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Volumn 8, Issue 10, 2013, Pages

Proteolysis during Tumor Cell Extravasation In Vitro: Metalloproteinase Involvement across Tumor Cell Types

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA V BETA 3; FURIN; GELATINASE A; GELATINASE B; HERMES ANTIGEN; MATRIX METALLOPROTEINASE 14; METALLOPROTEINASE; PROTEINASE; UNCLASSIFIED DRUG; CELL ADHESION MOLECULE;

EID: 84885970985     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0078413     Document Type: Article
Times cited : (35)

References (68)
  • 1
    • 84876019734 scopus 로고    scopus 로고
    • Missing the target: matrix metalloproteinase antitargets in inflammation and cancer CM
    • doi:10.1016/j.tips.2013.02.004
    • Dufour A, Overall CM, (2013) Missing the target: matrix metalloproteinase antitargets in inflammation and cancer CM. Trends Pharmacol Sci 34: 233-242. doi:10.1016/j.tips.2013.02.004. PubMed: 23541335.
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 233-242
    • Dufour, A.1    Overall, C.M.2
  • 2
    • 73449125521 scopus 로고    scopus 로고
    • Proteomic identification of multitasking proteins in unexpected locations complicates drug targeting
    • doi:10.1038/nrd2945
    • Butler GS, Overall CM, (2009) Proteomic identification of multitasking proteins in unexpected locations complicates drug targeting. Nat Rev Drug Discov 8: 935-948. doi:10.1038/nrd2945. PubMed: 19949400.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 935-948
    • Butler, G.S.1    Overall, C.M.2
  • 3
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • doi:10.1038/nrc745
    • Egeblad M, Werb Z, (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2: 161-174. doi:10.1038/nrc745. PubMed: 11990853.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 4
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • doi:10.1074/jbc.270.10.5331
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, et al. (1995) Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 270: 5331-5338. doi:10.1074/jbc.270.10.5331. PubMed: 7890645.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5
  • 5
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • doi:10.1074/jbc.275.16.12080
    • Hernandez-Barrantes S, Toth M, Bernardo MM, Yurkova M, Gervasi DC, et al. (2000) Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J Biol Chem 275: 12080-12089. doi:10.1074/jbc.275.16.12080. PubMed: 10766841.
    • (2000) J Biol Chem , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3    Yurkova, M.4    Gervasi, D.C.5
  • 6
    • 0033828585 scopus 로고    scopus 로고
    • Matrix metalloproteinases in human melanoma
    • doi:10.1046/j.1523-1747.2000.00068.x
    • Hofmann UB, Westphal JR, van Muijen GNP, Ruiter DJ, (2000) Matrix metalloproteinases in human melanoma. J Invest Dermatol 115: 337-344. doi:10.1046/j.1523-1747.2000.00068.x. PubMed: 10951266.
    • (2000) J Invest Dermatol , vol.115 , pp. 337-344
    • Hofmann, U.B.1    Westphal, J.R.2    van Muijen, G.N.P.3    Ruiter, D.J.4
  • 7
    • 0034671857 scopus 로고    scopus 로고
    • Domain interactions in the gelatinase A-TIMP-2-MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation
    • doi:10.1074/jbc.M005932200
    • Overall CM, Tam E, McQuibban GA, Morrison C, Wallon UM, et al. (2000) Domain interactions in the gelatinase A-TIMP-2-MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation. J Biol Chem 275: 39497-39506. doi:10.1074/jbc.M005932200. PubMed: 10991943.
    • (2000) J Biol Chem , vol.275 , pp. 39497-39506
    • Overall, C.M.1    Tam, E.2    McQuibban, G.A.3    Morrison, C.4    Wallon, U.M.5
  • 8
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • doi:10.1016/S0955-0674(96)80116-5
    • Basbaum CB, Werb Z, (1996) Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr Opin Cell Biol 8: 731-738. doi:10.1016/S0955-0674(96)80116-5. PubMed: 8939664.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 731-738
    • Basbaum, C.B.1    Werb, Z.2
  • 9
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • doi:10.1091/mbc.11.7.2387
    • Yana I, Weiss SJ, (2000) Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol Cell Biol 11: 2387-2401. doi:10.1091/mbc.11.7.2387. PubMed: 10888676.
    • (2000) Mol Cell Biol , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 10
    • 33748644942 scopus 로고    scopus 로고
    • Furin Regulates the intracellular activation and the uptake rate of cell surface- associated MT1-MMP
    • doi:10.1038/sj.onc.1209572
    • Remacle AG, Rozanov DV, Fugere M, Day R, Strongin AY, (2006) Furin Regulates the intracellular activation and the uptake rate of cell surface- associated MT1-MMP. Oncogene 25: 5648-5655. doi:10.1038/sj.onc.1209572. PubMed: 16636666.
    • (2006) Oncogene , vol.25 , pp. 5648-5655
    • Remacle, A.G.1    Rozanov, D.V.2    Fugere, M.3    Day, R.4    Strongin, A.Y.5
  • 11
    • 80053196585 scopus 로고    scopus 로고
    • Intradomain cleavage of inhibitory prodomain is essential to protumorigenic function of membrane type-1 matrix metalloproteinase (MT1-MMP) in vivo
    • doi:10.1074/jbc.M111.264036
    • Golubkov VS, Chernov AV, Strongin AY, (2011) Intradomain cleavage of inhibitory prodomain is essential to protumorigenic function of membrane type-1 matrix metalloproteinase (MT1-MMP) in vivo. J Biol Chem 286: 34215-34223. doi:10.1074/jbc.M111.264036. PubMed: 21832072.
    • (2011) J Biol Chem , vol.286 , pp. 34215-34223
    • Golubkov, V.S.1    Chernov, A.V.2    Strongin, A.Y.3
  • 12
    • 41649118952 scopus 로고    scopus 로고
    • A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness
    • Coppola JM, Bhojani MS, Ross RD, Rehemtulla A, (2008) A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness. Neoplasia 10: 363-370. PubMed: 18392131.
    • (2008) Neoplasia , vol.10 , pp. 363-370
    • Coppola, J.M.1    Bhojani, M.S.2    Ross, R.D.3    Rehemtulla, A.4
  • 13
    • 0033601360 scopus 로고    scopus 로고
    • Furin-independent pathway of membrane type 1-matrix metalloproteinase activation in rabbit dermal fibroblasts
    • doi:10.1074/jbc.274.52.37280
    • Sato T, Kondo T, Fujisawa T, Seiki M, Ito A, (1999) Furin-independent pathway of membrane type 1-matrix metalloproteinase activation in rabbit dermal fibroblasts. J Biol Chem 274: 37280-37284. doi:10.1074/jbc.274.52.37280. PubMed: 10601293.
    • (1999) J Biol Chem , vol.274 , pp. 37280-37284
    • Sato, T.1    Kondo, T.2    Fujisawa, T.3    Seiki, M.4    Ito, A.5
  • 14
    • 0035854654 scopus 로고    scopus 로고
    • Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys-574, the active site Glu-240 and furin cleavage motifs in oligomerization, procession and self-proteolysis of MT1-MMP expressed in breast carcinoma cells
    • doi:10.1074/jbc.M007921200
    • Rozanov DV, Deryugina EI, Ratnikov BI, Monosov EZ, Marchenko GN, et al. (2001) Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys-574, the active site Glu-240 and furin cleavage motifs in oligomerization, procession and self-proteolysis of MT1-MMP expressed in breast carcinoma cells. J Biol Chem 276: 25705-25714. doi:10.1074/jbc.M007921200. PubMed: 11335709.
    • (2001) J Biol Chem , vol.276 , pp. 25705-25714
    • Rozanov, D.V.1    Deryugina, E.I.2    Ratnikov, B.I.3    Monosov, E.Z.4    Marchenko, G.N.5
  • 15
    • 0030977009 scopus 로고    scopus 로고
    • Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants
    • doi:10.1093/emboj/16.9.2319
    • Mazzieri R, Masiero L, Zanetta L, Monea S, Onisto M, et al. (1997) Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants. EMBO J 16: 2319-2332. doi:10.1093/emboj/16.9.2319. PubMed: 9171346.
    • (1997) EMBO J , vol.16 , pp. 2319-2332
    • Mazzieri, R.1    Masiero, L.2    Zanetta, L.3    Monea, S.4    Onisto, M.5
  • 16
    • 15844420283 scopus 로고    scopus 로고
    • Localization of Matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αvβ3
    • Brooks PC, Stromblad S, Sanders LC, von Schalscha TL, Aimes RT, et al. (1996) Localization of Matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin αvβ3. Cell 85: 638-693.
    • (1996) Cell , vol.85 , pp. 638-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3    von Schalscha, T.L.4    Aimes, R.T.5
  • 17
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • doi:10.1016/S0092-8674(00)80931-9
    • Brooks PC, Silletti S, von Schalscha TL, Friedlander M, Cheresh DA, (1998) Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell 92: 391-400. doi:10.1016/S0092-8674(00)80931-9. PubMed: 9476898.
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 18
    • 0033969626 scopus 로고    scopus 로고
    • Adhesion receptors and cell invasion: mechanisms of integrin-guided degradation of extracellular matrix
    • doi:10.1007/s000180050496
    • Ivaska J, Heino J, (2000) Adhesion receptors and cell invasion: mechanisms of integrin-guided degradation of extracellular matrix. Cell Mol Life Sci 57: 16-24. doi:10.1007/s000180050496. PubMed: 10949578.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 16-24
    • Ivaska, J.1    Heino, J.2
  • 19
    • 59449108662 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2-integrin αvβ3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: a computational time-lapse study
    • doi:10.1091/mbc.E07-05-0480
    • Rupp RA, Visconti RP, Czirok A, Cheresh DA, Little CD, (2008) Matrix metalloproteinase 2-integrin αvβ3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: a computational time-lapse study. Mol Cell Biol 19: 5529-5540. doi:10.1091/mbc.E07-05-0480.
    • (2008) Mol Cell Biol , vol.19 , pp. 5529-5540
    • Rupp, R.A.1    Visconti, R.P.2    Czirok, A.3    Cheresh, D.A.4    Little, C.D.5
  • 20
    • 14844315007 scopus 로고    scopus 로고
    • Transmigration of human ovarian adenocarcinooma cells through endothelial extracellular matrix involves αv integrins and the participation of MMP2
    • doi:10.1002/ijc.20778
    • Leroy-Dudal J, Demeilliers C, Gallet O, Pauthe E, Dutoit S, et al. (2005) Transmigration of human ovarian adenocarcinooma cells through endothelial extracellular matrix involves αv integrins and the participation of MMP2. Int J Cancer 114: 531-543. doi:10.1002/ijc.20778. PubMed: 15609323.
    • (2005) Int J Cancer , vol.114 , pp. 531-543
    • Leroy-Dudal, J.1    Demeilliers, C.2    Gallet, O.3    Pauthe, E.4    Dutoit, S.5
  • 21
    • 34948853273 scopus 로고    scopus 로고
    • A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier
    • doi:10.1007/s10585-007-9086-6
    • Kargozaran H, Yuan SY, Breslin JW, Watson KD, Gaudreault N, et al. (2007) A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier. Clin Exp Metastasis 24: 495-502. doi:10.1007/s10585-007-9086-6. PubMed: 17653824.
    • (2007) Clin Exp Metastasis , vol.24 , pp. 495-502
    • Kargozaran, H.1    Yuan, S.Y.2    Breslin, J.W.3    Watson, K.D.4    Gaudreault, N.5
  • 22
    • 84864398223 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 promotes αvβ3 integrin-mediated adhesion and migration of human melanoma cells by cleaving fibronectin
    • doi:10.1371/journal.pone.0041591
    • Jiao Y, Feng X, Zhan Y, Wang R, Zheng S, et al. (2012) Matrix metalloproteinase-2 promotes αvβ3 integrin-mediated adhesion and migration of human melanoma cells by cleaving fibronectin. PLOS ONE 7: e41591. doi:10.1371/journal.pone.0041591. PubMed: 22848537.
    • (2012) PLOS ONE , vol.7
    • Jiao, Y.1    Feng, X.2    Zhan, Y.3    Wang, R.4    Zheng, S.5
  • 23
    • 0032493657 scopus 로고    scopus 로고
    • The involvement of the fibronectin type II-like of human gelatinase A in cell surface localization and activation
    • doi:10.1074/jbc.273.32.20622
    • Steffensen B, Bigg HF, Overall CM, (1998) The involvement of the fibronectin type II-like of human gelatinase A in cell surface localization and activation. J Biol Chem 273: 20622-20628. doi:10.1074/jbc.273.32.20622. PubMed: 9685420.
    • (1998) J Biol Chem , vol.273 , pp. 20622-20628
    • Steffensen, B.1    Bigg, H.F.2    Overall, C.M.3
  • 24
    • 0033230113 scopus 로고    scopus 로고
    • Membrane associated matrix metalloproteinases in metastasis
    • doi:10.1002/(SICI)1521-1878(199911)21:11
    • Ellerbroek SM, Stack MS, (1999) Membrane associated matrix metalloproteinases in metastasis. BioEssays 21: 940-949. doi:10.1002/(SICI)1521-1878(199911)21:11. PubMed: 10517867.
    • (1999) BioEssays , vol.21 , pp. 940-949
    • Ellerbroek, S.M.1    Stack, M.S.2
  • 25
    • 0025012050 scopus 로고
    • Integrin distribution in malignant melanoma: association of the β3 subunit with tumor progression
    • Albelda SM, Mette SA, Elder DE, (1990) Integrin distribution in malignant melanoma: association of the β3 subunit with tumor progression. Cancer Res 50: 6757-6764. PubMed: 2208139.
    • (1990) Cancer Res , vol.50 , pp. 6757-6764
    • Albelda, S.M.1    Mette, S.A.2    Elder, D.E.3
  • 26
    • 0026670584 scopus 로고
    • CD44H regulates tumor cell migration of hyaluronate-coated substrate
    • doi:10.1083/jcb.118.4.971
    • Thomas L, Byers HR, Vink J, Stamenkovic I, (1992) CD44H regulates tumor cell migration of hyaluronate-coated substrate. J Cell Biol 118: 971-977. doi:10.1083/jcb.118.4.971. PubMed: 1380003.
    • (1992) J Cell Biol , vol.118 , pp. 971-977
    • Thomas, L.1    Byers, H.R.2    Vink, J.3    Stamenkovic, I.4
  • 27
    • 0031808063 scopus 로고    scopus 로고
    • CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells
    • doi:10.1002/(SICI)1097-4652(199807)176:1
    • Bourguignon LY, Gunja-Smith Z, Iida N, Young LJ, Muller WJ, et al. (1998) CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J Cell Physiol 176: 206-215. doi:10.1002/(SICI)1097-4652(199807)176:1. PubMed: 9618160.
    • (1998) J Cell Physiol , vol.176 , pp. 206-215
    • Bourguignon, L.Y.1    Gunja-Smith, Z.2    Iida, N.3    Young, L.J.4    Muller, W.J.5
  • 28
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • doi:10.1101/gad.13.1.35
    • Yu Q, Stamenkovic I, (1999) Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev 13: 35-48. doi:10.1101/gad.13.1.35. PubMed: 9887098.
    • (1999) Genes Dev , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 29
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I, (2000) Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 14: 163-176. PubMed: 10652271.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 30
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • doi:10.1083/jcb.153.5.893
    • Kajita M, Itoh Y, Chiba T, (2001) Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol 153: 893-904. doi:10.1083/jcb.153.5.893. PubMed: 11381077.
    • (2001) J Cell Biol , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3
  • 31
    • 0036683241 scopus 로고    scopus 로고
    • CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
    • doi:10.1093/emboj/cdf411
    • Mori H, Tomari T, Koshikawa N, Kajita M, Itoh Y, et al. (2002) CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. EMBO J 21: 3949-3959. doi:10.1093/emboj/cdf411. PubMed: 12145196.
    • (2002) EMBO J , vol.21 , pp. 3949-3959
    • Mori, H.1    Tomari, T.2    Koshikawa, N.3    Kajita, M.4    Itoh, Y.5
  • 32
    • 47249093296 scopus 로고    scopus 로고
    • α4β1 and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not in normal B cells
    • doi:10.1182/blood-2007-08-109249
    • Redondo-Muñoz J, Ugarte-Berzal E, García-Marco JA, Hernandez del Cerro M, Van den Steen PE, et al. (2008) α4β1 and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not in normal B cells. Blood 112: 169-178. doi:10.1182/blood-2007-08-109249. PubMed: 18326820.
    • (2008) Blood , vol.112 , pp. 169-178
    • Redondo-Muñoz, J.1    Ugarte-Berzal, E.2    García-Marco, J.A.3    Hernandez del Cerro, M.4    Van den Steen, P.E.5
  • 33
    • 76249122104 scopus 로고    scopus 로고
    • Characterization of the expression of variant and standard CD44 in prostate cancer cells: Identification of the possible molecular mechanism of CD44/MMP9 complex formation on the cell surface
    • doi:10.1002/jcb.22248
    • Desai B, Ma T, Zhu J, Chellaiah MA, (2009) Characterization of the expression of variant and standard CD44 in prostate cancer cells: Identification of the possible molecular mechanism of CD44/MMP9 complex formation on the cell surface. J Cell Biochem 108: 272-284. doi:10.1002/jcb.22248. PubMed: 19582779.
    • (2009) J Cell Biochem , vol.108 , pp. 272-284
    • Desai, B.1    Ma, T.2    Zhu, J.3    Chellaiah, M.A.4
  • 34
    • 79960167042 scopus 로고    scopus 로고
    • The role of a new CD44st in increasing the invasion capability of the human breast cancer cell line MCF-7
    • doi:10.1186/1471-2407-11-290
    • Fang XJ, Jiang H, Zhao XP, Jiang WM, (2011) The role of a new CD44st in increasing the invasion capability of the human breast cancer cell line MCF-7. BMC Cancer 11: 290-300. doi:10.1186/1471-2407-11-290. PubMed: 21749678.
    • (2011) BMC Cancer , vol.11 , pp. 290-300
    • Fang, X.J.1    Jiang, H.2    Zhao, X.P.3    Jiang, W.M.4
  • 35
    • 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, et al. (2003) Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J Cell Biol 160: 267-277. doi:10.1083/jcb.200209006. PubMed: 12527751.
    • (2003) J Cell Biol , vol.160 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3    Engelke, K.4    von Andrian, U.H.5
  • 36
    • 0028129494 scopus 로고
    • Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth
    • Koop S, Khokha R, Schmidt EE, MacDonald IC, Morris VL, et al. (1994) Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth. Cancer Res 54: 4791-4797. PubMed: 8062280.
    • (1994) Cancer Res , vol.54 , pp. 4791-4797
    • Koop, S.1    Khokha, R.2    Schmidt, E.E.3    MacDonald, I.C.4    Morris, V.L.5
  • 37
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • doi:10.1007/s10555-006-7886-9
    • Deryugina EI, Quigley JP, (2006) Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev 25: 9-34. doi:10.1007/s10555-006-7886-9. PubMed: 16680569.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 38
    • 0031752956 scopus 로고    scopus 로고
    • Cell shape changes and cytoskeleton reorganization during transendothelial migration of human melanoma cells
    • doi:10.1007/s004410051129
    • Voura EB, Sandig M, Kalnins VI, Siu CH, (1998) Cell shape changes and cytoskeleton reorganization during transendothelial migration of human melanoma cells. Cell Tissue Res 293: 375-387. doi:10.1007/s004410051129. PubMed: 9716727.
    • (1998) Cell Tissue Res , vol.293 , pp. 375-387
    • Voura, E.B.1    Sandig, M.2    Kalnins, V.I.3    Siu, C.H.4
  • 39
    • 0032211229 scopus 로고    scopus 로고
    • Cell-cell interactions during transendothelial migration of tumor cells
    • doi:10.1002/(SICI)1097-0029(19981101)43:3
    • Voura EB, Sandig M, Siu CH, (1998) Cell-cell interactions during transendothelial migration of tumor cells. Microsc Res Tech 43: 265-275. doi:10.1002/(SICI)1097-0029(19981101)43:3. PubMed: 9840805.
    • (1998) Microsc Res Tech , vol.43 , pp. 265-275
    • Voura, E.B.1    Sandig, M.2    Siu, C.H.3
  • 40
    • 0034856020 scopus 로고    scopus 로고
    • Platelet-endothelial cell adhesion molecule-1 (CD31) redistributes from the endothelial junction and is not required for the transendothelial migration of melanoma cells
    • doi:10.1023/A:1011884807746
    • Voura EB, Chen N, Kalnins VI, Siu CH, (2000) Platelet-endothelial cell adhesion molecule-1 (CD31) redistributes from the endothelial junction and is not required for the transendothelial migration of melanoma cells. Clin Exp Metastasis 18: 527-532. doi:10.1023/A:1011884807746. PubMed: 11592310.
    • (2000) Clin Exp Metastasis , vol.18 , pp. 527-532
    • Voura, E.B.1    Chen, N.2    Kalnins, V.I.3    Siu, C.H.4
  • 41
    • 0030728116 scopus 로고    scopus 로고
    • Role of cadherins in the transendothelial migration of melanoma cells in culture
    • doi:10.1002/(SICI)1097-0169(1997)38:4
    • Sandig M, Voura EB, Kalnins VI, Siu CH, (1997) Role of cadherins in the transendothelial migration of melanoma cells in culture. Cell Motil Cytoskel 38: 351-364. doi:10.1002/(SICI)1097-0169(1997)38:4. PubMed: 9415377.
    • (1997) Cell Motil Cytoskel , vol.38 , pp. 351-364
    • Sandig, M.1    Voura, E.B.2    Kalnins, V.I.3    Siu, C.H.4
  • 42
    • 0035158462 scopus 로고    scopus 로고
    • Involvement of the integrin αvβ3 and the cell adhesion molecule L1 in the transendothelial migration of melanoma cells
    • doi:10.1091/mbc.12.9.2699
    • Voura EB, Ramjeesingh RA, Montgomery AM, Siu CH, (2001) Involvement of the integrin αvβ3 and the cell adhesion molecule L1 in the transendothelial migration of melanoma cells. Mol Cell Biol 12: 2699-2710. doi:10.1091/mbc.12.9.2699.
    • (2001) Mol Cell Biol , vol.12 , pp. 2699-2710
    • Voura, E.B.1    Ramjeesingh, R.A.2    Montgomery, A.M.3    Siu, C.H.4
  • 43
    • 0033597728 scopus 로고    scopus 로고
    • Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines
    • doi:10.1074/jbc.274.30.21056
    • Kurschat P, Zigrino P, Nischt R, Breitkopf K, Steurer P, et al. (1999) Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines. J Biol Chem 274: 21056-21062. doi:10.1074/jbc.274.30.21056. PubMed: 10409657.
    • (1999) J Biol Chem , vol.274 , pp. 21056-21062
    • Kurschat, P.1    Zigrino, P.2    Nischt, R.3    Breitkopf, K.4    Steurer, P.5
  • 44
    • 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, Allen E, Punturieri A, Yana I, Weiss WJ, (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: 1309-1323.
    • (2000) J Cell Biol , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, W.J.5
  • 45
    • 0033548069 scopus 로고    scopus 로고
    • Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV
    • doi:10.1074/jbc.274.7.4421
    • Overall CM, King AE, Sam DK, Ong AD, Lau TT, et al. (1999) Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV. J Biol Chem 274: 4421-4429. doi:10.1074/jbc.274.7.4421. PubMed: 9933646.
    • (1999) J Biol Chem , vol.274 , pp. 4421-4429
    • Overall, C.M.1    King, A.E.2    Sam, D.K.3    Ong, A.D.4    Lau, T.T.5
  • 46
    • 0027270903 scopus 로고
    • The synthesis of inhibitors for processing proteases and their action on the Kex2 protease of yeast
    • Angliker H, Wikstrom P, Shaw E, Brenner C, Fuller RS, (1993) The synthesis of inhibitors for processing proteases and their action on the Kex2 protease of yeast. Biochem J 293: 75-81. PubMed: 8328974.
    • (1993) Biochem J , vol.293 , pp. 75-81
    • Angliker, H.1    Wikstrom, P.2    Shaw, E.3    Brenner, C.4    Fuller, R.S.5
  • 47
    • 0032513136 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor
    • doi:10.1016/S0014-5793(98)00187-2
    • Maquoi E, Noël A, Frankenne F, Angliker H, Murphy G, et al. (1998) Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor. FEBS Lett 424: 262-266. doi:10.1016/S0014-5793(98)00187-2. PubMed: 9539163.
    • (1998) FEBS Lett , vol.424 , pp. 262-266
    • Maquoi, E.1    Noël, A.2    Frankenne, F.3    Angliker, H.4    Murphy, G.5
  • 48
    • 0027856038 scopus 로고
    • Inhibition of matrix metalloproteinase 9 activation by a specific monoclonal antibody
    • doi:10.1089/hyb.1993.12.349
    • Ramos-DeSimone N, Moll UM, Quigley JP, French DL, (1993) Inhibition of matrix metalloproteinase 9 activation by a specific monoclonal antibody. Hybridoma 12: 349-363. doi:10.1089/hyb.1993.12.349. PubMed: 8244415.
    • (1993) Hybridoma , vol.12 , pp. 349-363
    • Ramos-DeSimone, N.1    Moll, U.M.2    Quigley, J.P.3    French, D.L.4
  • 49
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha v beta 3, and alpha 5 beta 1 integrins
    • Pfaff M, Tangemann K, Muller B, Gurrath M, Muller G, et al. (1994) Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha v beta 3, and alpha 5 beta 1 integrins. J Biol Chem 269: 20233-20238.
    • (1994) J Biol Chem , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Muller, B.3    Gurrath, M.4    Muller, G.5
  • 50
    • 1842331535 scopus 로고    scopus 로고
    • Altered tumor growth and metastasis of a T-cell lymphoma in TIMP-1 transgenic mice
    • Krüger A, Fata JE, Khokha R, (1997) Altered tumor growth and metastasis of a T-cell lymphoma in TIMP-1 transgenic mice. Blood 90: 1993-2000. PubMed: 9292534.
    • (1997) Blood , vol.90 , pp. 1993-2000
    • Krüger, A.1    Fata, J.E.2    Khokha, R.3
  • 51
    • 0032493066 scopus 로고    scopus 로고
    • Host TIMP-1 overexpression confers resistance to experimental brain metastasis of a fibrosarcoma cell line
    • doi:10.1038/sj.onc.1201774
    • Krüger A, Sanchez-Sweatman OH, Martin DC, Fata JE, Ho AT, et al. (1998) Host TIMP-1 overexpression confers resistance to experimental brain metastasis of a fibrosarcoma cell line. Oncogene 16: 2419-2423. doi:10.1038/sj.onc.1201774. PubMed: 9620561.
    • (1998) Oncogene , vol.16 , pp. 2419-2423
    • Krüger, A.1    Sanchez-Sweatman, O.H.2    Martin, D.C.3    Fata, J.E.4    Ho, A.T.5
  • 52
    • 80054997801 scopus 로고    scopus 로고
    • New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression
    • Bauvois B, (2012) New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression. Biochim Biophys Acta 1825: 29-36. PubMed: 22020293.
    • (2012) Biochim Biophys Acta , vol.1825 , pp. 29-36
    • Bauvois, B.1
  • 53
    • 53949121835 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor, MMI270 (CGS27023A) inhibited hematogenic metastasis of B16 melanoma cells in both experimental and spontaneous metastasis models
    • doi:10.1007/s10585-008-9198-7
    • Kasaoka T, Nishiyama H, Okada M, Nakajima M, (2008) Matrix metalloproteinase inhibitor, MMI270 (CGS27023A) inhibited hematogenic metastasis of B16 melanoma cells in both experimental and spontaneous metastasis models. Clin Exp Metastasis 25: 827-834. doi:10.1007/s10585-008-9198-7. PubMed: 18668328.
    • (2008) Clin Exp Metastasis , vol.25 , pp. 827-834
    • Kasaoka, T.1    Nishiyama, H.2    Okada, M.3    Nakajima, M.4
  • 54
    • 0037424402 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms
    • doi:10.1074/jbc.M213246200
    • Rozanov DV, Strongin AY, (2003) Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms. J Biol Chem 278: 8257-8260. doi:10.1074/jbc.M213246200. PubMed: 12514192.
    • (2003) J Biol Chem , vol.278 , pp. 8257-8260
    • Rozanov, D.V.1    Strongin, A.Y.2
  • 55
    • 9444290419 scopus 로고    scopus 로고
    • Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP
    • doi:10.1083/jcb.200408028
    • Sabeh F, Ota I, Holmbeck K, Birkedal-Hansen H, Soloway P, et al. (2004) Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP. J Cell Biol 167: 769-781. doi:10.1083/jcb.200408028. PubMed: 15557125.
    • (2004) J Cell Biol , vol.167 , pp. 769-781
    • Sabeh, F.1    Ota, I.2    Holmbeck, K.3    Birkedal-Hansen, H.4    Soloway, P.5
  • 56
    • 0033606774 scopus 로고    scopus 로고
    • Airway epithelial cell migration dynamics: MMP-9 role in cell extracellular matrix remodeling
    • doi:10.1083/jcb.146.2.517
    • Legrand C, Gilles C, Zahm JM, Polette M, Buisson AC, et al. (1999) Airway epithelial cell migration dynamics: MMP-9 role in cell extracellular matrix remodeling. J Cell Biol 146: 517-529. doi:10.1083/jcb.146.2.517. PubMed: 10427102.
    • (1999) J Cell Biol , vol.146 , pp. 517-529
    • Legrand, C.1    Gilles, C.2    Zahm, J.M.3    Polette, M.4    Buisson, A.C.5
  • 57
    • 0029029325 scopus 로고
    • Membrane vesicles shed into the extracellular medium by human breast carcinoma cells carry tumor-associated surface antigens
    • Dolo V, Adobati E, Canevari S, Picone AM, Vittorelli ML, (1995) Membrane vesicles shed into the extracellular medium by human breast carcinoma cells carry tumor-associated surface antigens. Clin Exp Metastasis 4: 277-286. PubMed: 7606890.
    • (1995) Clin Exp Metastasis , vol.4 , pp. 277-286
    • Dolo, V.1    Adobati, E.2    Canevari, S.3    Picone, A.M.4    Vittorelli, M.L.5
  • 58
    • 0018880842 scopus 로고
    • Arrest and metastasis of blood-borne tumor cells are modified by fusion of plasma membrane vesicles from highly metastatic cells
    • doi:10.1073/pnas.77.1.399
    • Poste G, Nicolson GL, (1980) Arrest and metastasis of blood-borne tumor cells are modified by fusion of plasma membrane vesicles from highly metastatic cells. Proc Natl Acad Sci U_S_A 77: 399-403. doi:10.1073/pnas.77.1.399. PubMed: 6928631.
    • (1980) Proc Natl Acad Sci U_S_A , vol.77 , pp. 399-403
    • Poste, G.1    Nicolson, G.L.2
  • 59
    • 0028409113 scopus 로고
    • Human breast carcinoma cells cultured in the presence of serum shed membrane vesicles rich in gelatinolytic activities
    • Dolo V, Ginestra A, Ghersi G, Nagase H, Vittorelli ML, (1994) Human breast carcinoma cells cultured in the presence of serum shed membrane vesicles rich in gelatinolytic activities. J Submicrosc Cytol Pathol 26: 173-180. PubMed: 8019942.
    • (1994) J Submicrosc Cytol Pathol , vol.26 , pp. 173-180
    • Dolo, V.1    Ginestra, A.2    Ghersi, G.3    Nagase, H.4    Vittorelli, M.L.5
  • 60
    • 0030758034 scopus 로고    scopus 로고
    • Urokinase plasminogen activator and gelatinases are associated with membrane vesicles shed by human HT1080 fibrosarcoma cells
    • doi:10.1074/jbc.272.27.17216
    • Ginestra A, Monea S, Seghezzi G, Dolo V, Nagase H, et al. (1997) Urokinase plasminogen activator and gelatinases are associated with membrane vesicles shed by human HT1080 fibrosarcoma cells. J Biol Chem 272: 17216-17222. doi:10.1074/jbc.272.27.17216. PubMed: 9202045.
    • (1997) J Biol Chem , vol.272 , pp. 17216-17222
    • Ginestra, A.1    Monea, S.2    Seghezzi, G.3    Dolo, V.4    Nagase, H.5
  • 61
    • 0032190127 scopus 로고    scopus 로고
    • Selective localization of matrix metalloproteinase 9, beta 1 integrins, and human lymphocyte antigen class I molecules on membrane vesicles shed by 8701-BC breast carcinoma cells
    • Dolo V, Ginestra A, Cassarà D, Violini S, Lucania G, et al. (1998) Selective localization of matrix metalloproteinase 9, beta 1 integrins, and human lymphocyte antigen class I molecules on membrane vesicles shed by 8701-BC breast carcinoma cells. Cancer Res 58: 4468-4474. PubMed: 9766680.
    • (1998) Cancer Res , vol.58 , pp. 4468-4474
    • Dolo, V.1    Ginestra, A.2    Cassarà, D.3    Violini, S.4    Lucania, G.5
  • 62
    • 0032801787 scopus 로고    scopus 로고
    • Matrix-degrading proteinases are shed in membrane vesicles by ovarian cancer cells in vivo and in vitro
    • doi:10.1023/A:1006500406240
    • Dolo V, D'Ascenzo S, Violini S, Pompucci L, Festuccia C, et al. (1999) Matrix-degrading proteinases are shed in membrane vesicles by ovarian cancer cells in vivo and in vitro. Clin Exp Metastasis 17: 131-140. doi:10.1023/A:1006500406240. PubMed: 10411105.
    • (1999) Clin Exp Metastasis , vol.17 , pp. 131-140
    • Dolo, V.1    D'Ascenzo, S.2    Violini, S.3    Pompucci, L.4    Festuccia, C.5
  • 63
    • 59149094419 scopus 로고    scopus 로고
    • The collagen binding domain of gelatinase A modulates degradation of collagen IV by gelatinase B
    • doi:10.1016/j.jmb.2008.12.021
    • Gioia M, Monaco S, Van Den Steen PE, Sbardella D, Grasso G, et al. (2009) The collagen binding domain of gelatinase A modulates degradation of collagen IV by gelatinase B. J Mol Biol 386: 419-434. doi:10.1016/j.jmb.2008.12.021. PubMed: 19109975.
    • (2009) J Mol Biol , vol.386 , pp. 419-434
    • Gioia, M.1    Monaco, S.2    Van Den Steen, P.E.3    Sbardella, D.4    Grasso, G.5
  • 64
    • 78149231567 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase-9 dimers in cell migation design of inhibitory peptides
    • doi:10.1074/jbc.M109.091769
    • Dufour A, Zucker S, Sampson NS, Kuscu C, Cao J, (2010) Role of matrix metalloproteinase-9 dimers in cell migation design of inhibitory peptides. J Biol Chem 285: 35944-35956. doi:10.1074/jbc.M109.091769. PubMed: 20837483.
    • (2010) J Biol Chem , vol.285 , pp. 35944-35956
    • Dufour, A.1    Zucker, S.2    Sampson, N.S.3    Kuscu, C.4    Cao, J.5
  • 65
    • 84877807530 scopus 로고    scopus 로고
    • RANKL/RANK/MMP-1 molecular triad contributes to the metastatic phenotype of breast and prostate cancer cells in vitro
    • doi:10.1371/journal.pone.0063153
    • Casimiro S, Mohammad KS, Pires R, Tato-Costa J, Alho I, et al. (2013) RANKL/RANK/MMP-1 molecular triad contributes to the metastatic phenotype of breast and prostate cancer cells in vitro. PLOS ONE 8: e63153. doi:10.1371/journal.pone.0063153. PubMed: 23696795.
    • (2013) PLOS ONE , vol.8
    • Casimiro, S.1    Mohammad, K.S.2    Pires, R.3    Tato-Costa, J.4    Alho, I.5
  • 66
    • 84864123612 scopus 로고    scopus 로고
    • Highly invasive melanoma cells activate the vascular endothelium via an MMP-2/integrin αvβ5-induced secretion of VEGF-A
    • doi:10.1016/j.ajpath.2012.04.012
    • Desch A, Strozyk EA, Bauer AT, Huck V, Niemeyer V, et al. (2012) Highly invasive melanoma cells activate the vascular endothelium via an MMP-2/integrin αvβ5-induced secretion of VEGF-A. Am J Pathol 181: 693-705. doi:10.1016/j.ajpath.2012.04.012. PubMed: 22659470.
    • (2012) Am J Pathol , vol.181 , pp. 693-705
    • Desch, A.1    Strozyk, E.A.2    Bauer, A.T.3    Huck, V.4    Niemeyer, V.5
  • 67
    • 84859997943 scopus 로고    scopus 로고
    • Angiotensin II facilitates breast cancer cell migration and metastasis
    • doi:10.1371/journal.pone.0035667
    • Rodrigues-Ferreira S, Abdelkarim M, Dillenburg-Pilla P, Luissint AC, di-Tommaso A, et al. (2012) Angiotensin II facilitates breast cancer cell migration and metastasis. PLOS ONE 7: e35667. doi:10.1371/journal.pone.0035667. PubMed: 22536420.
    • (2012) PLOS ONE , vol.7
    • Rodrigues-Ferreira, S.1    Abdelkarim, M.2    Dillenburg-Pilla, P.3    Luissint, A.C.4    di-Tommaso, A.5
  • 68
    • 77955372512 scopus 로고    scopus 로고
    • Monoclonal antibody 4C5 prevents activation of MMP2 and MMP9 by disruption their interaction with extracellular HSP90 and inhibits formation of metastatic breast cancer cell deposits
    • doi:10.1186/1471-2121-11-51
    • Stellas D, Haidieh AE, Patsavoudi E, (2010) Monoclonal antibody 4C5 prevents activation of MMP2 and MMP9 by disruption their interaction with extracellular HSP90 and inhibits formation of metastatic breast cancer cell deposits. BMC Cell Biol 11: 51. doi:10.1186/1471-2121-11-51. PubMed: 20602761.
    • (2010) BMC Cell Biol , vol.11 , pp. 51
    • Stellas, D.1    Haidieh, A.E.2    Patsavoudi, E.3


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