메뉴 건너뛰기




Volumn 21, Issue 12, 2011, Pages 736-744

Extracellular matrix determinants of proteolytic and non-proteolytic cell migration

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN; MATRIX METALLOPROTEINASE; SERINE PROTEINASE;

EID: 81355127254     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2011.09.006     Document Type: Review
Times cited : (274)

References (95)
  • 1
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: regulators of the tumor microenvironment
    • Kessenbrock K., et al. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 2010, 141:52-67.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1
  • 2
    • 77955928161 scopus 로고    scopus 로고
    • Tumors as organs: complex tissues that interface with the entire organism
    • Egeblad M., et al. Tumors as organs: complex tissues that interface with the entire organism. Dev. Cell 2010, 18:884-901.
    • (2010) Dev. Cell , vol.18 , pp. 884-901
    • Egeblad, M.1
  • 3
    • 61649119071 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase is a crucial promoter of synovial invasion in human rheumatoid arthritis
    • Miller M.C., et al. Membrane type 1 matrix metalloproteinase is a crucial promoter of synovial invasion in human rheumatoid arthritis. Arthritis Rheum. 2009, 60:686-697.
    • (2009) Arthritis Rheum. , vol.60 , pp. 686-697
    • Miller, M.C.1
  • 4
    • 75749157368 scopus 로고    scopus 로고
    • Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: ready for prime time?
    • Zucker S., Cao J. Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: ready for prime time?. Cancer Biol. Ther. 2009, 8:2371-2373.
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 2371-2373
    • Zucker, S.1    Cao, J.2
  • 5
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf K., et al. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J. Cell Biol. 2003, 160:267-277.
    • (2003) J. Cell Biol. , vol.160 , pp. 267-277
    • Wolf, K.1
  • 6
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited
    • Sabeh F., et al. Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. J. Cell Biol. 2009, 185:11-19.
    • (2009) J. Cell Biol. , vol.185 , pp. 11-19
    • Sabeh, F.1
  • 7
    • 32944459251 scopus 로고    scopus 로고
    • Matrix metalloproteinases: roles in cancer and metastasis
    • Fingleton B. Matrix metalloproteinases: roles in cancer and metastasis. Front. Biosci. 2006, 11:479-491.
    • (2006) Front. Biosci. , vol.11 , pp. 479-491
    • Fingleton, B.1
  • 8
    • 75749146306 scopus 로고    scopus 로고
    • Plasticity of cell migration: a multiscale tuning model
    • Friedl P., Wolf K. Plasticity of cell migration: a multiscale tuning model. J. Cell Biol. 2010, 188:11-19.
    • (2010) J. Cell Biol. , vol.188 , pp. 11-19
    • Friedl, P.1    Wolf, K.2
  • 9
    • 68549130679 scopus 로고    scopus 로고
    • Proteolytic interstitial cell migration: a five-step process
    • Friedl P., Wolf K. Proteolytic interstitial cell migration: a five-step process. Cancer Metastasis Rev. 2009, 28:129-135.
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 129-135
    • Friedl, P.1    Wolf, K.2
  • 10
    • 33645507413 scopus 로고    scopus 로고
    • Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function
    • Artym V.V., et al. Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res. 2006, 66:3034-3043.
    • (2006) Cancer Res. , vol.66 , pp. 3034-3043
    • Artym, V.V.1
  • 11
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf K., et al. Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat. Cell Biol. 2007, 9:893-904.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 893-904
    • Wolf, K.1
  • 12
    • 58149288221 scopus 로고    scopus 로고
    • Direct visualization of protease activity on cells migrating in three-dimensions
    • Packard B.Z., et al. Direct visualization of protease activity on cells migrating in three-dimensions. Matrix Biol. 2009, 28:3-10.
    • (2009) Matrix Biol. , vol.28 , pp. 3-10
    • Packard, B.Z.1
  • 13
    • 79951553475 scopus 로고    scopus 로고
    • Nuclear mechanics during cell migration
    • Friedl P., et al. Nuclear mechanics during cell migration. Curr. Opin. Cell Biol. 2011, 23:55-64.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 55-64
    • Friedl, P.1
  • 14
    • 78650527018 scopus 로고    scopus 로고
    • The role of chromatin structure in cell migration
    • Gerlitz G., Bustin M. The role of chromatin structure in cell migration. Trends Cell Biol. 2011, 21:6-11.
    • (2011) Trends Cell Biol. , vol.21 , pp. 6-11
    • Gerlitz, G.1    Bustin, M.2
  • 15
    • 43049085527 scopus 로고    scopus 로고
    • Rapid leukocyte migration by integrin-independent flowing and squeezing
    • Lammermann T., et al. Rapid leukocyte migration by integrin-independent flowing and squeezing. Nature 2008, 453:51-55.
    • (2008) Nature , vol.453 , pp. 51-55
    • Lammermann, T.1
  • 16
    • 33846014269 scopus 로고    scopus 로고
    • Smurf1 regulates tumor cell plasticity and motility through degradation of RhoA leading to localized inhibition of contractility
    • Sahai E., et al. Smurf1 regulates tumor cell plasticity and motility through degradation of RhoA leading to localized inhibition of contractility. J. Cell Biol. 2007, 176:35-42.
    • (2007) J. Cell Biol. , vol.176 , pp. 35-42
    • Sahai, E.1
  • 17
    • 70349314647 scopus 로고    scopus 로고
    • Mechanical modes of 'amoeboid' cell migration
    • Lammermann T., Sixt M. Mechanical modes of 'amoeboid' cell migration. Curr. Opin. Cell Biol. 2009, 21:636-644.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 636-644
    • Lammermann, T.1    Sixt, M.2
  • 18
    • 79251472096 scopus 로고    scopus 로고
    • TGF-b2 induction regulates invasiveness of Theileria-transformed leukocytes and disease susceptibility
    • Chaussepied M., et al. TGF-b2 induction regulates invasiveness of Theileria-transformed leukocytes and disease susceptibility. PLoS Pathog. 2010, 6:e1001197.
    • (2010) PLoS Pathog. , vol.6
    • Chaussepied, M.1
  • 19
    • 58849106652 scopus 로고    scopus 로고
    • A tense situation: forcing tumour progression
    • Butcher D.T., et al. A tense situation: forcing tumour progression. Nat. Rev. Cancer 2009, 9:108-122.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 108-122
    • Butcher, D.T.1
  • 20
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher D.E.P., et al. Tissue cells feel and respond to the stiffness of their substrate. Science 2005, 310:1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.P.1
  • 21
    • 0242278503 scopus 로고    scopus 로고
    • Enhancing mechanical properties of tissue-engineered constructs via lysyl oxidase crosslinking activity
    • Elbjeirami W.M., et al. Enhancing mechanical properties of tissue-engineered constructs via lysyl oxidase crosslinking activity. J. Biomed. Mater. Res. A 2003, 66:513-521.
    • (2003) J. Biomed. Mater. Res. A , vol.66 , pp. 513-521
    • Elbjeirami, W.M.1
  • 22
    • 51649093104 scopus 로고    scopus 로고
    • Dependence of invadopodia function on collagen fiber spacing and cross-linking: computational modeling and experimental evidence
    • Enderling H., et al. Dependence of invadopodia function on collagen fiber spacing and cross-linking: computational modeling and experimental evidence. Biophys. J. 2008, 95:2203-2218.
    • (2008) Biophys. J. , vol.95 , pp. 2203-2218
    • Enderling, H.1
  • 23
    • 78751682352 scopus 로고    scopus 로고
    • Elucidating the role of matrix stiffness in 3D cell migration and remodeling
    • Ehrbar M., et al. Elucidating the role of matrix stiffness in 3D cell migration and remodeling. Biophys. J. 2011, 100:284-293.
    • (2011) Biophys. J. , vol.100 , pp. 284-293
    • Ehrbar, M.1
  • 24
    • 70449133451 scopus 로고    scopus 로고
    • Collagen-based cell migration models in vitro and in vivo
    • Wolf K., et al. Collagen-based cell migration models in vitro and in vivo. Semin. Cell Dev. Biol. 2009, 20:931-941.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 931-941
    • Wolf, K.1
  • 25
    • 58149332179 scopus 로고    scopus 로고
    • Contact guidance mediated three-dimensional cell migration is regulated by Rho/ROCK-dependent matrix reorganization
    • Provenzano P.P., et al. Contact guidance mediated three-dimensional cell migration is regulated by Rho/ROCK-dependent matrix reorganization. Biophys. J. 2008, 95:5374-5384.
    • (2008) Biophys. J. , vol.95 , pp. 5374-5384
    • Provenzano, P.P.1
  • 26
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental K.R., et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 2009, 139:891-906.
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1
  • 27
    • 9444242129 scopus 로고    scopus 로고
    • Apatite-mediated actin dynamics in resorbing osteoclasts
    • Saltel F., et al. Apatite-mediated actin dynamics in resorbing osteoclasts. Mol. Biol. Cell 2004, 15:5231-5241.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5231-5241
    • Saltel, F.1
  • 28
    • 0036151201 scopus 로고    scopus 로고
    • A close-up view of migrating Langerhans cells in the skin
    • Stoitzner P., et al. A close-up view of migrating Langerhans cells in the skin. J. Invest. Dermatol. 2002, 118:117-125.
    • (2002) J. Invest. Dermatol. , vol.118 , pp. 117-125
    • Stoitzner, P.1
  • 29
    • 77957221459 scopus 로고    scopus 로고
    • Dynamic interplay between the collagen scaffold and tumor evolution
    • Egeblad M., et al. Dynamic interplay between the collagen scaffold and tumor evolution. Curr. Opin. Cell Biol. 2010, 22:697-706.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 697-706
    • Egeblad, M.1
  • 30
    • 0029942667 scopus 로고    scopus 로고
    • Structural biology of the fibres of the collagenous and elastic systems
    • Montes G.S. Structural biology of the fibres of the collagenous and elastic systems. Cell Biol. Int. 1996, 20:15-27.
    • (1996) Cell Biol. Int. , vol.20 , pp. 15-27
    • Montes, G.S.1
  • 31
    • 16844378037 scopus 로고    scopus 로고
    • Collagen in the scarless fetal skin wound: detection with picrosirius-polarization
    • Cuttle L., et al. Collagen in the scarless fetal skin wound: detection with picrosirius-polarization. Wound Repair Regen. 2005, 13:198-204.
    • (2005) Wound Repair Regen. , vol.13 , pp. 198-204
    • Cuttle, L.1
  • 32
    • 73949122565 scopus 로고    scopus 로고
    • Venular basement membranes ubiquitously express matrix protein low-expression regions: characterization in multiple tissues and remodeling during inflammation
    • Voisin M.B., et al. Venular basement membranes ubiquitously express matrix protein low-expression regions: characterization in multiple tissues and remodeling during inflammation. Am. J. Pathol. 2010, 176:482-495.
    • (2010) Am. J. Pathol. , vol.176 , pp. 482-495
    • Voisin, M.B.1
  • 33
    • 56749164863 scopus 로고    scopus 로고
    • Dynamic imaging of cancer growth and invasion: a modified skin-fold chamber model
    • Alexander S., et al. Dynamic imaging of cancer growth and invasion: a modified skin-fold chamber model. Histochem. Cell Biol. 2008, 130:1147-1154.
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 1147-1154
    • Alexander, S.1
  • 34
    • 36048952090 scopus 로고    scopus 로고
    • Collagen stiffness regulates cellular contraction and matrix remodeling gene expression
    • Karamichos D., et al. Collagen stiffness regulates cellular contraction and matrix remodeling gene expression. J. Biomed. Mater. Res. A 2007, 83:887-894.
    • (2007) J. Biomed. Mater. Res. A , vol.83 , pp. 887-894
    • Karamichos, D.1
  • 35
    • 34548760859 scopus 로고    scopus 로고
    • Complementary roles of intracellular and pericellular collagen degradation pathways in vivo
    • Wagenaar-Miller R.A., et al. Complementary roles of intracellular and pericellular collagen degradation pathways in vivo. Mol. Cell. Biol. 2007, 27:6309-6322.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6309-6322
    • Wagenaar-Miller, R.A.1
  • 36
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: multifunctional enzymes in cancer
    • Mohamed M.M, Sloane B.F. Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 2006, 6:764-775.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 37
    • 37249057731 scopus 로고    scopus 로고
    • Functional analysis of matrix metalloproteinases and tissue inhibitors of metalloproteinases differentially expressed by variants of human HT-(1080) fibrosarcoma exhibiting high and low levels of intravasation and metastasis
    • Partridge J.J., et al. Functional analysis of matrix metalloproteinases and tissue inhibitors of metalloproteinases differentially expressed by variants of human HT-(1080) fibrosarcoma exhibiting high and low levels of intravasation and metastasis. J. Biol. Chem. 2007, 282:35964-35977.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35964-35977
    • Partridge, J.J.1
  • 38
    • 59049085396 scopus 로고    scopus 로고
    • Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption
    • Wilson S.R., et al. Cathepsin K activity-dependent regulation of osteoclast actin ring formation and bone resorption. J. Biol. Chem. 2009, 284:2584-2592.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2584-2592
    • Wilson, S.R.1
  • 39
    • 63049095880 scopus 로고    scopus 로고
    • Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
    • Cavallo-Medved D., et al. Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation. Exp. Cell Res. 2009, 315:1234-1246.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1234-1246
    • Cavallo-Medved, D.1
  • 40
    • 0029131436 scopus 로고
    • Superficial accumulation of plasminogen during plasma clot lysis
    • Sakharov D.V., Rijken D.C. Superficial accumulation of plasminogen during plasma clot lysis. Circulation 1995, 92:1883-1890.
    • (1995) Circulation , vol.92 , pp. 1883-1890
    • Sakharov, D.V.1    Rijken, D.C.2
  • 41
    • 69649102613 scopus 로고    scopus 로고
    • Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability
    • Bhole A.P., et al. Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability. Philos. Transact. Ser. A: Math. Phys. Eng. Sci. 2009, 367:3339-3362.
    • (2009) Philos. Transact. Ser. A: Math. Phys. Eng. Sci. , vol.367 , pp. 3339-3362
    • Bhole, A.P.1
  • 42
    • 79954610203 scopus 로고    scopus 로고
    • Visualization of clot lysis in a rat embolic stroke model: application to comparative lytic efficacy. Stroke
    • Walvick R.P., et al. Visualization of clot lysis in a rat embolic stroke model: application to comparative lytic efficacy. Stroke. J. Cereb. Circ. 2011, 42:1110-1115.
    • (2011) J. Cereb. Circ. , vol.42 , pp. 1110-1115
    • Walvick, R.P.1
  • 43
    • 0030895688 scopus 로고    scopus 로고
    • Trafficking of matrix collagens through bone-resorbing osteoclasts
    • Nesbitt S.A., Horton M.A. Trafficking of matrix collagens through bone-resorbing osteoclasts. Science 1997, 276:26626-26629.
    • (1997) Science , vol.276 , pp. 26626-26629
    • Nesbitt, S.A.1    Horton, M.A.2
  • 44
    • 69249156451 scopus 로고    scopus 로고
    • Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion
    • Sabeh F., et al. Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J. Biol. Chem. 2009, 284:23001-23011.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23001-23011
    • Sabeh, F.1
  • 45
    • 84983157331 scopus 로고    scopus 로고
    • Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions
    • Wahlgren J., et al. Expression and induction of collagenases (MMP-8 and -13) in plasma cells associated with bone-destructive lesions. J. Pathol. 2001, 194:217-224.
    • (2001) J. Pathol. , vol.194 , pp. 217-224
    • Wahlgren, J.1
  • 46
    • 53149100519 scopus 로고    scopus 로고
    • Seprase: an overview of an important matrix serine protease
    • O'Brien P., O'Connor B.F. Seprase: an overview of an important matrix serine protease. Biochim. Biophys. Acta 2008, 1784:1130-1145.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1130-1145
    • O'Brien, P.1    O'Connor, B.F.2
  • 47
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • Hotary K., et al. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J. Cell Biol. 2000, 149:1309-1323.
    • (2000) J. Cell Biol. , vol.149 , pp. 1309-1323
    • Hotary, K.1
  • 48
    • 0037064041 scopus 로고    scopus 로고
    • Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
    • Tam E.M., et al. Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. J. Biol. Chem. 2002, 277:39005-39014.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39005-39014
    • Tam, E.M.1
  • 49
    • 71449088789 scopus 로고    scopus 로고
    • MT1-MMP- and Cdc42-dependent signaling co-regulate cell invasion and tunnel formation in 3D collagen matrices
    • Fisher K.E., et al. MT1-MMP- and Cdc42-dependent signaling co-regulate cell invasion and tunnel formation in 3D collagen matrices. J. Cell Sci. 2009, 122:4558-4569.
    • (2009) J. Cell Sci. , vol.122 , pp. 4558-4569
    • Fisher, K.E.1
  • 50
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • Holmbeck K., et al. MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 1999, 99:81-92.
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1
  • 51
    • 67651121845 scopus 로고    scopus 로고
    • Endothelial cell lumen and vascular guidance tunnel formation requires MT1-MMP-dependent proteolysis in 3-dimensional collagen matrices
    • Stratman A.N., et al. Endothelial cell lumen and vascular guidance tunnel formation requires MT1-MMP-dependent proteolysis in 3-dimensional collagen matrices. Blood 2009, 114:237-247.
    • (2009) Blood , vol.114 , pp. 237-247
    • Stratman, A.N.1
  • 52
    • 9444290419 scopus 로고    scopus 로고
    • Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP
    • Sabeh F., et al. Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP. J. Cell Biol. 2004, 167:769-781.
    • (2004) J. Cell Biol. , vol.167 , pp. 769-781
    • Sabeh, F.1
  • 53
    • 66949121118 scopus 로고    scopus 로고
    • Expression and regulation of cathepsin K in skin fibroblasts
    • Quintanilla-Dieck M.J., et al. Expression and regulation of cathepsin K in skin fibroblasts. Exp. Dermatol. 2009, 18:596-602.
    • (2009) Exp. Dermatol. , vol.18 , pp. 596-602
    • Quintanilla-Dieck, M.J.1
  • 54
    • 0242467574 scopus 로고    scopus 로고
    • Collagen phagocytosis by lung alveolar macrophages in animal models of emphysema
    • Lucattelli M., et al. Collagen phagocytosis by lung alveolar macrophages in animal models of emphysema. Eur. Respir. J. 2003, 22:728-734.
    • (2003) Eur. Respir. J. , vol.22 , pp. 728-734
    • Lucattelli, M.1
  • 55
    • 22344436842 scopus 로고    scopus 로고
    • Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy
    • Curino A.C., et al. Intracellular collagen degradation mediated by uPARAP/Endo180 is a major pathway of extracellular matrix turnover during malignancy. J. Cell Biol. 2005, 169:977-985.
    • (2005) J. Cell Biol. , vol.169 , pp. 977-985
    • Curino, A.C.1
  • 56
    • 34848866646 scopus 로고    scopus 로고
    • Extracellular collagenases and the endocytic receptor, urokinase plasminogen activator receptor-associated protein/Endo180, cooperate in fibroblast-mediated collagen degradation
    • Madsen D.H., et al. Extracellular collagenases and the endocytic receptor, urokinase plasminogen activator receptor-associated protein/Endo180, cooperate in fibroblast-mediated collagen degradation. J. Biol. Chem. 2007, 282:27037-27045.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27037-27045
    • Madsen, D.H.1
  • 57
    • 70849100053 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180
    • Messaritou G., et al. Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180. J. Cell Sci. 2009, 122:4042-4048.
    • (2009) J. Cell Sci. , vol.122 , pp. 4042-4048
    • Messaritou, G.1
  • 58
    • 0142245603 scopus 로고    scopus 로고
    • Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases
    • Wolf K., et al. Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases. Blood 2003, 102:3262-3269.
    • (2003) Blood , vol.102 , pp. 3262-3269
    • Wolf, K.1
  • 59
    • 1542495339 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic migration of tumour cells and leucocytes
    • Friedl P., Wolf K. Proteolytic and non-proteolytic migration of tumour cells and leucocytes. Biochem. Soc. Symp. 2003, 2003:277-285.
    • (2003) Biochem. Soc. Symp. , vol.2003 , pp. 277-285
    • Friedl, P.1    Wolf, K.2
  • 60
    • 79951867978 scopus 로고    scopus 로고
    • Two-photon laser-generated microtracks in 3D collagen lattices: principles of MMP-dependent and -independent collective cancer cell invasion
    • Ilina O., et al. Two-photon laser-generated microtracks in 3D collagen lattices: principles of MMP-dependent and -independent collective cancer cell invasion. Phys. Biol. 2011, 8:015010.
    • (2011) Phys. Biol. , vol.8 , pp. 015010
    • Ilina, O.1
  • 61
    • 54149097038 scopus 로고    scopus 로고
    • The role of myosin II in glioma invasion of the brain
    • Beadle C., et al. The role of myosin II in glioma invasion of the brain. Mol. Biol. Cell 2008, 19:3357-3368.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3357-3368
    • Beadle, C.1
  • 62
    • 33746562929 scopus 로고    scopus 로고
    • ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo
    • Wyckoff J.B., et al. ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo. Curr. Biol. 2006, 16:1515-1523.
    • (2006) Curr. Biol. , vol.16 , pp. 1515-1523
    • Wyckoff, J.B.1
  • 63
    • 44149123099 scopus 로고    scopus 로고
    • Collagen density promotes mammary tumor initiation and progression
    • Provenzano P.P., et al. Collagen density promotes mammary tumor initiation and progression. BMC Med. 2008, 6:11.
    • (2008) BMC Med. , vol.6 , pp. 11
    • Provenzano, P.P.1
  • 64
    • 70350345826 scopus 로고    scopus 로고
    • Shining new light on 3D cell motility and the metastatic process
    • Provenzano P.P., et al. Shining new light on 3D cell motility and the metastatic process. Trends Cell Biol. 2009, 19:638-648.
    • (2009) Trends Cell Biol. , vol.19 , pp. 638-648
    • Provenzano, P.P.1
  • 65
    • 31544468879 scopus 로고    scopus 로고
    • Epidermal growth factor receptor overexpression results in increased tumor cell motility in vivo coordinately with enhanced intravasation and metastasis
    • Xue C., et al. Epidermal growth factor receptor overexpression results in increased tumor cell motility in vivo coordinately with enhanced intravasation and metastasis. Cancer Res. 2006, 66:192-197.
    • (2006) Cancer Res. , vol.66 , pp. 192-197
    • Xue, C.1
  • 66
    • 34548077168 scopus 로고    scopus 로고
    • Noninvasive optical detection of bone mineral
    • Kozloff K.M., et al. Noninvasive optical detection of bone mineral. J. Bone Mineral Res. 2007, 22:1208-1216.
    • (2007) J. Bone Mineral Res. , vol.22 , pp. 1208-1216
    • Kozloff, K.M.1
  • 67
    • 78449270310 scopus 로고    scopus 로고
    • Zoledronic acid reduces bone loss and tumor growth in an orthotopic xenograft model of osteolytic oral squamous cell carcinoma
    • Martin C.K., et al. Zoledronic acid reduces bone loss and tumor growth in an orthotopic xenograft model of osteolytic oral squamous cell carcinoma. Cancer Res. 2010, 70:8607-8616.
    • (2010) Cancer Res. , vol.70 , pp. 8607-8616
    • Martin, C.K.1
  • 68
    • 73949156419 scopus 로고    scopus 로고
    • Preformed portals facilitate dendritic cell entry into afferent lymphatic vessels
    • Pflicke H., Sixt M. Preformed portals facilitate dendritic cell entry into afferent lymphatic vessels. J. Exp. Med. 2009, 206:2925-2935.
    • (2009) J. Exp. Med. , vol.206 , pp. 2925-2935
    • Pflicke, H.1    Sixt, M.2
  • 69
    • 68149178417 scopus 로고    scopus 로고
    • Monocytes and neutrophils exhibit both distinct and common mechanisms in penetrating the vascular basement membrane in vivo
    • Voisin M.B., et al. Monocytes and neutrophils exhibit both distinct and common mechanisms in penetrating the vascular basement membrane in vivo. Arterioscler. Thromb. Vasc. Biol. 2009, 29:1193-1199.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 1193-1199
    • Voisin, M.B.1
  • 70
    • 33745029732 scopus 로고    scopus 로고
    • Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils
    • Wang S., et al. Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils. J. Exp. Med. 2006, 203:1519-1532.
    • (2006) J. Exp. Med. , vol.203 , pp. 1519-1532
    • Wang, S.1
  • 71
    • 34249722613 scopus 로고    scopus 로고
    • Native and fragmented fibronectin oppositely modulate monocyte secretion of MMP-9
    • Marom B., et al. Native and fragmented fibronectin oppositely modulate monocyte secretion of MMP-9. J. Leuk. Biol. 2007, 81:1466-1476.
    • (2007) J. Leuk. Biol. , vol.81 , pp. 1466-1476
    • Marom, B.1
  • 72
    • 0024524974 scopus 로고
    • Disruption of the subendothelial basement membrane during neutrophil diapedesis in an in vitro construct of a blood vessel wall
    • Huber A.R., Weiss S.J. Disruption of the subendothelial basement membrane during neutrophil diapedesis in an in vitro construct of a blood vessel wall. J. Clin. Invest. 1989, 83:1122-1136.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1122-1136
    • Huber, A.R.1    Weiss, S.J.2
  • 73
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • Hotary K., et al. A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 2006, 20:2673-2686.
    • (2006) Genes Dev. , vol.20 , pp. 2673-2686
    • Hotary, K.1
  • 74
    • 61449181308 scopus 로고    scopus 로고
    • One-dimensional topography underlies three-dimensional fibrillar cell migration
    • Doyle A.D., et al. One-dimensional topography underlies three-dimensional fibrillar cell migration. J. Cell Biol. 2009, 184:481-490.
    • (2009) J. Cell Biol. , vol.184 , pp. 481-490
    • Doyle, A.D.1
  • 75
    • 77649324204 scopus 로고    scopus 로고
    • Impact of tumor cell cytoskeleton organization on invasiveness and migration: a microchannel-based approach
    • Rolli C.G., et al. Impact of tumor cell cytoskeleton organization on invasiveness and migration: a microchannel-based approach. PLoS ONE 2010, 5:e8726.
    • (2010) PLoS ONE , vol.5
    • Rolli, C.G.1
  • 76
    • 39349115654 scopus 로고    scopus 로고
    • Biological second and third harmonic generation microscopy
    • 4.15.1-4.15.21
    • Friedl P., et al. Biological second and third harmonic generation microscopy. Curr. Protoc. Cell Biol. 2007, 34. 4.15.1-4.15.21.
    • (2007) Curr. Protoc. Cell Biol. , vol.34
    • Friedl, P.1
  • 77
    • 79953849744 scopus 로고    scopus 로고
    • In vivo imaging of myelin in the vertebrate central nervous system using third harmonic generation microscopy
    • Farrar M.J., et al. In vivo imaging of myelin in the vertebrate central nervous system using third harmonic generation microscopy. Biophys. J. 2011, 100:1362-1371.
    • (2011) Biophys. J. , vol.100 , pp. 1362-1371
    • Farrar, M.J.1
  • 78
    • 31344446932 scopus 로고    scopus 로고
    • Imaging lipid bodies in cells and tissues using third-harmonic generation microscopy
    • Debarre D., et al. Imaging lipid bodies in cells and tissues using third-harmonic generation microscopy. Nat. Methods 2006, 3:47-53.
    • (2006) Nat. Methods , vol.3 , pp. 47-53
    • Debarre, D.1
  • 79
    • 77950273418 scopus 로고    scopus 로고
    • Simultaneous visualization of protumorigenic Src and MT1-MMP activities with fluorescence resonance energy transfer
    • Ouyang M., et al. Simultaneous visualization of protumorigenic Src and MT1-MMP activities with fluorescence resonance energy transfer. Cancer Res. 2010, 70:2204-2212.
    • (2010) Cancer Res. , vol.70 , pp. 2204-2212
    • Ouyang, M.1
  • 80
    • 68149166462 scopus 로고    scopus 로고
    • Comparative assessment of substrates and activity based probes as tools for non-invasive optical imaging of cysteine protease activity
    • Blum G., et al. Comparative assessment of substrates and activity based probes as tools for non-invasive optical imaging of cysteine protease activity. PLoS ONE 2009, 4:e6374.
    • (2009) PLoS ONE , vol.4
    • Blum, G.1
  • 81
    • 79958792489 scopus 로고    scopus 로고
    • Two-dimensional intravascular near-infrared fluorescence molecular imaging of inflammation in atherosclerosis and stent-induced vascular injury
    • Jaffer F.A., et al. Two-dimensional intravascular near-infrared fluorescence molecular imaging of inflammation in atherosclerosis and stent-induced vascular injury. J. Am. Coll. Cardiol. 2011, 57:2516-2526.
    • (2011) J. Am. Coll. Cardiol. , vol.57 , pp. 2516-2526
    • Jaffer, F.A.1
  • 82
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski J.E., et al. Unraveling the role of proteases in cancer. Clin. Chim. Acta 2000, 291:113-135.
    • (2000) Clin. Chim. Acta , vol.291 , pp. 113-135
    • Koblinski, J.E.1
  • 83
    • 0030907299 scopus 로고    scopus 로고
    • Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation
    • Baramova E.N., et al. Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation. FEBS Lett. 1997, 405:157-162.
    • (1997) FEBS Lett. , vol.405 , pp. 157-162
    • Baramova, E.N.1
  • 84
    • 0242361774 scopus 로고    scopus 로고
    • Mice lacking tissue plasminogen activator and urokinase plasminogen activator genes show attenuated matrix metalloproteases activity after sciatic nerve crush
    • Siconolfi L.B., Seeds N.W. Mice lacking tissue plasminogen activator and urokinase plasminogen activator genes show attenuated matrix metalloproteases activity after sciatic nerve crush. J. Neurosci. Res. 2003, 74:430-434.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 430-434
    • Siconolfi, L.B.1    Seeds, N.W.2
  • 85
    • 79960660983 scopus 로고    scopus 로고
    • The non-phagocytic route of collagen uptake: a distinct degradation pathway
    • Madsen D.H., et al. The non-phagocytic route of collagen uptake: a distinct degradation pathway. J. Biol. Chem. 2011, 286:26996-27010.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26996-27010
    • Madsen, D.H.1
  • 86
    • 62449216585 scopus 로고    scopus 로고
    • Mapping proteolytic cancer cell-extracellular matrix interfaces
    • Wolf K., Friedl P. Mapping proteolytic cancer cell-extracellular matrix interfaces. Clin. Exp. Metastasis 2009, 26:289-298.
    • (2009) Clin. Exp. Metastasis , vol.26 , pp. 289-298
    • Wolf, K.1    Friedl, P.2
  • 87
    • 33847343034 scopus 로고    scopus 로고
    • The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
    • Linder S. The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol. 2007, 17:107-117.
    • (2007) Trends Cell Biol. , vol.17 , pp. 107-117
    • Linder, S.1
  • 88
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M., et al. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 2010, 189:541-556.
    • (2010) J. Cell Biol. , vol.189 , pp. 541-556
    • Schoumacher, M.1
  • 89
    • 77957231341 scopus 로고    scopus 로고
    • The 'chemoinvasion' assay, 25 years and still going strong: the use of reconstituted basement membranes to study cell invasion and angiogenesis
    • Albini A., Noonan D.M. The 'chemoinvasion' assay, 25 years and still going strong: the use of reconstituted basement membranes to study cell invasion and angiogenesis. Curr. Opin. Cell Biol. 2010, 22:677-689.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 677-689
    • Albini, A.1    Noonan, D.M.2
  • 90
    • 33846293595 scopus 로고    scopus 로고
    • Probing the microenvironment of mammary tumors using multiphoton microscopy
    • Sidani M., et al. Probing the microenvironment of mammary tumors using multiphoton microscopy. J. Mammary Gland Biol. Neoplasia 2006, 11:151-163.
    • (2006) J. Mammary Gland Biol. Neoplasia , vol.11 , pp. 151-163
    • Sidani, M.1
  • 91
    • 33947654947 scopus 로고    scopus 로고
    • Noninvasive assessment of collagen gel microstructure and mechanics using multiphoton microscopy
    • Raub C.B., et al. Noninvasive assessment of collagen gel microstructure and mechanics using multiphoton microscopy. Biophys. J. 2007, 92:2212-2222.
    • (2007) Biophys. J. , vol.92 , pp. 2212-2222
    • Raub, C.B.1
  • 92
    • 70349456133 scopus 로고    scopus 로고
    • The regulatory role of cell mechanics for migration of differentiating myeloid cells
    • Lautenschlager F., et al. The regulatory role of cell mechanics for migration of differentiating myeloid cells. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:15696-15701.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 15696-15701
    • Lautenschlager, F.1
  • 93
    • 79953709696 scopus 로고    scopus 로고
    • Two-photon fluorescence and second-harmonic generation imaging of collagen in human tissue based on multiphoton microscopy
    • Jiang X., et al. Two-photon fluorescence and second-harmonic generation imaging of collagen in human tissue based on multiphoton microscopy. Scanning 2011, 33:53-56.
    • (2011) Scanning , vol.33 , pp. 53-56
    • Jiang, X.1
  • 94
    • 79955958019 scopus 로고    scopus 로고
    • Mu-Slide Chemotaxis: a new chamber for long-term chemotaxis studies
    • Zengel P., et al. mu-Slide Chemotaxis: a new chamber for long-term chemotaxis studies. BMC Cell Biol. 2011, 12:21.
    • (2011) BMC Cell Biol. , vol.12 , pp. 21
    • Zengel, P.1
  • 95
    • 69249144496 scopus 로고    scopus 로고
    • Simultaneous 3D visualization and quantification of murine bone and bone vasculature using micro-computed tomography and vascular replica
    • Schneider P., et al. Simultaneous 3D visualization and quantification of murine bone and bone vasculature using micro-computed tomography and vascular replica. Microsc. Res. Tech. 2009, 72:690-701.
    • (2009) Microsc. Res. Tech. , vol.72 , pp. 690-701
    • Schneider, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.