메뉴 건너뛰기




Volumn 19, Issue 8, 2008, Pages 3221-3233

Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COLLAGENASE; HEMOPEXIN; MATRIX METALLOPROTEINASE 14;

EID: 54049102110     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-01-0016     Document Type: Article
Times cited : (102)

References (66)
  • 1
    • 34547770377 scopus 로고    scopus 로고
    • Cleavage of growth differentiation factor 15 (GDF15) by membrane type 1-matrix metalloproteinase abrogates GDF15-mediated suppression of tumor cell growth
    • Abd El-Aziz, S. H., Endo, Y., Miyamaori, H., Takino, T., and Sato, H. (2007). Cleavage of growth differentiation factor 15 (GDF15) by membrane type 1-matrix metalloproteinase abrogates GDF15-mediated suppression of tumor cell growth. Cancer Sci. 98, 1330-1335.
    • (2007) Cancer Sci , vol.98 , pp. 1330-1335
    • Abd El-Aziz, S.H.1    Endo, Y.2    Miyamaori, H.3    Takino, T.4    Sato, H.5
  • 2
    • 23444460823 scopus 로고    scopus 로고
    • Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration
    • Anilkumar, N., Uekita, T., Couchman, J. R., Nagase, H., Seiki, M., and Itoh, Y. (2005). Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. FASEB J. 19, 1326-1328.
    • (2005) FASEB J , vol.19 , pp. 1326-1328
    • Anilkumar, N.1    Uekita, T.2    Couchman, J.R.3    Nagase, H.4    Seiki, M.5    Itoh, Y.6
  • 3
    • 33747176841 scopus 로고    scopus 로고
    • MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells
    • Atkinson, S. J., Roghi, C., and Murphy, G. (2006). MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells. Biochem. J. 398, 15-22.
    • (2006) Biochem. J , vol.398 , pp. 15-22
    • Atkinson, S.J.1    Roghi, C.2    Murphy, G.3
  • 4
    • 34250307200 scopus 로고    scopus 로고
    • MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D
    • Basile, J. R., Holmbeck, K., Bugge, T. H., and Gutkind, J. S. (2007). MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D. J. Biol. Chem. 282, 6899-6905.
    • (2007) J. Biol. Chem , vol.282 , pp. 6899-6905
    • Basile, J.R.1    Holmbeck, K.2    Bugge, T.H.3    Gutkind, J.S.4
  • 5
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • Brinckerhoff, C. E., and Matrisian, L. M. (2002). Matrix metalloproteinases: a tail of a frog that became a prince. Nat. Rev. Mol. Cell Biol. 3, 207-214.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 6
    • 44449173164 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase induces epithelial-to-mesenchymal transition in prostate cancer
    • Cao, J., Chiarelli, C., Richman, O., Zarrabi, K., Kozarekar, P., and Zucker, S. (2008). Membrane type 1 matrix metalloproteinase induces epithelial-to-mesenchymal transition in prostate cancer. J. Biol. Chem. 283, 6232-6240.
    • (2008) J. Biol. Chem , vol.283 , pp. 6232-6240
    • Cao, J.1    Chiarelli, C.2    Richman, O.3    Zarrabi, K.4    Kozarekar, P.5    Zucker, S.6
  • 7
    • 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. (2004). Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration. J. Biol. Chem. 279, 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
  • 8
    • 33646139156 scopus 로고    scopus 로고
    • A pericellular collagenase directs the 3-dimensional development of white adipose tissue
    • Chun, T. H., Hotary, K. B., Sabeh, F., Saltiel, A. R., Allen, E. D., and Weiss, S. J. (2006). A pericellular collagenase directs the 3-dimensional development of white adipose tissue. Cell 125, 577-591.
    • (2006) Cell , vol.125 , pp. 577-591
    • Chun, T.H.1    Hotary, K.B.2    Sabeh, F.3    Saltiel, A.R.4    Allen, E.D.5    Weiss, S.J.6
  • 10
    • 38049174649 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism
    • D'Alessio, S. et al. (2008). Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism. J. Biol. Chem. 283, 87-99.
    • (2008) J. Biol. Chem , vol.283 , pp. 87-99
    • D'Alessio, S.1
  • 11
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • d'Ortho, M. P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., Smith, B., Timpl, R., Zardi, L., and Murphy, G. (1997). Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250, 751-757.
    • (1997) Eur. J. Biochem , vol.250 , pp. 751-757
    • d'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6    Smith, B.7    Timpl, R.8    Zardi, L.9    Murphy, G.10
  • 12
    • 0035834666 scopus 로고    scopus 로고
    • Characterization of the role of the "MT-loop": An eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases
    • English, W. R., Holtz, B., Vogt, G., Knauper, V., and Murphy, G. (2001). Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases. J. Biol. Chem. 276, 42018-42026.
    • (2001) J. Biol. Chem , vol.276 , pp. 42018-42026
    • English, W.R.1    Holtz, B.2    Vogt, G.3    Knauper, V.4    Murphy, G.5
  • 13
    • 0033568213 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal in the beta2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration
    • Fabbri, M., Fumagalli, L., Bossi, G., Bianchi, E., Bender, J. R., and Pardi, R. (1999). A tyrosine-based sorting signal in the beta2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration. EMBO J. 18, 4915-4925.
    • (1999) EMBO J , vol.18 , pp. 4915-4925
    • Fabbri, M.1    Fumagalli, L.2    Bossi, G.3    Bianchi, E.4    Bender, J.R.5    Pardi, R.6
  • 14
    • 24344442010 scopus 로고    scopus 로고
    • MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells
    • Filippov, S. et al. (2005). MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells. J. Exp. Med. 202, 663-671.
    • (2005) J. Exp. Med , vol.202 , pp. 663-671
    • Filippov, S.1
  • 15
    • 34547115457 scopus 로고    scopus 로고
    • Induction of Smad1 by MT1-MMP contributes to tumor growth
    • Freudenberg, J. A., and Chen, W. T. (2007). Induction of Smad1 by MT1-MMP contributes to tumor growth. Int. J. Cancer 121, 966-977.
    • (2007) Int. J. Cancer , vol.121 , pp. 966-977
    • Freudenberg, J.A.1    Chen, W.T.2
  • 16
    • 0037189584 scopus 로고    scopus 로고
    • Modulation of the catalytic activity of neutrophil collagenase MMP-8 on bovine collagen I. Role of the activation cleavage and of the hemopexin-like domain
    • Gioia, M., Fasciglione, G. F., Marini, S., D'Alessio, S., De Sanctis, G., Diekmann, O., Pieper, M., Politi, V., Tschesche, H., and Coletta, M. (2002). Modulation of the catalytic activity of neutrophil collagenase MMP-8 on bovine collagen I. Role of the activation cleavage and of the hemopexin-like domain. J. Biol. Chem. 277, 23123-23130.
    • (2002) J. Biol. Chem , vol.277 , pp. 23123-23130
    • Gioia, M.1    Fasciglione, G.F.2    Marini, S.3    D'Alessio, S.4    De Sanctis, G.5    Diekmann, O.6    Pieper, M.7    Politi, V.8    Tschesche, H.9    Coletta, M.10
  • 17
    • 34147150065 scopus 로고    scopus 로고
    • Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two alpha-chains
    • Gioia, M., Monaco, S., Fasciglione, G. F., Coletti, A., Modesti, A., Marini, S., and Coletta, M. (2007). Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two alpha-chains. J. Mol. Biol. 368, 1101-1113.
    • (2007) J. Mol. Biol , vol.368 , pp. 1101-1113
    • Gioia, M.1    Monaco, S.2    Fasciglione, G.F.3    Coletti, A.4    Modesti, A.5    Marini, S.6    Coletta, M.7
  • 18
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fi-brinolysins
    • Hiraoka, N., Allen, E., Apel, I. J., Gyetko, M. R., and Weiss, S. J. (1998). Matrix metalloproteinases regulate neovascularization by acting as pericellular fi-brinolysins. Cell 95, 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
  • 19
    • 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. (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, S.J.5
  • 20
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • Hotary, K., Li, X. Y., Allen, E., Stevens, S. L., and Weiss, S. J. (2006). A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 20, 2673-2686.
    • (2006) Genes Dev , vol.20 , pp. 2673-2686
    • Hotary, K.1    Li, X.Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 21
    • 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. (2003). Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 114, 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
  • 22
  • 23
    • 1242314741 scopus 로고    scopus 로고
    • Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities
    • Hurst, D. R., Schwartz, M. A., Ghaffari, M. A., Jin, Y., Tschesche, H., Fields, G. B., and Sang, Q. X. (2004). Catalytic- and ecto-domains of membrane type 1-matrix metalloproteinase have similar inhibition profiles but distinct endopeptidase activities. Biochem. J. 377, 775-779.
    • (2004) Biochem. J , vol.377 , pp. 775-779
    • Hurst, D.R.1    Schwartz, M.A.2    Ghaffari, M.A.3    Jin, Y.4    Tschesche, H.5    Fields, G.B.6    Sang, Q.X.7
  • 24
    • 33845396458 scopus 로고    scopus 로고
    • Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP
    • Itoh, Y., Ito, N., Nagase, H., Evans, R. D., Bird, S. A., and Seiki, M. (2006). Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP. Mol. Biol. Cell 17, 5390-5399.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5390-5399
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Evans, R.D.4    Bird, S.A.5    Seiki, M.6
  • 25
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: A potent modifier of pericellular microenvironment
    • Itoh, Y., and Seiki, M. (2006). MT1-MMP: a potent modifier of pericellular microenvironment. J. Cell. Physiol. 206, 1-8.
    • (2006) J. Cell. Physiol , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 26
    • 0141866772 scopus 로고    scopus 로고
    • Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis
    • Jiang, A., and Pei, D. (2003). Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis. J. Biol. Chem. 278, 38765-38771.
    • (2003) J. Biol. Chem , vol.278 , pp. 38765-38771
    • Jiang, A.1    Pei, D.2
  • 27
    • 12944288132 scopus 로고    scopus 로고
    • siRNA mediated inhibition of MMP-1 reduces invasive potential of a human chondrosarcoma cell line
    • Jiang, X., Dutton, C. M., Qi, W. N., Block, J. A., Garamszegi, N., and Scully, S. P. (2005). siRNA mediated inhibition of MMP-1 reduces invasive potential of a human chondrosarcoma cell line. J. Cell. Physiol. 202, 723-730.
    • (2005) J. Cell. Physiol , vol.202 , pp. 723-730
    • Jiang, X.1    Dutton, C.M.2    Qi, W.N.3    Block, J.A.4    Garamszegi, N.5    Scully, S.P.6
  • 28
    • 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. (1998). 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, 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
  • 29
    • 0034284862 scopus 로고    scopus 로고
    • Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP
    • Kojima, S., Itoh, Y., Matsumoto, S., Masuho, Y., and Seiki, M. (2000). Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP. FEBS Lett. 480, 142-146.
    • (2000) FEBS Lett , vol.480 , pp. 142-146
    • Kojima, S.1    Itoh, Y.2    Matsumoto, S.3    Masuho, Y.4    Seiki, M.5
  • 30
    • 12844275940 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain
    • Koshikawa, N., Minegishi, T., Sharabi, A., Quaranta, V., and Seiki, M. (2005). Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain. J. Biol. Chem. 280, 88-93.
    • (2005) J. Biol. Chem , vol.280 , pp. 88-93
    • Koshikawa, N.1    Minegishi, T.2    Sharabi, A.3    Quaranta, V.4    Seiki, M.5
  • 31
    • 0037189494 scopus 로고    scopus 로고
    • A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases
    • Kridel, S. J., Sawai, H., Ratnikov, B. I., Chen, E. I., Li, W., Godzik, A., Strongin, A. Y., and Smith, J. W. (2002). A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases. J. Biol. Chem. 277, 23788-23793.
    • (2002) J. Biol. Chem , vol.277 , pp. 23788-23793
    • Kridel, S.J.1    Sawai, H.2    Ratnikov, B.I.3    Chen, E.I.4    Li, W.5    Godzik, A.6    Strongin, A.Y.7    Smith, J.W.8
  • 32
    • 10644229956 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase
    • Labrecque, L., Nyalendo, C., Langlois, S., Durocher, Y., Roghi, C., Murphy, G., Gingras, D., and Beliveau, R. (2004). Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase. J. Biol. Chem. 279, 52132-52140.
    • (2004) J. Biol. Chem , vol.279 , pp. 52132-52140
    • Labrecque, L.1    Nyalendo, C.2    Langlois, S.3    Durocher, Y.4    Roghi, C.5    Murphy, G.6    Gingras, D.7    Beliveau, R.8
  • 33
    • 33646571255 scopus 로고    scopus 로고
    • Type I collagen abrogates the clathrin-mediated internalization of membrane type 1 matrix metalloproteinase (MT1-MMP) via the MT1-MMP hemopexin domain
    • Lafleur, M. A., Mercuri, F. A., Ruangpanit, N., Seiki, M., Sato, H., and Thompson, E. W. (2006). Type I collagen abrogates the clathrin-mediated internalization of membrane type 1 matrix metalloproteinase (MT1-MMP) via the MT1-MMP hemopexin domain. J. Biol. Chem. 281, 6826-6840.
    • (2006) J. Biol. Chem , vol.281 , pp. 6826-6840
    • Lafleur, M.A.1    Mercuri, F.A.2    Ruangpanit, N.3    Seiki, M.4    Sato, H.5    Thompson, E.W.6
  • 34
    • 33750495804 scopus 로고    scopus 로고
    • A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis
    • Lee, H., Overall, C. M., McCulloch, C. A., and Sodek, J. (2006). A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis. Mol. Biol. Cell 17, 4812-4826.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4812-4826
    • Lee, H.1    Overall, C.M.2    McCulloch, C.A.3    Sodek, J.4
  • 35
    • 0037040914 scopus 로고    scopus 로고
    • Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase
    • Lehti, K., Lohi, J., Juntunen, M. M., Pei, D., and Keski-Oja, J. (2002). Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase. J. Biol. Chem. 277, 8440-8448.
    • (2002) J. Biol. Chem , vol.277 , pp. 8440-8448
    • Lehti, K.1    Lohi, J.2    Juntunen, M.M.3    Pei, D.4    Keski-Oja, J.5
  • 36
    • 0034685778 scopus 로고    scopus 로고
    • Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain
    • Lehti, K., Valtanen, H., Wickstrom, S. A., Lohi, J., and Keski-Oja, J. (2000). Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain. J. Biol. Chem. 275, 15006-15013.
    • (2000) J. Biol. Chem , vol.275 , pp. 15006-15013
    • Lehti, K.1    Valtanen, H.2    Wickstrom, S.A.3    Lohi, J.4    Keski-Oja, J.5
  • 37
    • 0034646681 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase-associated degradation of tissue inhibitor of metalloproteinase 2 in human tumor cell lines
    • Maquoi, E., Frankenne, F., Baramova, E., Munaut, C., Sounni, N. E., Remacle, A., Noel, A., Murphy, G., and Foidart, J. M. (2000). Membrane type 1 matrix metalloproteinase-associated degradation of tissue inhibitor of metalloproteinase 2 in human tumor cell lines. J. Biol. Chem. 275, 11368-11378.
    • (2000) J. Biol. Chem , vol.275 , pp. 11368-11378
    • Maquoi, E.1    Frankenne, F.2    Baramova, E.3    Munaut, C.4    Sounni, N.E.5    Remacle, A.6    Noel, A.7    Murphy, G.8    Foidart, J.M.9
  • 38
    • 33846007294 scopus 로고    scopus 로고
    • The roles of substrate thermal stability and P2 and P1 subsite identity on matrix metalloproteinase triplehelical peptidase activity and collagen specificity
    • Minond, D., Lauer-Fields, J. L., Cudic, M., Overall, C. M., Pei, D., Brew, K., Visse, R., Nagase, H., and Fields, G. B. (2006). The roles of substrate thermal stability and P2 and P1 subsite identity on matrix metalloproteinase triplehelical peptidase activity and collagen specificity. J. Biol. Chem. 281, 38302-38313.
    • (2006) J. Biol. Chem , vol.281 , pp. 38302-38313
    • Minond, D.1    Lauer-Fields, J.L.2    Cudic, M.3    Overall, C.M.4    Pei, D.5    Brew, K.6    Visse, R.7    Nagase, H.8    Fields, G.B.9
  • 40
    • 0036683241 scopus 로고    scopus 로고
    • CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
    • Mori, H., Tomari, T., Koshikawa, N., Kajita, M., Itoh, Y., Sato, H., Tojo, H., Yana, I., and Seiki, M. (2002). CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. EMBO J. 21, 3949-3959.
    • (2002) EMBO J , vol.21 , pp. 3949-3959
    • Mori, H.1    Tomari, T.2    Koshikawa, N.3    Kajita, M.4    Itoh, Y.5    Sato, H.6    Tojo, H.7    Yana, I.8    Seiki, M.9
  • 41
    • 0030791315 scopus 로고    scopus 로고
    • Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion
    • Nakahara, H., Howard, L., Thompson, E. W., Sato, H., Seiki, M., Yeh, Y., and Chen, W. T. (1997). Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion. Proc. Natl. Acad. Sci. USA 94, 7959-7964.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7959-7964
    • Nakahara, H.1    Howard, L.2    Thompson, E.W.3    Sato, H.4    Seiki, M.5    Yeh, Y.6    Chen, W.T.7
  • 42
    • 34250344229 scopus 로고    scopus 로고
    • Complete restoration of cell surface activity of transmembrane-truncated MT1-MMP by a glycosylphosphatidylinositol anchor. Implications for MT1-MMP-mediated prommp2 activation and collagenolysis in three-dimensions
    • Nie, J., Pei, J., Blumenthal, M., and Pei, D. (2007). Complete restoration of cell surface activity of transmembrane-truncated MT1-MMP by a glycosylphosphatidylinositol anchor. Implications for MT1-MMP-mediated prommp2 activation and collagenolysis in three-dimensions. J. Biol. Chem. 282, 6438-6443.
    • (2007) J. Biol. Chem , vol.282 , pp. 6438-6443
    • Nie, J.1    Pei, J.2    Blumenthal, M.3    Pei, D.4
  • 43
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573, role in endothelial and tumor cell migration
    • Nyalendo, C., Michaud, M., Beaulieu, E., Roghi, C., Murphy, G., Gingras, D., and Beliveau, R. (2007). Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573, role in endothelial and tumor cell migration. J. Biol. Chem. 282, 15690-15699.
    • (2007) J. Biol. Chem , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Beliveau, R.7
  • 44
    • 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. (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272, 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
  • 45
    • 22544471867 scopus 로고    scopus 로고
    • Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing
    • Osenkowski, P., Meroueh, S. O., Pavel, D., Mobashery, S., and Fridman, R. (2005). Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing. J. Biol. Chem. 280, 26160-26168.
    • (2005) J. Biol. Chem , vol.280 , pp. 26160-26168
    • Osenkowski, P.1    Meroueh, S.O.2    Pavel, D.3    Mobashery, S.4    Fridman, R.5
  • 46
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D., and Weiss, S. J. (1995). Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375, 244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 47
    • 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. (1996). Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271, 9135-9140.
    • (1996) J. Biol. Chem , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 49
    • 9444290419 scopus 로고    scopus 로고
    • Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP
    • Sabeh, F. et al. (2004). Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP. J. Cell Biol. 167, 769-781.
    • (2004) J. Cell Biol , vol.167 , pp. 769-781
    • Sabeh, F.1
  • 50
    • 20044387216 scopus 로고    scopus 로고
    • Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis
    • Sato, H., Takino, T., and Miyamori, H. (2005). Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis. Cancer Sci. 96, 212-217.
    • (2005) Cancer Sci , vol.96 , pp. 212-217
    • Sato, H.1    Takino, T.2    Miyamori, H.3
  • 51
    • 33645294371 scopus 로고    scopus 로고
    • Controversy fuels trafficking of GPI-anchored proteins
    • Schuck, S., and Simons, K. (2006). Controversy fuels trafficking of GPI-anchored proteins. J. Cell Biol. 172, 963-965.
    • (2006) J. Cell Biol , vol.172 , pp. 963-965
    • Schuck, S.1    Simons, K.2
  • 52
    • 37348999017 scopus 로고    scopus 로고
    • Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis
    • Shi, J., Son, M. Y., Yamada, S., Szabova, L., Kahan, S., Chrysovergis, K., Wolf, L., Surmak, A., and Holmbeck, K. (2008). Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis. Dev. Biol. 313, 196-209.
    • (2008) Dev. Biol , vol.313 , pp. 196-209
    • Shi, J.1    Son, M.Y.2    Yamada, S.3    Szabova, L.4    Kahan, S.5    Chrysovergis, K.6    Wolf, L.7    Surmak, A.8    Holmbeck, K.9
  • 53
    • 43049084341 scopus 로고    scopus 로고
    • MT4-(MMP17) and MT6-MMP (MMP25), a unique set of membrane-anchored matrix metalloproteinases: Properties and expression in cancer
    • Sohail, A., Sun, Q., Zhao, H., Bernardo, M. M., Cho, J.-A., and Fridman, R. (2008). MT4-(MMP17) and MT6-MMP (MMP25), a unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer. Cancer Metastasis Rev. 27, 289-302.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 289-302
    • Sohail, A.1    Sun, Q.2    Zhao, H.3    Bernardo, M.M.4    Cho, J.-A.5    Fridman, R.6
  • 54
    • 11144353715 scopus 로고    scopus 로고
    • Up-regulation of vascular endothelial growth factor-A by active membrane-type 1 matrix metalloproteinase through activation of Src-tyrosine kinases
    • Sounni, N. E. et al. (2004). Up-regulation of vascular endothelial growth factor-A by active membrane-type 1 matrix metalloproteinase through activation of Src-tyrosine kinases. J. Biol. Chem. 279, 13564-13574.
    • (2004) J. Biol. Chem , vol.279 , pp. 13564-13574
    • Sounni, N.E.1
  • 55
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): The differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities
    • Tam, E. M., Moore, T. R., Butler, G. S., and Overall, C. M. (2004a). Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J. Biol. Chem. 279, 43336-43344.
    • (2004) J. Biol. Chem , vol.279 , pp. 43336-43344
    • Tam, E.M.1    Moore, T.R.2    Butler, G.S.3    Overall, C.M.4
  • 56
    • 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. (2004b). Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. USA 101, 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
  • 57
    • 0037064041 scopus 로고    scopus 로고
    • Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
    • Tam, E. M., Wu, Y. I., Butler, G. S., Stack, M. S., and Overall, C. M. (2002). Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. J. Biol. Chem. 277, 39005-39014.
    • (2002) J. Biol. Chem , vol.277 , pp. 39005-39014
    • Tam, E.M.1    Wu, Y.I.2    Butler, G.S.3    Stack, M.S.4    Overall, C.M.5
  • 58
    • 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. (2001). Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. J. Cell Biol. 155, 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
  • 59
    • 10944254090 scopus 로고    scopus 로고
    • The hemopexin domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) Is not required for its activation of proMMP2 on cell surface but is essential for MT1-MMP-mediated invasion in three-dimensional type I collagen
    • Wang, P., Nie, J., and Pei, D. (2004). The hemopexin domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) Is not required for its activation of proMMP2 on cell surface but is essential for MT1-MMP-mediated invasion in three-dimensional type I collagen. J. Biol. Chem. 279, 51148-51155.
    • (2004) J. Biol. Chem , vol.279 , pp. 51148-51155
    • Wang, P.1    Nie, J.2    Pei, D.3
  • 60
  • 61
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf, K., Wu, Y. I., Liu, Y., Geiger, J., Tam, E., Overall, C., Stack, M. S., and Friedl, P. (2007). Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat. Cell Biol. 9, 893-904.
    • (2007) Nat. Cell Biol , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 62
    • 22944438407 scopus 로고    scopus 로고
    • FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation
    • Wu, X., Gan, B., Yoo, Y., and Guan, J. L. (2005). FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation. Dev. Cell 9, 185-196.
    • (2005) Dev. Cell , vol.9 , pp. 185-196
    • Wu, X.1    Gan, B.2    Yoo, Y.3    Guan, J.L.4
  • 63
    • 28244483356 scopus 로고    scopus 로고
    • Short hairpin RNA-mediated inhibition of matrix metalloproteinase-1 in MDA-231 cells: Effects on matrix destruction and tumor growth
    • Wyatt, C. A., Geoghegan, J. C., and Brinckerhoff, C. E. (2005). Short hairpin RNA-mediated inhibition of matrix metalloproteinase-1 in MDA-231 cells: effects on matrix destruction and tumor growth. Cancer Res. 65, 11101-11108.
    • (2005) Cancer Res , vol.65 , pp. 11101-11108
    • Wyatt, C.A.1    Geoghegan, J.C.2    Brinckerhoff, C.E.3
  • 64
    • 34547931078 scopus 로고    scopus 로고
    • Modeling tissue morphogenesis and cancer in 3D
    • Yamada, K. M., and Cukierman, E. (2007). Modeling tissue morphogenesis and cancer in 3D. Cell 130, 601-610.
    • (2007) Cell , vol.130 , pp. 601-610
    • Yamada, K.M.1    Cukierman, E.2
  • 65
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana, I., and Weiss, S. J. (2000). Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol. Biol. Cell 11, 2387-2401.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 66
    • 0346690071 scopus 로고    scopus 로고
    • TIMP-2 is released as an intact molecule following binding to MT1-MMP on the cell surface
    • Zucker, S., Hymowitz, M., Conner, C., DeClerck, Y., and Cao, J. (2004). TIMP-2 is released as an intact molecule following binding to MT1-MMP on the cell surface. Exp. Cell Res. 293, 164-174.
    • (2004) Exp. Cell Res , vol.293 , pp. 164-174
    • Zucker, S.1    Hymowitz, M.2    Conner, C.3    DeClerck, Y.4    Cao, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.