucocytes
    • Friedl, P., and Wolf, K. (2003). Proteolytic and non-proteolytic migration of tumour cells and leucocytes. Biochem. Soc. Symp. 70, 277-285.
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 277-285
    • Friedl, P.1    Wolf, K.2
  • 10
    • 38649104788 scopus 로고    scopus 로고
    • Mathematical modelling of cancer cell invasion of tissue: local and non-local models and the effect of adhesion
    • Gerisch, A., and Chaplain, M. A. (2008). Mathematical modelling of cancer cell invasion of tissue: local and non-local models and the effect of adhesion. J. Theor. Biol. 250, 684-704.
    • (2008) J. Theor. Biol. , vol.250 , pp. 684-704
    • Gerisch, A.1    Chaplain, M.A.2
  • 11
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., and Weinberg, R. A. (2000). The hallmarks of cancer. Cell 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 12
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan, D., and Weinberg, R. A. (2011). Hallmarks of cancer: the next generation. Cell 144, 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 13
    • 84861167206 scopus 로고    scopus 로고
    • Establishment and validation of computational model for MT1-MMP dependent ECM degradation and intervention strategies
    • doi:10.1371/journal.pcbi.1002479
    • Hoshino, D., Koshikawa, N., Suzuki, T., Quaranta, V., Weaver, A. M., Seiki, M., et al. (2012). Establishment and validation of computational model for MT1-MMP dependent ECM degradation and intervention strategies. PLoS Comput. Biol. 8:e1002479. doi:10.1371/journal.pcbi.1002479
    • (2012) PLoS Comput. Biol. , vol.8
    • Hoshino, D.1    Koshikawa, N.2    Suzuki, T.3    Quaranta, V.4    Weaver, A.M.5    Seiki, M.6
  • 14
    • 0035022861 scopus 로고    scopus 로고
    • A-Cell: graphical user interface for the construction of biochemical reaction models
    • Ichikawa, K. (2001). A-Cell: graphical user interface for the construction of biochemical reaction models. Bioinformatics 17, 483-484.
    • (2001) Bioinformatics , vol.17 , pp. 483-484
    • Ichikawa, K.1
  • 15
    • 4644236059 scopus 로고    scopus 로고
    • A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2
    • Karagiannis, E. D., and Popel, A. S. (2004). A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2. J. Biol. Chem. 279, 39105-39114.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39105-39114
    • Karagiannis, E.D.1    Popel, A.S.2
  • 16
    • 28444488632 scopus 로고    scopus 로고
    • Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: insights from a computational model
    • Karagiannis, E. D., and Popel, A. S. (2006). Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: insights from a computational model. J. Theor. Biol. 238, 124-145.
    • (2006) J. Theor. Biol. , vol.238 , pp. 124-145
    • Karagiannis, E.D.1    Popel, A.S.2
  • 17
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: regulators of the tumor microenvironment
    • Kessenbrock, K., Plaks, V., and Werb, Z. (2010). Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141, 52-67.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 18
    • 0029977810 scopus 로고    scopus 로고
    • MT-MMP, the cell surface activator of proMMP-2 (pro-gelatinase A), is expressed with its substrate in mouse tissue during embryogenesis
    • Kinoh, H., Sato, H., Tsunezuka, Y., Takino, T., Kawashima, A., Okada, Y., et al. (1996). MT-MMP, the cell surface activator of proMMP-2 (pro-gelatinase A), is expressed with its substrate in mouse tissue during embryogenesis. J. Cell. Sci. 109, 953-959.
    • (1996) J. Cell. Sci. , vol.109 , pp. 953-959
    • Kinoh, H.1    Sato, H.2    Tsunezuka, Y.3    Takino, T.4    Kawashima, A.5    Okada, Y.6
  • 20
    • 0142169378 scopus 로고    scopus 로고
    • Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism
    • Lafleur, M. A., Tester, A. M., and Thompson, E. W. (2003). Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism. FEBS Lett. 553, 457-463.
    • (2003) FEBS Lett. , vol.553 , pp. 457-463
    • Lafleur, M.A.1    Tester, A.M.2    Thompson, E.W.3
  • 21
    • 54049102110 scopus 로고    scopus 로고
    • Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase
    • Li, X. Y., Ota, I., Yana, I., Sabeh, F., and Weiss, S. J. (2008). Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase. Mol. Biol. Cell 19, 3221-3233.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3221-3233
    • Li, X.Y.1    Ota, I.2    Yana, I.3    Sabeh, F.4    Weiss, S.J.5
  • 22
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: a new challenge for proteomics
    • López-Otín, C., and Overall, C. M. (2002). Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol. 3, 509-519.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 509-519
    • López-Otín, C.1    Overall, C.M.2
  • 24
    • 69449084464 scopus 로고    scopus 로고
    • Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen
    • Martins, V. L., Vyas, J. J., Chen, M., Purdie, K., Mein, C. A., South, A. P., et al. (2009). Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen. J. Cell. Sci. 122(Pt 11), 1788-1799.
    • (2009) J. Cell. Sci. , vol.122 , Issue.PART 11 , pp. 1788-1799
    • Martins, V.L.1    Vyas, J.J.2    Chen, M.3    Purdie, K.4    Mein, C.A.5    South, A.P.6
  • 25
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase, H., and Woessner, J. F. (1999). Matrix metalloproteinases. J. Biol. Chem. 274, 21491-21494.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 26
    • 55349094310 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-2 (MMP-2) by membrane type 1 matrix metalloproteinase through an artificial receptor for proMMP-2 generates active MMP-2
    • Nishida, Y., Miyamori, H., Thompson, E. W., Takino, T., Endo, Y., and Sato, H. (2008). Activation of matrix metalloproteinase-2 (MMP-2) by membrane type 1 matrix metalloproteinase through an artificial receptor for proMMP-2 generates active MMP-2. Cancer Res. 68, 9096-9104.
    • (2008) Cancer Res. , vol.68 , pp. 9096-9104
    • Nishida, Y.1    Miyamori, H.2    Thompson, E.W.3    Takino, T.4    Endo, Y.5    Sato, H.6
  • 27
    • 84866143444 scopus 로고    scopus 로고
    • New and paradoxical roles of matrix metalloproteinases in the tumor microenvironment
    • doi:10.3389/fphar.2012.00140
    • Nöel, A., Gutiérrez-Fernández, A., Sounni, N. E., Behrendt, N., Maquoi, E., Lund, I. K., et al. (2012). New and paradoxical roles of matrix metalloproteinases in the tumor microenvironment. Front. Pharmacol. 3:140. doi:10.3389/fphar.2012.00140
    • (2012) Front. Pharmacol. , vol.3 , pp. 140
    • Nöel, A.1    Gutiérrez-Fernández, A.2    Sounni, N.E.3    Behrendt, N.4    Maquoi, E.5    Lund, I.K.6
  • 28
    • 14944357291 scopus 로고    scopus 로고
    • Development of a quantitative method to analyse tumour cell invasion in organotypic culture
    • Nyström, M. L., Thomas, G. J., Stone, M., Mackenzie, I. C., Hart, I. R., and Marshall, J. F. (2005). Development of a quantitative method to analyse tumour cell invasion in organotypic culture. J. Pathol. 205, 468-475.
    • (2005) J. Pathol. , vol.205 , pp. 468-475
    • Nyström, M.L.1    Thomas, G.J.2    Stone, M.3    Mackenzie, I.C.4    Hart, I.R.5    Marshall, J.F.6
  • 29
    • 44149123099 scopus 로고    scopus 로고
    • Collagen density promotes mammary tumor initiation and progression
    • doi:10.1186/1741-7015-6-11
    • Provenzano, P. P., Inman, D. R., Eliceiri, K. W., Knittel, J. G., Yan, L., Rueden, C. T., et al. (2008). Collagen density promotes mammary tumor initiation and progression. BMC Med. 6:11. doi:10.1186/1741-7015-6-11
    • (2008) BMC Med. , vol.6 , pp. 11
    • Provenzano, P.P.1    Inman, D.R.2    Eliceiri, K.W.3    Knittel, J.G.4    Yan, L.5    Rueden, C.T.6
  • 30
    • 77951636153 scopus 로고    scopus 로고
    • Current trends in mathematical modeling of tumor-microenvironment interactions: a survey of tools and applications
    • Rejniak, K. A., and McCawley, L. J. (2010). Current trends in mathematical modeling of tumor-microenvironment interactions: a survey of tools and applications. Exp. Biol. Med. (Maywood) 235, 411-423.
    • (2010) Exp. Biol. Med. (Maywood) , vol.235 , pp. 411-423
    • Rejniak, K.A.1    McCawley, L.J.2
  • 31
    • 70350233406 scopus 로고    scopus 로고
    • Navigating ECM barriers at the invasive front: the cancer cell-stroma interface
    • Rowe, R. G., and Weiss, S. J. (2009). Navigating ECM barriers at the invasive front: the cancer cell-stroma interface. Annu. Rev. Cell Dev. Biol. 25, 567-595.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 567-595
    • Rowe, R.G.1    Weiss, S.J.2
  • 32
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus-independent cancer cell invasion programs: three-dimensional amoeboid movement revisited
    • Sabeh, F., Shimizu-Hirota, R., and Weiss, S. J. (2009). Protease-dependent versus-independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. J. Cell Biol. 185, 11-19.
    • (2009) J. Cell Biol. , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3
  • 33
    • 12344252751 scopus 로고    scopus 로고
    • Mechanisms of cancer cell invasion
    • Sahai, E. (2005). Mechanisms of cancer cell invasion. Curr. Opin. Genet. Dev. 15, 87-96.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 87-96
    • Sahai, E.1
  • 35
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities
    • Tam, E. M., Moore, T. R., Butler, G. S., and Overall, C. M. (2004). Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J. Biol. Chem. 279, 43336-43344.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43336-43344
    • Tam, E.M.1    Moore, T.R.2    Butler, G.S.3    Overall, C.M.4
  • 36
    • 84966192535 scopus 로고
    • The histological structure of some human lung cancers and the possible implications for radiotherapy
    • Thomlinson, R. H., and Gray, L. H. (1955). The histological structure of some human lung cancers and the possible implications for radiotherapy. Br. J. Cancer 9, 539-549.
    • (1955) Br. J. Cancer , vol.9 , pp. 539-549
    • Thomlinson, R.H.1    Gray, L.H.2
  • 37
    • 0034731479 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2
    • Toth, M., Bernardo, M. M., Gervasi, D. C., Soloway, P. D., Wang, Z., Bigg, H. F., et al. (2000). Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2. J. Biol. Chem. 275, 41415-41423.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41415-41423
    • Toth, M.1    Bernardo, M.M.2    Gervasi, D.C.3    Soloway, P.D.4    Wang, Z.5    Bigg, H.F.6
  • 38
    • 84876372443 scopus 로고    scopus 로고
    • A multiscale moving boundary model arising in cancer invasion
    • Trucu, D., Lin, P., Chaplain, M., and Wang, Y. (2013). A multiscale moving boundary model arising in cancer invasion. Multiscale Model. Simul. 11, 309-335.
    • (2013) Multiscale Model. Simul. , vol.11 , pp. 309-335
    • Trucu, D.1    Lin, P.2    Chaplain, M.3    Wang, Y.4
  • 39
    • 0142117232 scopus 로고    scopus 로고
    • Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients
    • Tutton, M. G., George, M. L., Eccles, S. A., Burton, S., Swift, R. I., and Abulafi, A. M. (2003). Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients. Int. J. Cancer 107, 541-550.
    • (2003) Int. J. Cancer , vol.107 , pp. 541-550
    • Tutton, M.G.1    George, M.L.2    Eccles, S.A.3    Burton, S.4    Swift, R.I.5    Abulafi, A.M.6
  • 40
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb, Z. (1997). ECM and cell surface proteolysis: regulating cellular ecology. Cell 91, 439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 42
    • 84874965736 scopus 로고    scopus 로고
    • Resistance of corneal RFUVA-cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases
    • Zhang, Y., Mao, X., Schwend, T., Littlechild, S., and Conrad, G. W. (2013). Resistance of corneal RFUVA-cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases. Invest. Ophthalmol. Vis. Sci. 54, 1014-1025.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 1014-1025
    • Zhang, Y.1    Mao, X.2    Schwend, T.3    Littlechild, S.4    Conrad, G.W.5
  • 43
    • 0035138546 scopus 로고    scopus 로고
    • Collagen-induced proMMP-2 activation by MT1-MMP in human dermal fibroblasts and the possible role of alpha2beta1 integrins
    • Zigrino, P., Drescher, C., and Mauch, C. (2001). Collagen-induced proMMP-2 activation by MT1-MMP in human dermal fibroblasts and the possible role of alpha2beta1 integrins. Eur. J. Cell Biol. 80, 68-77.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 68-77
    • Zigrino, P.1    Drescher, C.2    Mauch, C.3


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