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Volumn 53, Issue 3, 2014, Pages 499-510

α 5 ß1-integrin and MT1-MMP promote tumor cell migration in 2D but not in 3D fibronectin microenvironments

Author keywords

Cell migration; Fibronectin matrix; Integrins; MT1 MMP; Tumor microenvironment

Indexed keywords

BINS; CELLS; CYTOLOGY; DISEASES; GLYCOPROTEINS; MEDICAL NANOTECHNOLOGY; PROTEINS; TUMORS;

EID: 84898596396     PISSN: 01787675     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00466-013-0960-6     Document Type: Article
Times cited : (5)

References (59)
  • 1
    • 41749100830 scopus 로고    scopus 로고
    • Metastatic cancer cell
    • doi:10.1146/annurev.pathmechdis.3.121806.151523
    • Bacac M, Stamenkovic I (2008) Metastatic cancer cell. Annu Rev Pathol 3:221-247. doi:10.1146/annurev.pathmechdis.3.121806. 151523
    • (2008) Annu Rev Pathol , vol.3 , pp. 221-247
    • Bacac, M.1    Stamenkovic, I.2
  • 2
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2(3):161-174
    • (2002) Nat Rev Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 3
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • doi:10.1038/nrm2125
    • Page-McCaw A, Ewald AJ, Werb Z (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8(3):221-233. doi:10.1038/nrm2125
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.3 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 4
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • Seiki M (2003) Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion. Cancer Lett 194(1):1-11
    • (2003) Cancer Lett , vol.194 , Issue.1 , pp. 1-11
    • Seiki, M.1
  • 5
    • 0030037395 scopus 로고    scopus 로고
    • Cellularmechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, MurphyG(1996) Cellularmechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J Biol Chem 271(29):17124-17131
    • (1996) J Biol Chem , vol.271 , Issue.29 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 6
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • doi:10.1038/ 370061a0
    • Sato H,TakinoT, OkadaY,Cao J, ShinagawaA,YamamotoE, Seiki M (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370(6484):61-65. doi:10.1038/ 370061a0
    • (1994) Nature , vol.370 , Issue.6484 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 7
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellularmatrixmacromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y (1997) Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellularmatrixmacromolecules. J Biol Chem 272(4):2446-2451
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 8
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • doi:10. 1016/j.tibs.2004.04.001
    • Itoh Y, Seiki M (2004) MT1-MMP: An enzyme with multidimensional regulation. Trends Biochem Sci 29(6):285-289. doi:10. 1016/j.tibs.2004.04.001
    • (2004) Trends Biochem Sci , vol.29 , Issue.6 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 9
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • doi:10.1126/science.285.5430.1028
    • Giancotti FG, Ruoslahti E (1999) Integrin signaling. Science 285(5430):1028-1032. doi:10.1126/science.285.5430.1028
    • (1999) Science , vol.285 , Issue.5430 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 10
    • 21744435478 scopus 로고    scopus 로고
    • The role of focal-adhesion kinase in cancer-A newtherapeutic opportunity
    • doi:10. 1038/nrc1647
    • McLean GW, Carragher NO, Avizienyte E, Evans J, Brunton VG, Frame MC (2005) The role of focal-adhesion kinase in cancer-a newtherapeutic opportunity.Nat RevCancer 5(7):505-515. doi:10. 1038/nrc1647
    • (2005) Nat RevCancer , vol.5 , Issue.7 , pp. 505-515
    • McLean, G.W.1    Carragher, N.O.2    Avizienyte, E.3    Evans, J.4    Brunton, V.G.5    Frame, M.C.6
  • 11
    • 77953121357 scopus 로고    scopus 로고
    • A distinctive role for focal adhesion proteins in three-dimensional cell motility
    • doi:10.1038/ncb2062
    • Fraley SI, Feng Y, Krishnamurthy R, Kim DH, Celedon A, Longmore GD,Wirtz D (2010) A distinctive role for focal adhesion proteins in three-dimensional cell motility. Nat Cell Biol 12(6):598-604. doi:10.1038/ncb2062
    • (2010) Nat Cell Biol , vol.12 , Issue.6 , pp. 598-604
    • Fraley, S.I.1    Feng, Y.2    Krishnamurthy, R.3    Kim, D.H.4    Celedon, A.5    Longmore, G.D.6    Wirtz, D.7
  • 12
    • 0032834211 scopus 로고    scopus 로고
    • Functional hierarchy of simultaneously expressed adhesion receptors: Integrin alpha2beta1 but not CD44 mediates MV3melanoma cellmigration andmatrix reorganization within three-dimensional hyaluronan-containing collagen matrices
    • Maaser K, Wolf K, Klein CE, Niggemann B, Zanker KS, Brocker EB, Friedl P (1999) Functional hierarchy of simultaneously expressed adhesion receptors: integrin alpha2beta1 but not CD44 mediates MV3melanoma cellmigration andmatrix reorganization within three-dimensional hyaluronan-containing collagen matrices. Mol Biol Cell 10(10):3067-3079
    • (1999) Mol Biol Cell , vol.10 , Issue.10 , pp. 3067-3079
    • Maaser, K.1    Wolf, K.2    Klein, C.E.3    Niggemann, B.4    Zanker, K.S.5    Brocker, E.B.6    Friedl, P.7
  • 13
    • 84864023323 scopus 로고    scopus 로고
    • 2D protrusion but not motility predicts growth factor-induced cancer cell migration in 3D collagen
    • doi:10.1083/jcb.201201003
    • MeyerAS, Hughes-Alford SK,Kay JE,CastilloA,Wells A, Gertler FB, Lauffenburger DA (2012) 2D protrusion but not motility predicts growth factor-induced cancer cell migration in 3D collagen. J Cell Biol 197(6):721-729. doi:10.1083/jcb.201201003
    • (2012) J Cell Biol , vol.197 , Issue.6 , pp. 721-729
    • Meyer, A.S.1    Hughes-Alford, S.K.2    Kay, J.E.3    Castillo, A.4    Wells, A.5    Gertler, F.B.6    Lauffenburger, D.A.7
  • 14
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane trans- migration program
    • doi:10.1101/gad.1451806
    • Hotary K, Li XY, Allen E, Stevens SL, Weiss SJ (2006) A cancer cell metalloprotease triad regulates the basement membrane trans- migration program. Genes Dev 20(19):2673-2686. doi:10.1101/ gad.1451806
    • (2006) Genes Dev , vol.20 , Issue.19 , pp. 2673-2686
    • Hotary, K.1    Li, X.Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 15
    • 54049102110 scopus 로고    scopus 로고
    • Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase
    • doi:10.1091/mbc.E08-01-0016
    • Li XY, Ota I, Yana I, Sabeh F, Weiss SJ (2008) Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase. Mol Biol Cell 19(8):3221-3233. doi:10.1091/mbc.E08-01-0016
    • (2008) Mol Biol Cell , vol.19 , Issue.8 , pp. 3221-3233
    • Li, X.Y.1    Ota, I.2    Yana, I.3    Sabeh, F.4    Weiss, S.J.5
  • 16
    • 84859375474 scopus 로고    scopus 로고
    • Invasive matrix degradation at focal adhesions occurs via protease recruitment by a FAK-p130Cas complex
    • doi:10.1083/jcb.201105153
    • Wang Y, McNivenMA (2012) Invasive matrix degradation at focal adhesions occurs via protease recruitment by a FAK-p130Cas complex. J Cell Biol 196(3):375-385. doi:10.1083/jcb.201105153
    • (2012) J Cell Biol , vol.196 , Issue.3 , pp. 375-385
    • Wang, Y.1    McNiven, M.A.2
  • 17
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • doi:10.1038/ncb1616
    • Wolf K,Wu YI, LiuY, Geiger J, TamE,Overall C, Stack MS, Friedl P (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9(8):893-904. doi:10.1038/ncb1616
    • (2007) Nat Cell Biol , vol.9 , Issue.8 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 18
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: Mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • doi:10.1083/jcb.200209006
    • Wolf K, Mazo I, Leung H, Engelke K, von Andrian UH, Deryugina EI, StronginAY, Brocker EB, Friedl P (2003) Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J Cell Biol 160(2):267-277. doi:10.1083/jcb.200209006
    • (2003) J Cell Biol , vol.160 , Issue.2 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3    Engelke, K.4    Von Andrian, U.H.5    Deryugina, E.I.6    Strongin, A.Y.7    Brocker, E.B.8    Friedl, P.9
  • 19
    • 58149288221 scopus 로고    scopus 로고
    • Direct visualization of protease activity on cells migrating in threedimensions
    • doi:10.1016/j.matbio.2008.10.001
    • Packard BZ, Artym VV, Komoriya A, Yamada KM (2009) Direct visualization of protease activity on cells migrating in threedimensions. Matrix Biol 28(1):3-10. doi:10.1016/j.matbio.2008. 10.001
    • (2009) Matrix Biol , vol.28 , Issue.1 , pp. 3-10
    • Packard, B.Z.1    Artym, V.V.2    Komoriya, A.3    Yamada, K.M.4
  • 20
    • 61449181308 scopus 로고    scopus 로고
    • One-dimensional topography underlies three-dimensional fibrillar cell migration
    • doi:10.1083/jcb.200810041
    • Doyle AD, Wang FW, Matsumoto K, Yamada KM (2009) One-dimensional topography underlies three-dimensional fibrillar cell migration. J Cell Biol 184(4):481-490. doi:10.1083/jcb. 200810041
    • (2009) J Cell Biol , vol.184 , Issue.4 , pp. 481-490
    • Doyle, A.D.1    Wang, F.W.2    Matsumoto, K.3    Yamada, K.M.4
  • 22
    • 0004043397 scopus 로고
    • Springer series in molecular biology. Springer, New York
    • Hynes RO (1990) Fibronectins. Springer series in molecular biology. Springer, New York
    • (1990) Fibronectins.
    • Hynes, R.O.1
  • 23
    • 34848863979 scopus 로고    scopus 로고
    • Impact of the non-cellular tumor microenvironment on metastasis: Potential therapeutic and imaging opportunities
    • doi:10.1002/jcp.21222
    • Cretu A, Brooks PC (2007) Impact of the non-cellular tumor microenvironment on metastasis: potential therapeutic and imaging opportunities. J Cell Physiol 213(2):391-402. doi:10.1002/jcp. 21222
    • (2007) J Cell Physiol , vol.213 , Issue.2 , pp. 391-402
    • Cretu, A.1    Brooks, P.C.2
  • 24
    • 63049121364 scopus 로고    scopus 로고
    • Themetastatic niche: Adapting the foreign soil
    • doi:10.1038/nrc2621
    • Psaila B,LydenD(2009) Themetastatic niche: Adapting the foreign soil. Nat Rev Cancer 9(4):285-293. doi:10.1038/nrc2621
    • (2009) Nat Rev Cancer , vol.9 , Issue.4 , pp. 285-293
    • Psaila, B.1    Lyden, D.2
  • 25
    • 33646020670 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase modulates focal adhesion stability and cell migration
    • doi:10.1016/j.yexcr.2006.01.008
    • Takino T, Watanabe Y, Matsui M, Miyamori H, Kudo T, Seiki M, Sato H (2006) Membrane-type 1 matrix metalloproteinase modulates focal adhesion stability and cell migration. Exp Cell Res 312(8):1381-1389. doi:10.1016/j.yexcr.2006.01.008
    • (2006) Exp Cell Res , vol.312 , Issue.8 , pp. 1381-1389
    • Takino, T.1    Watanabe, Y.2    Matsui, M.3    Miyamori, H.4    Kudo, T.5    Seiki, M.6    Sato, H.7
  • 26
    • 37549029111 scopus 로고    scopus 로고
    • Inhibition of membrane-type 1 matrix metalloproteinase at cell-matrix adhesions
    • doi:10.1158/0008-5472.CAN-07-5251
    • Takino T, Saeki H, Miyamori H, Kudo T, Sato H (2007) Inhibition of membrane-type 1 matrix metalloproteinase at cell-matrix adhesions. Cancer Res 67(24):11621-11629. doi:10.1158/0008-5472. CAN-07-5251
    • (2007) Cancer Res , vol.67 , Issue.24 , pp. 11621-11629
    • Takino, T.1    Saeki, H.2    Miyamori, H.3    Kudo, T.4    Sato, H.5
  • 27
    • 84856840530 scopus 로고    scopus 로고
    • MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin
    • doi:10.1242/jcs.087858
    • Shi F, Sottile J (2011) MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin. J Cell Sci 124(Pt 23):4039-4050. doi:10.1242/jcs.087858
    • (2011) J Cell Sci , vol.124 , Issue.PART 23 , pp. 4039-4050
    • Shi, F.1    Sottile, J.2
  • 28
    • 67349229153 scopus 로고    scopus 로고
    • Revisiting the mystery of fibronectin multimers: The fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds
    • doi:10.1016/j.matbio.2009.03.002
    • Ohashi T, Erickson HP (2009) Revisiting the mystery of fibronectin multimers: The fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds. Matrix Biol 28(3):170-175. doi:10.1016/j.matbio.2009.03. 002
    • (2009) Matrix Biol , vol.28 , Issue.3 , pp. 170-175
    • Ohashi, T.1    Erickson, H.P.2
  • 30
    • 27644473227 scopus 로고    scopus 로고
    • Stimulatory effects of a threedimensional microenvironment on cell-mediated fibronectin fibrillogenesis
    • doi:10.1242/jcs.02566
    • Mao Y, Schwarzbauer JE (2005) Stimulatory effects of a threedimensional microenvironment on cell-mediated fibronectin fibrillogenesis. JCell Sci 118(Pt 19):4427-4436. doi:10.1242/jcs.02566
    • (2005) JCell Sci , vol.118 , Issue.PART 19 , pp. 4427-4436
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 31
    • 84863205849 scopus 로고    scopus 로고
    • NIH image to imageJ: 25 years of image analysis
    • doi:10.1038/nmeth.2089
    • Schneider CA, Rasband WS, Eliceiri KW (2012) NIH image to imageJ: 25 years of image analysis. Nat Methods Hist Comment 9(7):671-675. doi:10.1038/nmeth.2089
    • (2012) Nat Methods Hist Comment , vol.9 , Issue.7 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 32
    • 84898598467 scopus 로고    scopus 로고
    • The motile actin system in health and disease
    • Lambrechts A, Ampe C (eds) (2008) The motile actin system in health and disease. Transw Res Netw
    • (2008) Transw Res Netw
    • Lambrechts, A.1    Ampe, C.2
  • 33
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM,BurridgeK(1998) Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 141(2):539-551
    • (1998) J Cell Biol , vol.141 , Issue.2 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 34
    • 0029957287 scopus 로고    scopus 로고
    • Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha v integrins
    • Yang JT, Hynes RO (1996) Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha V integrins. Mol Biol Cell 7(11):1737-1748
    • (1996) Mol Biol Cell , vol.7 , Issue.11 , pp. 1737-1748
    • Yang, J.T.1    Hynes, R.O.2
  • 35
    • 0032926793 scopus 로고    scopus 로고
    • Fibronectin and its integrin receptors in cancer
    • Ruoslahti E (1999) Fibronectin and its integrin receptors in cancer. Adv Cancer Res 76:1-20
    • (1999) Adv Cancer Res , vol.76 , pp. 1-20
    • Ruoslahti, E.1
  • 36
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • doi:10.1016/ S0092-8674(02)00971-6
    • Hynes RO (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110(6):673-687. doi:10.1016/S0092-8674(02)00971-6
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 37
    • 0021997189 scopus 로고
    • Alterations in neural crest migration by a monoclonal antibody that affects cell adhesion
    • Bronner-Fraser M (1985) Alterations in neural crest migration by a monoclonal antibody that affects cell adhesion. J Cell Biol 101(2):610-617
    • (1985) J Cell Biol , vol.101 , Issue.2 , pp. 610-617
    • Bronner-Fraser, M.1
  • 38
    • 0141429921 scopus 로고    scopus 로고
    • A novel mode for integrin-mediated signaling: Tethering is required for phosphorylation of FAK Y397
    • doi:10.1091/mbc.E03-01-0046
    • Shi Q, Boettiger D (2003) A novel mode for integrin-mediated signaling: Tethering is required for phosphorylation of FAK Y397. Mol Biol Cell 14(10):4306-4315. doi:10.1091/mbc.E03-01-0046
    • (2003) Mol Biol Cell , vol.14 , Issue.10 , pp. 4306-4315
    • Shi, Q.1    Boettiger, D.2
  • 39
    • 67649922824 scopus 로고    scopus 로고
    • A novel mode of cell detachment from fibrillar fibronectin matrix under shear
    • doi:10.1242/jcs.040824
    • Engler AJ, ChanM, Boettiger D, Schwarzbauer JE (2009) A novel mode of cell detachment from fibrillar fibronectin matrix under shear. J Cell Sci 122(Pt 10):1647-1653. doi:10.1242/jcs.040824
    • (2009) J Cell Sci , vol.122 , Issue.PART 10 , pp. 1647-1653
    • Engler, A.J.1    Chan, M.2    Boettiger, D.3    Schwarzbauer, J.E.4
  • 40
    • 33845428422 scopus 로고    scopus 로고
    • Accessibility to the fibronectin synergy site in a 3D matrix regulates engagement of alpha5beta1 versus alphavbeta3 integrin receptors
    • doi:10.1080/15419060601072215
    • Mao Y, Schwarzbauer JE (2006) Accessibility to the fibronectin synergy site in a 3D matrix regulates engagement of alpha5beta1 versus alphavbeta3 integrin receptors. Cell Commun Adhes 13(5- 6):267-277. doi:10.1080/ 15419060601072215
    • (2006) Cell Commun Adhes , vol.13 , Issue.5-6 , pp. 267-277
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 42
    • 78049427279 scopus 로고    scopus 로고
    • Assembly of fibronectin extracellular matrix
    • doi:10.1146/annurev-cellbio-100109-104020
    • Singh P, Carraher C, Schwarzbauer JE (2010) Assembly of fibronectin extracellular matrix. Annu Rev Cell Dev Biol 26:397-419. doi:10.1146/annurev- cellbio-100109-104020
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 397-419
    • Singh, P.1    Carraher, C.2    Schwarzbauer, J.E.3
  • 43
    • 69449108652 scopus 로고    scopus 로고
    • Extracellular matrix stiffness and architecture govern intracellular rheology in cancer
    • doi:10.1016/j.bpj.2009.05.054
    • Baker EL, Bonnecaze RT, Zaman MH (2009) Extracellular matrix stiffness and architecture govern intracellular rheology in cancer. Biophys J 97(4):1013-1021. doi:10.1016/j.bpj.2009.05.054
    • (2009) Biophys J , vol.97 , Issue.4 , pp. 1013-1021
    • Baker, E.L.1    Bonnecaze, R.T.2    Zaman, M.H.3
  • 44
    • 81355127254 scopus 로고    scopus 로고
    • Extracellular matrix determinants of proteolytic and non-proteolytic cell migration
    • doi:10.1016/j.tcb.2011.09.006
    • Wolf K, Friedl P (2011) Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol 21(12):736-744. doi:10.1016/j.tcb.2011.09.006
    • (2011) Trends Cell Biol , vol.21 , Issue.12 , pp. 736-744
    • Wolf, K.1    Friedl, P.2
  • 45
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • doi:10.1016/j.cell.2010.03.015
    • KessenbrockK, PlaksV,Werb Z (2010) Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141(1):52-67. doi:10.1016/j.cell.2010.03.015
    • (2010) Cell , vol.141 , Issue.1 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 46
    • 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, AllenE, Punturieri A,Yana I,Weiss SJ (2000) 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 149(6):1309-1323
    • (2000) J Cell Biol , vol.149 , Issue.6 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 47
    • 71449088789 scopus 로고    scopus 로고
    • MT1-MMP- and Cdc42- dependent signaling co-regulate cell invasion and tunnel formation in 3D collagen matrices
    • doi:10.1242/jcs.050724
    • Fisher KE, Sacharidou A, Stratman AN, Mayo AM, Fisher SB, Mahan RD, Davis MJ, Davis GE (2009) MT1-MMP- and Cdc42- dependent signaling co-regulate cell invasion and tunnel formation in 3D collagen matrices. J Cell Sci 122(Pt 24):4558-4569. doi:10.1242/jcs.050724
    • (2009) J Cell Sci , vol.122 , Issue.PART 24 , pp. 4558-4569
    • Fisher, K.E.1    Sacharidou, A.2    Stratman, A.N.3    Mayo, A.M.4    Fisher, S.B.5    Mahan, R.D.6    Davis, M.J.7    Davis, G.E.8
  • 48
    • 79957646416 scopus 로고    scopus 로고
    • Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling
    • doi:10.1242/jcs.079343
    • Kirmse R, Otto H, Ludwig T (2011) Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling. J Cell Sci 124(Pt 11):1857-1866. doi:10.1242/jcs. 079343
    • (2011) J Cell Sci , vol.124 , Issue.PART 11 , pp. 1857-1866
    • Kirmse, R.1    Otto, H.2    Ludwig, T.3
  • 49
    • 84887021974 scopus 로고    scopus 로고
    • The extracellular matrix remodeled: Interdependency of matrix proteolysis, cell adhesion, and force sensing
    • Kirmse R, Otto H, Ludwig T (2012) The extracellular matrix remodeled: Interdependency of matrix proteolysis, cell adhesion, and force sensing. Commun Integr Biol 5(1):71-73
    • (2012) Commun Integr Biol , vol.5 , Issue.1 , pp. 71-73
    • Kirmse, R.1    Otto, H.2    Ludwig, T.3
  • 50
    • 0026768692 scopus 로고
    • Inhibition of human skin fibroblast collagenase, thermolysin, and pseudomonas aeruginosa elastase by peptide hydroxamic acids
    • Grobelny D, Poncz L, Galardy RE (1992) Inhibition of human skin fibroblast collagenase, thermolysin, and pseudomonas aeruginosa elastase by peptide hydroxamic acids. Biochemistry 31(31):7152-7154
    • (1992) Biochemistry , vol.31 , Issue.31 , pp. 7152-7154
    • Grobelny, D.1    Poncz, L.2    Galardy, R.E.3
  • 51
    • 0017810151 scopus 로고
    • Peptide hydroxamic acids as inhibitors of thermolysin
    • Nishino N, Powers JC (1978) Peptide hydroxamic acids as inhibitors of thermolysin. Biochemistry 17(14):2846-2850
    • (1978) Biochemistry , vol.17 , Issue.14 , pp. 2846-2850
    • Nishino, N.1    Powers, J.C.2
  • 52
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escapemechanisms
    • doi:10. 1038/nrc1075
    • Friedl P,Wolf K (2003) Tumour-cell invasion and migration: diversity and escapemechanisms. NatRev Cancer 3(5):362-374. doi:10. 1038/nrc1075
    • (2003) NatRev Cancer , vol.3 , Issue.5 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 53
    • 1642282882 scopus 로고    scopus 로고
    • Prespecification and plasticity: Shifting mechanisms of cell migration
    • doi:10.1016/j.ceb.2003.11.001
    • Friedl P (2004) Prespecification and plasticity: Shifting mechanisms of cell migration. Curr Opin Cell Biol 16(1):14-23. doi:10. 1016/j.ceb.2003.11.001
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.1 , pp. 14-23
    • Friedl, P.1
  • 54
    • 84860815876 scopus 로고    scopus 로고
    • Regulation of ROCK1 via Notch1 during breast cancer cell migration into dense matrices
    • doi:10.1186/1471-2121-13-12
    • Raviraj V, Fok S, Zhao J, Chien HY, Lyons JG, Thompson EW, Soon L (2012) Regulation of ROCK1 via Notch1 during breast cancer cell migration into dense matrices. BMC Cell Biol 13:12. doi:10.1186/1471-2121-13-12
    • (2012) BMC Cell Biol , vol.13 , pp. 12
    • Raviraj, V.1    Fok, S.2    Zhao, J.3    Chien, H.Y.4    Lyons, J.G.5    Thompson, E.W.6    Soon, L.7
  • 55
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • doi:10.1038/ncb1019
    • Sahai E, Marshall CJ (2003) Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis.Nat Cell Biol 5(8):711-719. doi:10.1038/ncb1019
    • (2003) Nat Cell Biol , vol.5 , Issue.8 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 56
    • 1542495339 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic migration of tumour cells and leucocytes
    • Friedl P, 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
  • 57
    • 78649460225 scopus 로고    scopus 로고
    • The effect ofMMPinhibitorGM6001 on early fibroblastmediated collagen matrix contraction is correlated to a decrease in cell protrusive activity
    • doi:10.1016/j.ejcb.2010.09.008
    • Martin-Martin B, Tovell V, Dahlmann-Noor AH, Khaw PT, Bailly M(2011) The effect ofMMPinhibitorGM6001 on early fibroblastmediated collagen matrix contraction is correlated to a decrease in cell protrusive activity. Eur J Cell Biol 90(1):26-36. doi:10.1016/ j.ejcb.2010.09.008
    • (2011) Eur J Cell Biol , vol.90 , Issue.1 , pp. 26-36
    • Martin-Martin, B.1    Tovell, V.2    Dahlmann-Noor, A.H.3    Khaw, P.T.4    Bailly, M.5
  • 58
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cellmigration
    • Sieg DJ, Hauck CR, Schlaepfer DD (1999) Required role of focal adhesion kinase (FAK) for integrin-stimulated cellmigration. JCell Sci 112(Pt 16):2677-2691
    • (1999) JCell Sci , vol.112 , Issue.PART 16 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 59
    • 0032400495 scopus 로고    scopus 로고
    • Cell migration strategies in 3-D extracellular matrix: Differences in morphology, cell matrix interactions, and integrin function
    • doi:10.1002/(SICI)1097-0029(19981201)43: 5<369:AID-JEMT3>3.0.CO;2-6
    • Friedl P, Zanker KS, Brocker EB (1998) Cell migration strategies in 3-D extracellular matrix: differences in morphology, cell matrix interactions, and integrin function. Microsc Res Tech 43(5):369-378. doi: 10.1002/(SICI)1097- 0029(19981201)43:5<369:AID-JEMT3>3.0.CO;2-6
    • (1998) Microsc Res Tech , vol.43 , Issue.5 , pp. 369-378
    • Friedl, P.1    Zanker, K.S.2    Brocker, E.B.3


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