메뉴 건너뛰기




Volumn 87, Issue 3-4 SPEC. ISS., 2005, Pages 329-342

Membrane type-matrix metalloproteinases and tumor progression

Author keywords

Cancer; Cell signaling; MT MMP; Protease inhibitors; Tumor angiogenesis

Indexed keywords

ALPHA 2 MACROGLOBULIN; BATIMASTAT; CELL ADHESION MOLECULE; CONNECTIVE TISSUE GROWTH FACTOR; FIBRONECTIN; LAMININ 1; LYMPHOCYTE ANTIGEN; MATRIX METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; PLASMINOGEN; SOMATOMEDIN BINDING PROTEIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG; VASCULOTROPIN; VITRONECTIN RECEPTOR;

EID: 15244352321     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.07.012     Document Type: Short Survey
Times cited : (128)

References (178)
  • 1
    • 0038236716 scopus 로고    scopus 로고
    • The basement membrane matrix in malignancy
    • Engbring J.A., and Kleinman H.K. The basement membrane matrix in malignancy J. Pathol. 200 2003 465 470
    • (2003) J. Pathol. , vol.200 , pp. 465-470
    • Engbring, J.A.1    Kleinman, H.K.2
  • 2
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behavior Annu. Rev. Cell Dev. Biol. 17 2001 463 516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 4
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., and Werb Z. New functions for the matrix metalloproteinases in cancer progression Nat. Rev. Cancer 2 2002 161 174
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 5
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • Lopez-Otin C., and Overall C.M. Protease degradomics: a new challenge for proteomics Nat. Rev. Mol. Cell Biol. 3 2002 509 519
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 6
    • 0038702657 scopus 로고    scopus 로고
    • RECK: A novel suppressor of malignancy linking oncogenic signaling to extracellular matrix remodeling
    • Noda M., Oh J., Takahashi R., Kondo S., Kitayama H., and Takahashi C. RECK: a novel suppressor of malignancy linking oncogenic signaling to extracellular matrix remodeling Cancer Metastasis Rev. 22 2003 167 175
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 167-175
    • Noda, M.1    Oh, J.2    Takahashi, R.3    Kondo, S.4    Kitayama, H.5    Takahashi, C.6
  • 7
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker A.H., Edwards D.R., and Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities J. Cell Sci. 115 2002 3719 3727
    • (2002) J. Cell Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 9
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens L.M., Fingleton B., and Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations Science 295 2002 2387 2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 10
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall C.M., and Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era Nat. Rev. Cancer 2 2002 657 672
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 11
    • 0033617532 scopus 로고    scopus 로고
    • Effects of angiogenesis inhibitors on multistage carcinogenesis in mice
    • Bergers G., Javaherian K., Lo K.M., Folkman J., and Hanahan D. Effects of angiogenesis inhibitors on multistage carcinogenesis in mice Science 284 1999 808 812
    • (1999) Science , vol.284 , pp. 808-812
    • Bergers, G.1    Javaherian, K.2    Lo, K.M.3    Folkman, J.4    Hanahan, D.5
  • 12
    • 0036133646 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme
    • Black R.A. Tumor necrosis factor-alpha converting enzyme Int. J. Biochem. Cell Biol. 34 2002 1 5
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1-5
    • Black, R.A.1
  • 13
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: The role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases J. Pathol. 200 2003 448 464
    • (2003) J. Pathol. , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 15
    • 0842308319 scopus 로고    scopus 로고
    • Transmembrane proteases in cell growth and invasion: New contributors to angiogenesis?
    • Bauvois B. Transmembrane proteases in cell growth and invasion: new contributors to angiogenesis? Oncogene 23 2004 317 329
    • (2004) Oncogene , vol.23 , pp. 317-329
    • Bauvois, B.1
  • 18
    • 0036793734 scopus 로고    scopus 로고
    • Cell-surface proteolysis, growth factor activation and intercellular communication in the progression of melanoma
    • Bogenrieder T., and Herlyn M. Cell-surface proteolysis, growth factor activation and intercellular communication in the progression of melanoma Crit Rev. Oncol. Hematol. 44 2002 1 15
    • (2002) Crit Rev. Oncol. Hematol. , vol.44 , pp. 1-15
    • Bogenrieder, T.1    Herlyn, M.2
  • 21
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., and Seiki M. A matrix metalloproteinase expressed on the surface of invasive tumour cells Nature 370 1994 61 65 (see comments)
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 22
    • 0037169483 scopus 로고    scopus 로고
    • A conserved sequence within the propeptide domain of membrane type 1:matrix metalloproteinase is critical for function as an intramolecular chaperone
    • Pavlaki M., Cao J., Hymowitz M., Chen W.T., Bahou W., and Zucker S. A conserved sequence within the propeptide domain of membrane type 1:matrix metalloproteinase is critical for function as an intramolecular chaperone J. Biol. Chem. 277 2002 2740 2749
    • (2002) J. Biol. Chem. , vol.277 , pp. 2740-2749
    • Pavlaki, M.1    Cao, J.2    Hymowitz, M.3    Chen, W.T.4    Bahou, W.5    Zucker, S.6
  • 23
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase a and express intrinsic matrix-degrading activity
    • Pei D., and Weiss S.J. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity J. Biol. Chem. 271 1996 9135 9140
    • (1996) J. Biol. Chem. , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 24
    • 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., and Weiss S.J. 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 2000 1309 1323
    • (2000) J. Cell Biol. , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 25
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana I., and Weiss S.J. Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases Mol. Biol. Cell 11 2000 2387 2401
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 26
    • 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, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells
    • Rozanov D.V., Deryugina E.I., Ratnikov B.I., Monosov E.Z., Marchenko G.N., Quigley J.P., and Strongin A.Y. 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, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells J. Biol. Chem. 276 2001 25705 25714
    • (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    Quigley, J.P.6    Strongin, A.Y.7
  • 27
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato H., Kinoshita T., Takino T., Nakayama K., and Seiki M. Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2 FEBS Lett. 393 1996 101 104
    • (1996) FEBS Lett. , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 28
    • 0036109679 scopus 로고    scopus 로고
    • MT-MMPs play pivotal roles in cancer dissemination
    • Yana I., and Seiki M. MT-MMPs play pivotal roles in cancer dissemination Clin. Exp. Metastasis 19 2002 209 215
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 209-215
    • Yana, I.1    Seiki, M.2
  • 29
    • 0029910358 scopus 로고    scopus 로고
    • Membrane type matrix metalloproteinase 1:activates pro-gelatinase a without furin cleavage of the N-terminal domain
    • Cao J., Rehemtulla A., Bahou W., and Zucker S. Membrane type matrix metalloproteinase 1:activates pro-gelatinase A without furin cleavage of the N-terminal domain J. Biol. Chem. 271 1996 30174 30180
    • (1996) J. Biol. Chem. , vol.271 , pp. 30174-30180
    • Cao, J.1    Rehemtulla, A.2    Bahou, W.3    Zucker, S.4
  • 30
    • 0031048966 scopus 로고    scopus 로고
    • Proteolytic activation of the precursor of membrane type 1:matrix metalloproteinase by human plasmin. A possible cell surface activator
    • Okumura Y., Sato H., Seiki M., and Kido H. Proteolytic activation of the precursor of membrane type 1:matrix metalloproteinase by human plasmin. A possible cell surface activator FEBS Lett. 402 1997 181 184
    • (1997) FEBS Lett. , vol.402 , pp. 181-184
    • Okumura, Y.1    Sato, H.2    Seiki, M.3    Kido, H.4
  • 31
    • 0032167522 scopus 로고    scopus 로고
    • Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor
    • Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J.J., Lichte A., Tschesche H., and Maskos K. Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor EMBO J. 17 1998 5238 5248
    • (1998) EMBO J. , vol.17 , pp. 5238-5248
    • Fernandez-Catalan, C.1    Bode, W.2    Huber, R.3    Turk, D.4    Calvete, J.J.5    Lichte, A.6    Tschesche, H.7    Maskos, K.8
  • 32
    • 0347130906 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features
    • Lang R., Braun M., Sounni N.E., Noel A., Frankenne F., Foidart J.M., Bode W., and Maskos K. Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features J. Mol. Biol. 336 2004 213 225
    • (2004) J. Mol. Biol. , vol.336 , pp. 213-225
    • Lang, R.1    Braun, M.2    Sounni, N.E.3    Noel, A.4    Frankenne, F.5    Foidart, J.M.6    Bode, W.7    Maskos, K.8
  • 33
    • 0035834666 scopus 로고    scopus 로고
    • Characterization of the role of the "mT-loop": An eight-amino acid insertion specific to progelatinase a (MMP2) activating membrane-type matrix metalloproteinases
    • English W.R., Holtz B., Vogt G., Knauper V., and Murphy G. Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases J. Biol. Chem. 276 2001 42018 42026
    • (2001) J. Biol. Chem. , vol.276 , pp. 42018-42026
    • English, W.R.1    Holtz, B.2    Vogt, G.3    Knauper, V.4    Murphy, G.5
  • 34
    • 0034719342 scopus 로고    scopus 로고
    • Human membrane type-2 matrix metalloproteinase is defective in cell-associated activation of progelatinase a
    • Miyamori H., Takino T., Seiki M., and Sato H. Human membrane type-2 matrix metalloproteinase is defective in cell-associated activation of progelatinase A Biochem. Biophys. Res. Commun. 267 2000 796 800
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 796-800
    • Miyamori, H.1    Takino, T.2    Seiki, M.3    Sato, H.4
  • 35
    • 0037358503 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis
    • Sounni N.E., Janssen M., Foidart J.M., and Noel A. Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis Matrix Biol. 22 2003 55 61
    • (2003) Matrix Biol. , vol.22 , pp. 55-61
    • Sounni, N.E.1    Janssen, M.2    Foidart, J.M.3    Noel, A.4
  • 36
    • 2542513460 scopus 로고    scopus 로고
    • Pathogenic role of matrix metalloproteases and their inhibitors in asthma and chronic obstructive pulmonary disease and therapeutic relevance of matrix metalloproteases inhibitors
    • Cataldo D.D., Gueders M.M., Rocks N., Sounni N.E., Evrard B., Bartsch P., Louis R., Noel A., and Foidart J.M. Pathogenic role of matrix metalloproteases and their inhibitors in asthma and chronic obstructive pulmonary disease and therapeutic relevance of matrix metalloproteases inhibitors Cell Mol. Biol. (Noisy. -le-grand) 49 2003 875 884
    • (2003) Cell Mol. Biol. (Noisy. -le-grand) , vol.49 , pp. 875-884
    • Cataldo, D.D.1    Gueders, M.M.2    Rocks, N.3    Sounni, N.E.4    Evrard, B.5    Bartsch, P.6    Louis, R.7    Noel, A.8    Foidart, J.M.9
  • 37
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y., Takamura A., Ito N., Maru Y., Sato H., Suenaga N., Aoki T., and Seiki M. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion EMBO J. 20 2001 4782 4793
    • (2001) EMBO J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 38
    • 1842581954 scopus 로고    scopus 로고
    • Membrane-type 1:matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the cupin superfamily: A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors
    • Uekita T., Gotoh I., Kinoshita T., Itoh Y., Sato H., Shiomi T., Okada Y., and Seiki M. Membrane-type 1:matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the cupin superfamily: a possible multifunctional protein acting as an invasion suppressor down-regulated in tumors J. Biol. Chem. 279 2004 12734 12743
    • (2004) J. Biol. Chem. , vol.279 , pp. 12734-12743
    • Uekita, T.1    Gotoh, I.2    Kinoshita, T.3    Itoh, Y.4    Sato, H.5    Shiomi, T.6    Okada, Y.7    Seiki, M.8
  • 39
    • 1542304781 scopus 로고    scopus 로고
    • Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal
    • Wang X., Ma D., Keski-Oja J., and Pei D. Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal J. Biol. Chem. 279 2004 9331 9336
    • (2004) J. Biol. Chem. , vol.279 , pp. 9331-9336
    • Wang, X.1    Ma, D.2    Keski-Oja, J.3    Pei, D.4
  • 41
    • 0035955469 scopus 로고    scopus 로고
    • Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP)
    • Gingras D., Bousquet-Gagnon N., Langlois S., Lachambre M.P., Annabi B., and Beliveau R. Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP) FEBS Lett. 507 2001 231 236
    • (2001) FEBS Lett. , vol.507 , pp. 231-236
    • Gingras, D.1    Bousquet-Gagnon, N.2    Langlois, S.3    Lachambre, M.P.4    Annabi, B.5    Beliveau, R.6
  • 42
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1:matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., and Okada Y. Membrane type 1:matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules J. Biol. Chem. 272 1997 2446 2451
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 44
    • 0242677702 scopus 로고    scopus 로고
    • MT1-MMP-dependent, apoptotic remodeling of unmineralized cartilage: A critical process in skeletal growth
    • Holmbeck K., Bianco P., Chrysovergis K., Yamada S., and Birkedal-Hansen H. MT1-MMP-dependent, apoptotic remodeling of unmineralized cartilage: a critical process in skeletal growth J. Cell Biol. 163 2003 661 671
    • (2003) J. Cell Biol. , vol.163 , pp. 661-671
    • Holmbeck, K.1    Bianco, P.2    Chrysovergis, K.3    Yamada, S.4    Birkedal-Hansen, H.5
  • 46
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka N., Allen E., Apel I.J., Gyetko M.R., and Weiss S.J. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins Cell 95 1998 365 377
    • (1998) Cell , vol.95 , pp. 365-377
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3    Gyetko, M.R.4    Weiss, S.J.5
  • 48
  • 50
    • 0033674182 scopus 로고    scopus 로고
    • Functional characterization of MT3-MMP in transfected MDCK cells: Progelatinase a activation and tubulogenesis in 3-D collagen lattice
    • Kang T., Yi J., Yang W., Wang X., Jiang A., and Pei D. Functional characterization of MT3-MMP in transfected MDCK cells: progelatinase A activation and tubulogenesis in 3-D collagen lattice FASEB J. 14 2000 2559 2568
    • (2000) FASEB J. , vol.14 , pp. 2559-2568
    • Kang, T.1    Yi, J.2    Yang, W.3    Wang, X.4    Jiang, A.5    Pei, D.6
  • 52
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo K., Takino T., Miyamori H., Kinsen H., Yoshizaki T., Furukawa M., and Sato H. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration J. Biol. Chem. 278 2003 40764 40770
    • (2003) J. Biol. Chem. , vol.278 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5    Furukawa, M.6    Sato, H.7
  • 53
    • 0032722873 scopus 로고    scopus 로고
    • Catalytic activities and substrate specificity of the human membrane type 4:matrix metalloproteinase catalytic domain
    • Wang Y., Johnson A.R., Ye Q.Z., and Dyer R.D. Catalytic activities and substrate specificity of the human membrane type 4:matrix metalloproteinase catalytic domain J. Biol. Chem. 274 1999 33043 33049
    • (1999) J. Biol. Chem. , vol.274 , pp. 33043-33049
    • Wang, Y.1    Johnson, A.R.2    Ye, Q.Z.3    Dyer, R.D.4
  • 54
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type 4:matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2
    • English W.R., Puente X.S., Freije J.M., Knauper V., Amour A., Merryweather A., Lopez-Otin C., and Murphy G. Membrane type 4:matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2 J. Biol. Chem. 275 2000 14046 14055
    • (2000) J. Biol. Chem. , vol.275 , pp. 14046-14055
    • English, W.R.1    Puente, X.S.2    Freije, J.M.3    Knauper, V.4    Amour, A.5    Merryweather, A.6    Lopez-Otin, C.7    Murphy, G.8
  • 55
    • 1642354112 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1
    • Gao G., Plaas A., Thompson V.P., Jin S., Zuo F., and Sandy J.D. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1 J. Biol. Chem. 279 2004 10042 10051
    • (2004) J. Biol. Chem. , vol.279 , pp. 10042-10051
    • Gao, G.1    Plaas, A.2    Thompson, V.P.3    Jin, S.4    Zuo, F.5    Sandy, J.D.6
  • 56
    • 0033152980 scopus 로고    scopus 로고
    • Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors
    • Llano E., Pendas A.M., Freije J.P., Nakano A., Knauper V., Murphy G., and Lopez-Otin C. Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors Cancer Res. 59 1999 2570 2576
    • (1999) Cancer Res. , vol.59 , pp. 2570-2576
    • Llano, E.1    Pendas, A.M.2    Freije, J.P.3    Nakano, A.4    Knauper, V.5    Murphy, G.6    Lopez-Otin, C.7
  • 57
    • 0141815661 scopus 로고    scopus 로고
    • Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils
    • Matsuda A., Itoh Y., Koshikawa N., Akizawa T., Yana I., and Seiki M. Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils J. Biol. Chem. 278 2003 36350 36357
    • (2003) J. Biol. Chem. , vol.278 , pp. 36350-36357
    • Matsuda, A.1    Itoh, Y.2    Koshikawa, N.3    Akizawa, T.4    Yana, I.5    Seiki, M.6
  • 58
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin A.Y., Collier I., Bannikov G., Marmer B.L., Grant G.A., and Goldberg G.I. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease J. Biol. Chem. 270 1995 5331 5338
    • (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    Goldberg, G.I.6
  • 59
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • Seiki M. Membrane-type matrix metalloproteinases APMIS 107 1999 137 143
    • (1999) APMIS , vol.107 , pp. 137-143
    • Seiki, M.1
  • 60
    • 0038026913 scopus 로고    scopus 로고
    • Role of pericellular proteolysis by membrane-type 1:matrix metalloproteinase in cancer invasion and angiogenesis
    • Seiki M., Koshikawa N., and Yana I. Role of pericellular proteolysis by membrane-type 1:matrix metalloproteinase in cancer invasion and angiogenesis Cancer Metastasis Rev. 22 2003 129 143
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 129-143
    • Seiki, M.1    Koshikawa, N.2    Yana, I.3
  • 64
    • 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., Bajou K., Remacle A., L'Hoir C., Krell H.W., Weidle U.H., Noel A., and Foidart J.M. Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation FEBS Lett. 405 1997 157 162
    • (1997) FEBS Lett. , vol.405 , pp. 157-162
    • Baramova, E.N.1    Bajou, K.2    Remacle, A.3    L'Hoir, C.4    Krell, H.W.5    Weidle, U.H.6    Noel, A.7    Foidart, J.M.8
  • 65
    • 0036497904 scopus 로고    scopus 로고
    • Expression of membrane type 1:matrix metalloproteinase (MT1-MMP) in A2058 melanoma cells is associated with MMP-2 activation and increased tumor growth and vascularization
    • Sounni N.E., Baramova E.N., Munaut C., Maquoi E., Frankenne F., Foidart J.M., and Noel A. Expression of membrane type 1:matrix metalloproteinase (MT1-MMP) in A2058 melanoma cells is associated with MMP-2 activation and increased tumor growth and vascularization Int. J. Cancer 98 2002 23 28
    • (2002) Int. J. Cancer , vol.98 , pp. 23-28
    • Sounni, N.E.1    Baramova, E.N.2    Munaut, C.3    Maquoi, E.4    Frankenne, F.5    Foidart, J.M.6    Noel, A.7
  • 67
    • 0035396863 scopus 로고    scopus 로고
    • Activation of pro-(matrix metalloproteinase-2) (pro-MMP-2) by thrombin is membrane-type-MMP-dependent in human umbilical vein endothelial cells and generates a distinct 63:kDa active species
    • Lafleur M.A., Hollenberg M.D., Atkinson S.J., Knauper V., Murphy G., and Edwards D.R. Activation of pro-(matrix metalloproteinase-2) (pro-MMP-2) by thrombin is membrane-type-MMP-dependent in human umbilical vein endothelial cells and generates a distinct 63:kDa active species Biochem. J. 357 2001 107 115
    • (2001) Biochem. J. , vol.357 , pp. 107-115
    • Lafleur, M.A.1    Hollenberg, M.D.2    Atkinson, S.J.3    Knauper, V.4    Murphy, G.5    Edwards, D.R.6
  • 68
    • 0034731479 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2
    • Toth M., Bernardo M.M., Gervasi D.C., Soloway P.D., Wang Z., Bigg H.F., Overall C.M., DeClerck Y.A., Tschesche H., Cher M.L., Brown S., Mobashery S., and Fridman R. Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2 J. Biol. Chem. 275 2000 41415 41423
    • (2000) J. Biol. Chem. , vol.275 , pp. 41415-41423
    • Toth, M.1    Bernardo, M.M.2    Gervasi, D.C.3    Soloway, P.D.4    Wang, Z.5    Bigg, H.F.6    Overall, C.M.7    Declerck, Y.A.8    Tschesche, H.9    Cher, M.L.10    Brown, S.11    Mobashery, S.12    Fridman, R.13
  • 69
    • 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
    • Hernandez-Barrantes S., Toth M., Bernardo M.M., Yurkova M., Gervasi D.C., Raz Y., Sang Q.A., and Fridman R. 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 2000 12080 12089
    • (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    Raz, Y.6    Sang, Q.A.7    Fridman, R.8
  • 70
    • 0038266866 scopus 로고    scopus 로고
    • Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase a (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP)
    • Worley J.R., Thompkins P.B., Lee M.H., Hutton M., Soloway P., Edwards D.R., Murphy G., and Knauper V. Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP) Biochem. J. 372 2003 799 809
    • (2003) Biochem. J. , vol.372 , pp. 799-809
    • Worley, J.R.1    Thompkins, P.B.2    Lee, M.H.3    Hutton, M.4    Soloway, P.5    Edwards, D.R.6    Murphy, G.7    Knauper, V.8
  • 72
    • 0035861560 scopus 로고    scopus 로고
    • Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
    • Morrison C.J., Butler G.S., Bigg H.F., Roberts C.R., Soloway P.D., and Overall C.M. Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway J. Biol. Chem. 276 2001 47402 47410
    • (2001) J. Biol. Chem. , vol.276 , pp. 47402-47410
    • Morrison, C.J.1    Butler, G.S.2    Bigg, H.F.3    Roberts, C.R.4    Soloway, P.D.5    Overall, C.M.6
  • 75
    • 0035958937 scopus 로고    scopus 로고
    • Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases
    • Miyamori H., Takino T., Kobayashi Y., Tokai H., Itoh Y., Seiki M., and Sato H. Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases J. Biol. Chem. 276 2001 28204 28211
    • (2001) J. Biol. Chem. , vol.276 , pp. 28204-28211
    • Miyamori, H.1    Takino, T.2    Kobayashi, Y.3    Tokai, H.4    Itoh, Y.5    Seiki, M.6    Sato, H.7
  • 77
    • 0142219888 scopus 로고    scopus 로고
    • Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6:matrix metalloproteinase/matrix metalloproteinase 25:at the asn(109)-Tyr bond
    • Nie J., and Pei D. Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6:matrix metalloproteinase/matrix metalloproteinase 25:at the asn(109)-Tyr bond Cancer Res. 63 2003 6758 6762
    • (2003) Cancer Res. , vol.63 , pp. 6758-6762
    • Nie, J.1    Pei, D.2
  • 78
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms 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 S.J., Stanton H., Hembry R.M., and Murphy G. Cellular mechanisms 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 1996 17124 17131
    • (1996) J. Biol. Chem. , vol.271 , 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
  • 79
    • 0037021469 scopus 로고    scopus 로고
    • Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13
    • Knauper V., Bailey L., Worley J.R., Soloway P., Patterson M.L., and Murphy G. Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13 FEBS Lett. 532 2002 127 130
    • (2002) FEBS Lett. , vol.532 , pp. 127-130
    • Knauper, V.1    Bailey, L.2    Worley, J.R.3    Soloway, P.4    Patterson, M.L.5    Murphy, G.6
  • 82
    • 1542289879 scopus 로고    scopus 로고
    • The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1
    • Velasco-Loyden G., Arribas J., and Lopez-Casillas F. The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1 J. Biol. Chem. 279 2004 7721 7733
    • (2004) J. Biol. Chem. , vol.279 , pp. 7721-7733
    • Velasco-Loyden, G.1    Arribas, J.2    Lopez-Casillas, F.3
  • 84
    • 0040439972 scopus 로고    scopus 로고
    • The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells
    • Manes S., Llorente M., Lacalle R.A., Gomez-Mouton C., Kremer L., Mira E., and Martinez A. The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells J. Biol. Chem. 274 1999 6935 6945
    • (1999) J. Biol. Chem. , vol.274 , pp. 6935-6945
    • Manes, S.1    Llorente, M.2    Lacalle, R.A.3    Gomez-Mouton, C.4    Kremer, L.5    Mira, E.6    Martinez, A.7
  • 85
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock J.M., Murdoch A.D., Iozzo R.V., and Underwood P.A. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases J. Biol. Chem. 271 1996 10079 10086
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 86
    • 0037183997 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165
    • Hashimoto G., Inoki I., Fujii Y., Aoki T., Ikeda E., and Okada Y. Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165 J. Biol. Chem. 277 2002 36288 36295
    • (2002) J. Biol. Chem. , vol.277 , pp. 36288-36295
    • Hashimoto, G.1    Inoki, I.2    Fujii, Y.3    Aoki, T.4    Ikeda, E.5    Okada, Y.6
  • 87
    • 0031467314 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site
    • Suzuki M., Raab G., Moses M.A., Fernandez C.A., and Klagsbrun M. Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site J. Biol. Chem. 272 1997 31730 31737
    • (1997) J. Biol. Chem. , vol.272 , pp. 31730-31737
    • Suzuki, M.1    Raab, G.2    Moses, M.A.3    Fernandez, C.A.4    Klagsbrun, M.5
  • 88
    • 0036468005 scopus 로고    scopus 로고
    • CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling
    • Yu W.H., Woessner J.F. Jr, McNeish J.D., and Stamenkovic I. CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling Genes Dev. 16 2002 307 323
    • (2002) Genes Dev. , vol.16 , pp. 307-323
    • Yu, W.H.1    Woessner Jr., J.F.2    McNeish, J.D.3    Stamenkovic, I.4
  • 89
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2:releases active soluble ectodomain of fibroblast growth factor receptor 1
    • Levi E., Fridman R., Miao H.Q., Ma Y.S., Yayon A., and Vlodavsky I. Matrix metalloproteinase 2:releases active soluble ectodomain of fibroblast growth factor receptor 1 Proc. Natl. Acad. Sci. USA 93 1996 7069 7074
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7069-7074
    • Levi, E.1    Fridman, R.2    Miao, H.Q.3    Ma, Y.S.4    Yayon, A.5    Vlodavsky, I.6
  • 90
    • 0033559210 scopus 로고    scopus 로고
    • Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells
    • Codony-Servat J., Albanell J., Lopez-Talavera J.C., Arribas J., and Baselga J. Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells Cancer Res. 59 1999 1196 1201
    • (1999) Cancer Res. , vol.59 , pp. 1196-1201
    • Codony-Servat, J.1    Albanell, J.2    Lopez-Talavera, J.C.3    Arribas, J.4    Baselga, J.5
  • 91
    • 0032493646 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin
    • Vecchi M., Rudolph-Owen L.A., Brown C.L., Dempsey P.J., and Carpenter G. Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin J. Biol. Chem. 273 1998 20589 20595
    • (1998) J. Biol. Chem. , vol.273 , pp. 20589-20595
    • Vecchi, M.1    Rudolph-Owen, L.A.2    Brown, C.L.3    Dempsey, P.J.4    Carpenter, G.5
  • 92
    • 0035074356 scopus 로고    scopus 로고
    • Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase
    • Nath D., Williamson N.J., Jarvis R., and Murphy G. Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase J. Cell Sci. 114 2001 1213 1220
    • (2001) J. Cell Sci. , vol.114 , pp. 1213-1220
    • Nath, D.1    Williamson, N.J.2    Jarvis, R.3    Murphy, G.4
  • 94
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban G.A., Gong J.H., Wong J.P., Wallace J.L., Clark-Lewis I., and Overall C.M. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo Blood 100 2002 1160 1167
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 95
    • 0036661037 scopus 로고    scopus 로고
    • Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: A new tool for degradomics
    • Overall C.M., McQuibban G.A., and Clark-Lewis I. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics Biol. Chem. 383 2002 1059 1066
    • (2002) Biol. Chem. , vol.383 , pp. 1059-1066
    • Overall, C.M.1    McQuibban, G.A.2    Clark-Lewis, I.3
  • 97
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam E.M., Morrison C.J., Wu Y.I., Stack M.S., and Overall C.M. Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates Proc. Natl. Acad. Sci. USA 101 2004 6917 6922
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6917-6922
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 98
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin A.M., Akimov S.S., Zaritskaya L.S., Ratnikov B.I., Deryugina E.I., and Strongin A.Y. Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion J. Biol. Chem. 276 2001 18415 18422
    • (2001) J. Biol. Chem. , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 99
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1:matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita M., Itoh Y., Chiba T., Mori H., Okada A., Kinoh H., and Seiki M. Membrane-type 1:matrix metalloproteinase cleaves CD44 and promotes cell migration J. Cell Biol. 153 2001 893 904
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 100
    • 0037155874 scopus 로고    scopus 로고
    • Processing of integrin alpha(v) subunit by membrane type 1:matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase
    • Deryugina E.I., Ratnikov B.I., Postnova T.I., Rozanov D.V., and Strongin A.Y. Processing of integrin alpha(v) subunit by membrane type 1:matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase J. Biol. Chem. 277 2002 9749 9756
    • (2002) J. Biol. Chem. , vol.277 , pp. 9749-9756
    • Deryugina, E.I.1    Ratnikov, B.I.2    Postnova, T.I.3    Rozanov, D.V.4    Strongin, A.Y.5
  • 101
    • 0037088631 scopus 로고    scopus 로고
    • The hemopexin-like C-terminal domain of membrane type 1:matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR
    • Rozanov D.V., Ghebrehiwet B., Postnova T.I., Eichinger A., Deryugina E.I., and Strongin A.Y. The hemopexin-like C-terminal domain of membrane type 1:matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR J. Biol. Chem. 277 2002 9318 9325
    • (2002) J. Biol. Chem. , vol.277 , pp. 9318-9325
    • Rozanov, D.V.1    Ghebrehiwet, B.2    Postnova, T.I.3    Eichinger, A.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 103
    • 1042301387 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells
    • Rozanov D.V., Hahn-Dantona E., Strickland D.K., and Strongin A.Y. The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells J. Biol. Chem. 279 2004 4260 4268
    • (2004) J. Biol. Chem. , vol.279 , pp. 4260-4268
    • Rozanov, D.V.1    Hahn-Dantona, E.2    Strickland, D.K.3    Strongin, A.Y.4
  • 105
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1:activity by dynamin-mediated endocytosis
    • Jiang A., Lehti K., Wang X., Weiss S.J., Keski-Oja J., and Pei D. Regulation of membrane-type matrix metalloproteinase 1:activity by dynamin-mediated endocytosis Proc. Natl. Acad. Sci. USA 98 2001 13693 13698
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13693-13698
    • Jiang, A.1    Lehti, K.2    Wang, X.3    Weiss, S.J.4    Keski-Oja, J.5    Pei, D.6
  • 106
    • 0142011033 scopus 로고    scopus 로고
    • Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface
    • Remacle A., Murphy G., and Roghi C. Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface J. Cell Sci. 116 2003 3905 3916
    • (2003) J. Cell Sci. , vol.116 , pp. 3905-3916
    • Remacle, A.1    Murphy, G.2    Roghi, C.3
  • 107
    • 0842304200 scopus 로고    scopus 로고
    • Membrane type 1:matrix metalloproteinase regulates collagen-dependent mitogen-activated protein/extracellular signal-related kinase activation and cell migration
    • Takino T., Miyamori H., Watanabe Y., Yoshioka K., Seiki M., and Sato H. Membrane type 1:matrix metalloproteinase regulates collagen-dependent mitogen-activated protein/extracellular signal-related kinase activation and cell migration Cancer Res. 64 2004 1044 1049
    • (2004) Cancer Res. , vol.64 , pp. 1044-1049
    • Takino, T.1    Miyamori, H.2    Watanabe, Y.3    Yoshioka, K.4    Seiki, M.5    Sato, H.6
  • 108
    • 1842790801 scopus 로고    scopus 로고
    • Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration
    • Cao J., Kozarekar P., Pavlaki M., Chiarelli C., Bahou W.F., and Zucker S. Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration J. Biol. Chem. 279 2004 14129 14139
    • (2004) J. Biol. Chem. , vol.279 , pp. 14129-14139
    • Cao, J.1    Kozarekar, P.2    Pavlaki, M.3    Chiarelli, C.4    Bahou, W.F.5    Zucker, S.6
  • 109
    • 0842347494 scopus 로고    scopus 로고
    • Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-Type 1:matrix metalloproteinase
    • Nakamura H., Suenaga N., Taniwaki K., Matsuki H., Yonezawa K., Fujii M., Okada Y., and Seiki M. Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-Type 1:matrix metalloproteinase Cancer Res. 64 2004 876 882
    • (2004) Cancer Res. , vol.64 , pp. 876-882
    • Nakamura, H.1    Suenaga, N.2    Taniwaki, K.3    Matsuki, H.4    Yonezawa, K.5    Fujii, M.6    Okada, Y.7    Seiki, M.8
  • 111
    • 0344443646 scopus 로고    scopus 로고
    • Matrix metalloproteinases 2:and 9:mediate epidermal growth factor receptor transactivation by gonadotropin-releasing hormone
    • Roelle S., Grosse R., Aigner A., Krell H.W., Czubayko F., and Gudermann T. Matrix metalloproteinases 2:and 9:mediate epidermal growth factor receptor transactivation by gonadotropin-releasing hormone J. Biol. Chem. 278 2003 47307 47318
    • (2003) J. Biol. Chem. , vol.278 , pp. 47307-47318
    • Roelle, S.1    Grosse, R.2    Aigner, A.3    Krell, H.W.4    Czubayko, F.5    Gudermann, T.6
  • 113
    • 0035896502 scopus 로고    scopus 로고
    • Activation of MAPKs by angiotensin II in vascular smooth muscle cells. Metalloprotease-dependent EGF receptor activation is required for activation of ERK and p38 MAPK but not for JNK
    • Eguchi S., Dempsey P.J., Frank G.D., Motley E.D., and Inagami T. Activation of MAPKs by angiotensin II in vascular smooth muscle cells. Metalloprotease-dependent EGF receptor activation is required for activation of ERK and p38 MAPK but not for JNK J. Biol. Chem. 276 2001 7957 7962
    • (2001) J. Biol. Chem. , vol.276 , pp. 7957-7962
    • Eguchi, S.1    Dempsey, P.J.2    Frank, G.D.3    Motley, E.D.4    Inagami, T.5
  • 114
    • 0142089835 scopus 로고    scopus 로고
    • Galardin (GM 6001), a broad-spectrum matrix metalloproteinase inhibitor, blocks bombesin- and LPA-induced EGF receptor transactivation and DNA synthesis in rat-1 cells
    • Santiskulvong C., and Rozengurt E. Galardin (GM 6001), a broad-spectrum matrix metalloproteinase inhibitor, blocks bombesin- and LPA-induced EGF receptor transactivation and DNA synthesis in rat-1 cells Exp. Cell Res. 290 2003 437 446
    • (2003) Exp. Cell Res. , vol.290 , pp. 437-446
    • Santiskulvong, C.1    Rozengurt, E.2
  • 115
    • 1842474897 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation
    • Langlois S., Gingras D., and Beliveau R. Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation Blood 103 2004 3020 3028
    • (2004) Blood , vol.103 , pp. 3020-3028
    • Langlois, S.1    Gingras, D.2    Beliveau, R.3
  • 116
    • 15244356639 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation
    • Langlois S., Gingras D., and Beliveau R. Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation Blood 2003
    • (2003) Blood
    • Langlois, S.1    Gingras, D.2    Beliveau, R.3
  • 117
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1:matrix metalloproteinase is important for its invasion-promoting activity
    • Uekita T., Itoh Y., Yana I., Ohno H., and Seiki M. Cytoplasmic tail-dependent internalization of membrane-type 1:matrix metalloproteinase is important for its invasion-promoting activity J. Cell Biol. 155 2001 1345 1356
    • (2001) J. Cell Biol. , vol.155 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 118
    • 15244356639 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation
    • Langlois S., Gingras D., and Beliveau R. Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation Blood 2003
    • (2003) Blood
    • Langlois, S.1    Gingras, D.2    Beliveau, R.3
  • 119
    • 0037063349 scopus 로고    scopus 로고
    • The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment- specific chaperone-like regulatory protein
    • Rozanov D.V., Ghebrehiwet B., Ratnikov B., Monosov E.Z., Deryugina E.I., and Strongin A.Y. The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment- specific chaperone-like regulatory protein FEBS Lett. 527 2002 51 57
    • (2002) FEBS Lett. , vol.527 , pp. 51-57
    • Rozanov, D.V.1    Ghebrehiwet, B.2    Ratnikov, B.3    Monosov, E.Z.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 120
    • 0032212994 scopus 로고    scopus 로고
    • Membrane-type metalloproteinases in tumor invasion
    • Polette M., and Birembaut P. Membrane-type metalloproteinases in tumor invasion Int. J. Biochem. Cell Biol. 30 1998 1195 1202
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 1195-1202
    • Polette, M.1    Birembaut, P.2
  • 121
    • 0030019731 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis
    • Sato H., and Seiki M. Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis J. Biochem. 119 1996 209 215 (Tokyo)
    • (1996) J. Biochem. , vol.119 , pp. 209-215
    • Sato, H.1    Seiki, M.2
  • 122
    • 0032953789 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase-1 expression and activation of gelatinase a as prognostic markers in advanced pediatric neuroblastoma
    • Sakakibara M., Koizumi S., Saikawa Y., Wada H., Ichihara T., Sato H., Horita S., Mugishima H., Kaneko Y., and Koike K. Membrane-type matrix metalloproteinase-1 expression and activation of gelatinase A as prognostic markers in advanced pediatric neuroblastoma Cancer 85 1999 231 239
    • (1999) Cancer , vol.85 , pp. 231-239
    • Sakakibara, M.1    Koizumi, S.2    Saikawa, Y.3    Wada, H.4    Ichihara, T.5    Sato, H.6    Horita, S.7    Mugishima, H.8    Kaneko, Y.9    Koike, K.10
  • 123
    • 0033047083 scopus 로고    scopus 로고
    • Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer
    • Michael M., Babic B., Khokha R., Tsao M., Ho J., Pintilie M., Leco K., Chamberlain D., and Shepherd F.A. Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer J. Clin. Oncol. 17 1999 1802 1808
    • (1999) J. Clin. Oncol. , vol.17 , pp. 1802-1808
    • Michael, M.1    Babic, B.2    Khokha, R.3    Tsao, M.4    Ho, J.5    Pintilie, M.6    Leco, K.7    Chamberlain, D.8    Shepherd, F.A.9
  • 124
    • 0035915805 scopus 로고    scopus 로고
    • Expression of tissue inhibitor of matrix metalloproteinase-2 correlates with activation of matrix metalloproteinase-2 and predicts poor prognosis in tongue squamous cell carcinoma
    • Yoshizaki T., Maruyama Y., Sato H., and Furukawa M. Expression of tissue inhibitor of matrix metalloproteinase-2 correlates with activation of matrix metalloproteinase-2 and predicts poor prognosis in tongue squamous cell carcinoma Int. J. Cancer 95 2001 44 50
    • (2001) Int. J. Cancer , vol.95 , pp. 44-50
    • Yoshizaki, T.1    Maruyama, Y.2    Sato, H.3    Furukawa, M.4
  • 125
    • 0031022581 scopus 로고    scopus 로고
    • Increased expression of membrane type 1-matrix metalloproteinase in head and neck carcinoma
    • Yoshizaki T., Sato H., Maruyama Y., Murono S., Furukawa M., Park C.S., and Seiki M. Increased expression of membrane type 1-matrix metalloproteinase in head and neck carcinoma Cancer 79 1997 139 144
    • (1997) Cancer , vol.79 , pp. 139-144
    • Yoshizaki, T.1    Sato, H.2    Maruyama, Y.3    Murono, S.4    Furukawa, M.5    Park, C.S.6    Seiki, M.7
  • 126
    • 0032055870 scopus 로고    scopus 로고
    • Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer
    • Kanayama H., Yokota K., Kurokawa Y., Murakami Y., Nishitani M., and Kagawa S. Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer Cancer 82 1998 1359 1366
    • (1998) Cancer , vol.82 , pp. 1359-1366
    • Kanayama, H.1    Yokota, K.2    Kurokawa, Y.3    Murakami, Y.4    Nishitani, M.5    Kagawa, S.6
  • 128
    • 0346058325 scopus 로고    scopus 로고
    • Low collagenase-1 (MMP-1) and MT1-MMP expression levels are favourable survival markers in advanced colorectal carcinoma
    • Bendardaf R., Lamlum H., Vihinen P., Ristamaki R., Laine J., and Pyrhonen S. Low collagenase-1 (MMP-1) and MT1-MMP expression levels are favourable survival markers in advanced colorectal carcinoma Oncology 65 2003 337 346
    • (2003) Oncology , vol.65 , pp. 337-346
    • Bendardaf, R.1    Lamlum, H.2    Vihinen, P.3    Ristamaki, R.4    Laine, J.5    Pyrhonen, S.6
  • 131
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • Okada A., Bellocq J.P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., and Basset P. Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas Proc. Natl. Acad. Sci. USA 92 1995 2730 2734
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.P.2    Rouyer, N.3    Chenard, M.P.4    Rio, M.C.5    Chambon, P.6    Basset, P.7
  • 132
    • 0030922614 scopus 로고    scopus 로고
    • Implication of collagen type I-induced membrane-type 1-matrix metalloproteinase expression and matrix metalloproteinase-2 activation in the metastatic progression of breast carcinoma
    • Gilles C., Polette M., Seiki M., Birembaut P., and Thompson E.W. Implication of collagen type I-induced membrane-type 1-matrix metalloproteinase expression and matrix metalloproteinase-2 activation in the metastatic progression of breast carcinoma Lab. Invest. 76 1997 651 660
    • (1997) Lab. Invest. , vol.76 , pp. 651-660
    • Gilles, C.1    Polette, M.2    Seiki, M.3    Birembaut, P.4    Thompson, E.W.5
  • 134
    • 0032959030 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-type 1, 2, and 3:matrix metalloproteinases in human astrocytic tumors
    • Nakada M., Nakamura H., Ikeda E., Fujimoto N., Yamashita J., Sato H., Seiki M., and Okada Y. Expression and tissue localization of membrane-type 1, 2, and 3:matrix metalloproteinases in human astrocytic tumors Am. J. Pathol. 154 1999 417 428
    • (1999) Am. J. Pathol. , vol.154 , pp. 417-428
    • Nakada, M.1    Nakamura, H.2    Ikeda, E.3    Fujimoto, N.4    Yamashita, J.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 135
    • 0037359601 scopus 로고    scopus 로고
    • Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells
    • Nuttall R.K., Pennington C.J., Taplin J., Wheal A., Yong V.W., Forsyth P.A., and Edwards D.R. Elevated membrane-type matrix metalloproteinases in gliomas revealed by profiling proteases and inhibitors in human cancer cells Mol. Cancer Res. 1 2003 333 345
    • (2003) Mol. Cancer Res. , vol.1 , pp. 333-345
    • Nuttall, R.K.1    Pennington, C.J.2    Taplin, J.3    Wheal, A.4    Yong, V.W.5    Forsyth, P.A.6    Edwards, D.R.7
  • 136
    • 0032835586 scopus 로고    scopus 로고
    • Expression of messenger RNAs for membrane-type 1, 2, and 3:matrix metalloproteinases in human renal cell carcinomas
    • Kitagawa Y., Kunimi K., Uchibayashi T., Sato H., and Namiki M. Expression of messenger RNAs for membrane-type 1, 2, and 3:matrix metalloproteinases in human renal cell carcinomas J. Urol. 162 1999 905 909
    • (1999) J. Urol. , vol.162 , pp. 905-909
    • Kitagawa, Y.1    Kunimi, K.2    Uchibayashi, T.3    Sato, H.4    Namiki, M.5
  • 137
    • 0030951910 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-types 1, 2, and 3:matrix metalloproteinases in human invasive breast carcinomas
    • Ueno H., Nakamura H., Inoue M., Imai K., Noguchi M., Sato H., Seiki M., and Okada Y. Expression and tissue localization of membrane-types 1, 2, and 3:matrix metalloproteinases in human invasive breast carcinomas Cancer Res. 57 1997 2055 2060
    • (1997) Cancer Res. , vol.57 , pp. 2055-2060
    • Ueno, H.1    Nakamura, H.2    Inoue, M.3    Imai, K.4    Noguchi, M.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 138
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT- MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino T., Sato H., Shinagawa A., and Seiki M. Identification of the second membrane-type matrix metalloproteinase (MT- MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family J. Biol. Chem. 270 1995 23013 23020
    • (1995) J. Biol. Chem. , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 140
    • 0035110730 scopus 로고    scopus 로고
    • Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice
    • Ha H.Y., Moon H.B., Nam M.S., Lee J.W., Ryoo Z.Y., Lee T.H., Lee K.K., So B.J., Sato H., Seiki M., and Yu D.Y. Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice Cancer Res. 61 2001 984 990
    • (2001) Cancer Res. , vol.61 , pp. 984-990
    • Ha, H.Y.1    Moon, H.B.2    Nam, M.S.3    Lee, J.W.4    Ryoo, Z.Y.5    Lee, T.H.6    Lee, K.K.7    So, B.J.8    Sato, H.9    Seiki, M.10    Yu, D.Y.11
  • 144
    • 0037081306 scopus 로고    scopus 로고
    • Up-regulation of vascular endothelial growth factor by membrane-type 1:matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis
    • Deryugina E.I., Soroceanu L., and Strongin A.Y. Up-regulation of vascular endothelial growth factor by membrane-type 1:matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis Cancer Res. 62 2002 580 588
    • (2002) Cancer Res. , vol.62 , pp. 580-588
    • Deryugina, E.I.1    Soroceanu, L.2    Strongin, A.Y.3
  • 145
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary K.B., Allen E.D., Brooks P.C., Datta N.S., Long M.W., and Weiss S.J. Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix Cell 114 2003 33 45
    • (2003) Cell , vol.114 , pp. 33-45
    • Hotary, K.B.1    Allen, E.D.2    Brooks, P.C.3    Datta, N.S.4    Long, M.W.5    Weiss, S.J.6
  • 147
    • 9144232875 scopus 로고    scopus 로고
    • Pro-matrix metalloproteinase-2 transfection increases orthotopic primary growth and experimental metastasis of MDA-MB-231 human breast cancer cells in nude mice
    • Tester A.M., Waltham M., Oh S.J., Bae S.N., Bills M.M., Walker E.C., Kern F.G., Stetler-Stevenson W.G., Lippman M.E., and Thompson E.W. Pro-matrix metalloproteinase-2 transfection increases orthotopic primary growth and experimental metastasis of MDA-MB-231 human breast cancer cells in nude mice Cancer Res. 64 2004 652 658
    • (2004) Cancer Res. , vol.64 , pp. 652-658
    • Tester, A.M.1    Waltham, M.2    Oh, S.J.3    Bae, S.N.4    Bills, M.M.5    Walker, E.C.6    Kern, F.G.7    Stetler-Stevenson, W.G.8    Lippman, M.E.9    Thompson, E.W.10
  • 148
    • 0042090268 scopus 로고    scopus 로고
    • Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases
    • Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., and Sato H. Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases Oncogene 22 2003 4617 4626
    • (2003) Oncogene , vol.22 , pp. 4617-4626
    • Takino, T.1    Koshikawa, N.2    Miyamori, H.3    Tanaka, M.4    Sasaki, T.5    Okada, Y.6    Seiki, M.7    Sato, H.8
  • 150
    • 0029753004 scopus 로고    scopus 로고
    • Expression of membrane-type matrix metalloproteinase 1 (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis assay
    • Tsunezuka Y., Kinoh H., Takino T., Watanabe Y., Okada Y., Shinagawa A., Sato H., and Seiki M. Expression of membrane-type matrix metalloproteinase 1 (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis assay Cancer Res. 56 1996 5678 5683
    • (1996) Cancer Res. , vol.56 , pp. 5678-5683
    • Tsunezuka, Y.1    Kinoh, H.2    Takino, T.3    Watanabe, Y.4    Okada, Y.5    Shinagawa, A.6    Sato, H.7    Seiki, M.8
  • 151
    • 0035109581 scopus 로고    scopus 로고
    • Enhanced production and activation of progelatinase a mediated by membrane-type 1:matrix metalloproteinase in human oral squamous cell carcinomas: Implications for lymph node metastasis
    • Shimada T., Nakamura H., Yamashita K., Kawata R., Murakami Y., Fujimoto N., Sato H., Seiki M., and Okada Y. Enhanced production and activation of progelatinase A mediated by membrane-type 1:matrix metalloproteinase in human oral squamous cell carcinomas: implications for lymph node metastasis Clin. Exp. Metastasis 18 2000 179 188
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 179-188
    • Shimada, T.1    Nakamura, H.2    Yamashita, K.3    Kawata, R.4    Murakami, Y.5    Fujimoto, N.6    Sato, H.7    Seiki, M.8    Okada, Y.9
  • 154
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N., Giannelli G., Cirulli V., Miyazaki K., and Quaranta V. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5 J. Cell Biol. 148 2000 615 624
    • (2000) J. Cell Biol. , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 155
    • 0346363608 scopus 로고    scopus 로고
    • Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: Importance of MT1-MMP as a therapeutic target for invasive tumors
    • Ueda J., Kajita M., Suenaga N., Fujii K., and Seiki M. Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: importance of MT1-MMP as a therapeutic target for invasive tumors Oncogene 22 2003 8716 8722
    • (2003) Oncogene , vol.22 , pp. 8716-8722
    • Ueda, J.1    Kajita, M.2    Suenaga, N.3    Fujii, K.4    Seiki, M.5
  • 156
    • 0036712828 scopus 로고    scopus 로고
    • Endothelial tubulogenesis within fibrin gels specifically requires the activity of membrane-type-matrix metalloproteinases (MT-MMPs)
    • Lafleur M.A., Handsley M.M., Knauper V., Murphy G., and Edwards D.R. Endothelial tubulogenesis within fibrin gels specifically requires the activity of membrane-type-matrix metalloproteinases (MT-MMPs) J. Cell Sci. 115 2002 3427 3438
    • (2002) J. Cell Sci. , vol.115 , pp. 3427-3438
    • Lafleur, M.A.1    Handsley, M.M.2    Knauper, V.3    Murphy, G.4    Edwards, D.R.5
  • 157
    • 0032578775 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase is involved in the formation of hepatocyte growth factor/scatter factor-induced branching tubules in madin-darby canine kidney epithelial cells
    • Kadono Y., Shibahara K., Namiki M., Watanabe Y., Seiki M., and Sato H. Membrane type 1-matrix metalloproteinase is involved in the formation of hepatocyte growth factor/scatter factor-induced branching tubules in madin-darby canine kidney epithelial cells Biochem. Biophys. Res. Commun. 251 1998 681 687
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 681-687
    • Kadono, Y.1    Shibahara, K.2    Namiki, M.3    Watanabe, Y.4    Seiki, M.5    Sato, H.6
  • 158
    • 0032488895 scopus 로고    scopus 로고
    • Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells
    • Haas T.L., Davis S.J., and Madri J.A. Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells J. Biol. Chem. 273 1998 3604 3610
    • (1998) J. Biol. Chem. , vol.273 , pp. 3604-3610
    • Haas, T.L.1    Davis, S.J.2    Madri, J.A.3
  • 160
    • 0035417897 scopus 로고    scopus 로고
    • Cooperative interactions of laminin 5:gamma2 chain, matrix metalloproteinase-2, and membrane type-1-matrix/metalloproteinase are required for mimicry of embryonic vasculogenesis by aggressive melanoma
    • Seftor R.E., Seftor E.A., Koshikawa N., Meltzer P.S., Gardner L.M., Bilban M., Stetler-Stevenson W.G., Quaranta V., and Hendrix M.J. Cooperative interactions of laminin 5:gamma2 chain, matrix metalloproteinase-2, and membrane type-1-matrix/metalloproteinase are required for mimicry of embryonic vasculogenesis by aggressive melanoma Cancer Res. 61 2001 6322 6327
    • (2001) Cancer Res. , vol.61 , pp. 6322-6327
    • Seftor, R.E.1    Seftor, E.A.2    Koshikawa, N.3    Meltzer, P.S.4    Gardner, L.M.5    Bilban, M.6    Stetler-Stevenson, W.G.7    Quaranta, V.8    Hendrix, M.J.9
  • 161
    • 3042526364 scopus 로고    scopus 로고
    • Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor
    • Maquoi E., Sounni N.E., Devy L., Olivier F., Frankenne F., Krell H.W., Grams F., Foidart J.M., and Noel A. Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor Clin. Cancer Res. 10 2004 4038 4047
    • (2004) Clin. Cancer Res. , vol.10 , pp. 4038-4047
    • Maquoi, E.1    Sounni, N.E.2    Devy, L.3    Olivier, F.4    Frankenne, F.5    Krell, H.W.6    Grams, F.7    Foidart, J.M.8    Noel, A.9
  • 162
    • 18744397808 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (MIF) expression in human glioblastomas correlates with vascular endothelial growth factor (VEGF) expression
    • Munaut C., Boniver J., Foidart J.M., and Deprez M. Macrophage migration inhibitory factor (MIF) expression in human glioblastomas correlates with vascular endothelial growth factor (VEGF) expression Neuropathol. Appl. Neurobiol. 28 2002 452 460
    • (2002) Neuropathol. Appl. Neurobiol. , vol.28 , pp. 452-460
    • Munaut, C.1    Boniver, J.2    Foidart, J.M.3    Deprez, M.4
  • 163
    • 0037007146 scopus 로고    scopus 로고
    • In vitro cartilage formation by human adult stem cells from bone marrow stroma defines the sequence of cellular and molecular events during chondrogenesis
    • Sekiya I., Vuoristo J.T., Larson B.L., and Prockop D.J. In vitro cartilage formation by human adult stem cells from bone marrow stroma defines the sequence of cellular and molecular events during chondrogenesis Proc. Natl. Acad. Sci. USA 99 2002 4397 4402
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4397-4402
    • Sekiya, I.1    Vuoristo, J.T.2    Larson, B.L.3    Prockop, D.J.4
  • 165
    • 0141482154 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: Implications for ascites formation
    • Belotti D., Paganoni P., Manenti L., Garofalo A., Marchini S., Taraboletti G., and Giavazzi R. Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation Cancer Res. 63 2003 5224 5229
    • (2003) Cancer Res. , vol.63 , pp. 5224-5229
    • Belotti, D.1    Paganoni, P.2    Manenti, L.3    Garofalo, A.4    Marchini, S.5    Taraboletti, G.6    Giavazzi, R.7
  • 166
    • 0036790181 scopus 로고    scopus 로고
    • Increase in gelatinase-specificity of matrix metalloproteinase inhibitors correlates with antimetastatic efficacy in a T-cell lymphoma model
    • Arlt M., Kopitz C., Pennington C., Watson K.L., Krell H.W., Bode W., Gansbacher B., Khokha R., Edwards D.R., and Kruger A. Increase in gelatinase-specificity of matrix metalloproteinase inhibitors correlates with antimetastatic efficacy in a T-cell lymphoma model Cancer Res. 62 2002 5543 5550
    • (2002) Cancer Res. , vol.62 , pp. 5543-5550
    • Arlt, M.1    Kopitz, C.2    Pennington, C.3    Watson, K.L.4    Krell, H.W.5    Bode, W.6    Gansbacher, B.7    Khokha, R.8    Edwards, D.R.9    Kruger, A.10
  • 169
    • 0032484529 scopus 로고    scopus 로고
    • Mammary carcinoma cells over-expressing tissue inhibitor of metalloproteinases-1 show enhanced vascular endothelial growth factor expression
    • Yoshiji H., Harris S.R., Raso E., Gomez D.E., Lindsay C.K., Shibuya M., Sinha C.C., and Thorgeirsson U.P. Mammary carcinoma cells over-expressing tissue inhibitor of metalloproteinases-1 show enhanced vascular endothelial growth factor expression Int. J. Cancer 75 1998 81 87
    • (1998) Int. J. Cancer , vol.75 , pp. 81-87
    • Yoshiji, H.1    Harris, S.R.2    Raso, E.3    Gomez, D.E.4    Lindsay, C.K.5    Shibuya, M.6    Sinha, C.C.7    Thorgeirsson, U.P.8
  • 170
    • 0037345653 scopus 로고    scopus 로고
    • Retroviral vector-producer cell-mediated in vivo gene transfer of TIMP-3 restricts angiogenesis and neuroblastoma growth in mice
    • Spurbeck W.W., Ng C.Y., Vanin E.F., and Davidoff A.M. Retroviral vector-producer cell-mediated in vivo gene transfer of TIMP-3 restricts angiogenesis and neuroblastoma growth in mice Cancer Gene Ther. 10 2003 161 167
    • (2003) Cancer Gene Ther. , vol.10 , pp. 161-167
    • Spurbeck, W.W.1    Ng, C.Y.2    Vanin, E.F.3    Davidoff, A.M.4
  • 171
    • 0036839094 scopus 로고    scopus 로고
    • Enforced expression of tissue inhibitor of matrix metalloproteinase-3 affects functional capillary morphogenesis and inhibits tumor growth in a murine tumor model
    • Spurbeck W.W., Ng C.Y., Strom T.S., Vanin E.F., and Davidoff A.M. Enforced expression of tissue inhibitor of matrix metalloproteinase-3 affects functional capillary morphogenesis and inhibits tumor growth in a murine tumor model Blood 100 2002 3361 3368
    • (2002) Blood , vol.100 , pp. 3361-3368
    • Spurbeck, W.W.1    Ng, C.Y.2    Strom, T.S.3    Vanin, E.F.4    Davidoff, A.M.5
  • 172
    • 1642459321 scopus 로고    scopus 로고
    • The effect of human tissue factor pathway inhibitor-2 on the growth and metastasis of fibrosarcoma tumors in athymic mice
    • Chand H.S., Du X., Ma D., Inzunza H.D., Kamei S., Foster D., Brodie S., and Kisiel W. The effect of human tissue factor pathway inhibitor-2 on the growth and metastasis of fibrosarcoma tumors in athymic mice Blood 103 2004 1069 1077
    • (2004) Blood , vol.103 , pp. 1069-1077
    • Chand, H.S.1    Du, X.2    Ma, D.3    Inzunza, H.D.4    Kamei, S.5    Foster, D.6    Brodie, S.7    Kisiel, W.8
  • 173
    • 0037393850 scopus 로고    scopus 로고
    • A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): Inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor- 2
    • Qi J.H., Ebrahem Q., Moore N., Murphy G., Claesson-Welsh L., Bond M., Baker A., and Anand-Apte B. A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor- 2 Nat. Med. 9 2003 407 415
    • (2003) Nat. Med. , vol.9 , pp. 407-415
    • Qi, J.H.1    Ebrahem, Q.2    Moore, N.3    Murphy, G.4    Claesson-Welsh, L.5    Bond, M.6    Baker, A.7    Anand-Apte, B.8
  • 175
    • 0036830980 scopus 로고    scopus 로고
    • The membrane-anchored metalloproteinase inhibitor RECK
    • Takahashi C., Junseo O., and Noda M. The membrane-anchored metalloproteinase inhibitor RECK Tanpakushitsu Kakusan Koso 47 2002 1889 1895
    • (2002) Tanpakushitsu Kakusan Koso , vol.47 , pp. 1889-1895
    • Takahashi, C.1    Junseo, O.2    Noda, M.3
  • 176
    • 0035192918 scopus 로고    scopus 로고
    • RECK gene expression in hepatocellular carcinoma: Correlation with invasion-related clinicopathological factors and its clinical significance. Reverse-inducing--cysteine-rich protein with Kazal motifs
    • Furumoto K., Arii S., Mori A., Furuyama H., Gorrin Rivas M.J., Nakao T., Isobe N., Murata T., Takahashi C., Noda M., and Imamura M. RECK gene expression in hepatocellular carcinoma: correlation with invasion-related clinicopathological factors and its clinical significance. Reverse-inducing-- cysteine-rich protein with Kazal motifs Hepatology 33 2001 189 195
    • (2001) Hepatology , vol.33 , pp. 189-195
    • Furumoto, K.1    Arii, S.2    Mori, A.3    Furuyama, H.4    Gorrin Rivas, M.J.5    Nakao, T.6    Isobe, N.7    Murata, T.8    Takahashi, C.9    Noda, M.10    Imamura, M.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.