메뉴 건너뛰기




Volumn 206, Issue 1, 2006, Pages 1-8

MT1-MMP: A potent modifier of pericellular microenvironment

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; DOUBLE STRANDED RNA; GELATINASE A; HERMES ANTIGEN; MATRIX METALLOPROTEINASE 14; MEMBRANE ENZYME; MITOGEN ACTIVATED PROTEIN KINASE; OLIGOMER; SYNDECAN 1;

EID: 28444454893     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.20431     Document Type: Review
Times cited : (431)

References (92)
  • 1
    • 5444242206 scopus 로고    scopus 로고
    • The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells
    • Beauvais DM, Burbach BJ, Rapraeger AC. 2004. The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells. J Cell Biol 167:171-181.
    • (2004) J Cell Biol , vol.167 , pp. 171-181
    • Beauvais, D.M.1    Burbach, B.J.2    Rapraeger, A.C.3
  • 2
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin AM, Akimov SS, Zaritskaya LS, Ratnikov BI, Deryugina EI, Strongin AY. 2001. Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J Biol Chem 276:18415-18422.
    • (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
  • 4
    • 0035328844 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase
    • Bigg HF, Morrison CJ, Butler GS, Bogoyevitch MA, Wang Z, Sploway PD, Overall CM. 2001. Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase. Cancer Res 61:3610-3618.
    • (2001) Cancer Res , vol.61 , pp. 3610-3618
    • Bigg, H.F.1    Morrison, C.J.2    Butler, G.S.3    Bogoyevitch, M.A.4    Wang, Z.5    Sploway, P.D.6    Overall, C.M.7
  • 5
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tale of a frog that became a prince
    • Brinckerhoff CE, Matrisian LM. 2002. Matrix metalloproteinases: A tale 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
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • Brooks PC, Silletti S, von Schalscha TL, Friedlander M, Cheresh DA. 1998. Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell 92:391-400.
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    Von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 8
    • 0028924956 scopus 로고
    • The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation
    • Cao J, Sato H, Takino T, Seiki M. 1995. The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation. J Biol Chem 270:801-805.
    • (1995) J Biol Chem , vol.270 , pp. 801-805
    • Cao, J.1    Sato, H.2    Takino, T.3    Seiki, M.4
  • 9
    • 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 WF, 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
  • 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 MP, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J, Smith B, Timpl R, Zardi L, 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
    • 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
    • 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 EI, Ratnikov BI, Postnova TI, Rozanov DV, Strongin AY. 2002a. 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 277:9749-9756.
    • (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
  • 13
    • 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 EI, Soroceanu L, Strongin AY. 2002b. Up-regulation of vascular endothelial growth factor by membrane-type 1 matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis. Cancer Res 62:580-588.
    • (2002) Cancer Res , vol.62 , pp. 580-588
    • Deryugina, E.I.1    Soroceanu, L.2    Strongin, A.Y.3
  • 14
    • 0035816605 scopus 로고    scopus 로고
    • Functional interplay between type I collagen and cell surface matrix metalloproteinase activity
    • Ellerbroek SM, Wu YI, Overall CM, Stack MS. 2001. Functional interplay between type I collagen and cell surface matrix metalloproteinase activity. J Biol Chem 276:24833-24842.
    • (2001) J Biol Chem , vol.276 , pp. 24833-24842
    • Ellerbroek, S.M.1    Wu, Y.I.2    Overall, C.M.3    Stack, M.S.4
  • 15
    • 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, Sato H. 2003. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J Biol Chem 278:40764-40770.
    • (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
  • 17
    • 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 MP, Annabi B, Beliveau R. 2001. Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP). FEBS Lett 507:231-236.
    • (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
  • 18
    • 0032707133 scopus 로고    scopus 로고
    • Shedding of membrane type 1 matrix metalloproteinase in a human breast carcinoma cell line
    • Harayama T, Ohuchi E, Aoki T, Sato H, Seiki M, Okada Y. 1999. Shedding of membrane type 1 matrix metalloproteinase in a human breast carcinoma cell line. Jpn J Cancer Res 90:942-950.
    • (1999) Jpn J Cancer Res , vol.90 , pp. 942-950
    • Harayama, T.1    Ohuchi, E.2    Aoki, T.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 19
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka N, Allen E, Apel IJ, Gyetko MR, Weiss SJ. 1998. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. 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
  • 23
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • Hotary K, Allen E, Punturieri A, Yana I, Weiss SJ. 2000. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J Cell Biol 149:1309-1323.
    • (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
  • 24
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary KB, Allen ED, Brooks PC, Datta NS, Long MW, Weiss SJ. 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
  • 25
    • 0037509851 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer
    • Itoh Y, Nagase H. 2002. Matrix metalloproteinases in cancer. Essays Biochem 38:21-36.
    • (2002) Essays Biochem , vol.38 , pp. 21-36
    • Itoh, Y.1    Nagase, H.2
  • 26
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • Itoh Y, Seiki M. 2004. MT1-MMP: An enzyme with multidimensional regulation. TiBS 29:285-289.
    • (2004) TiBS , vol.29 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 27
    • 0033607524 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase
    • Itoh Y, Kajita M, Kinoh H, Mori H, Okada A, Seiki M. 1999. Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol- anchored proteinase. J Biol Chem 274:34260-34266.
    • (1999) J Biol Chem , vol.274 , pp. 34260-34266
    • Itoh, Y.1    Kajita, M.2    Kinoh, H.3    Mori, H.4    Okada, A.5    Seiki, M.6
  • 28
    • 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, Seiki M. 2001. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 20:4782-4793.
    • (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
  • 29
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis
    • Jiang A, Lehti K, Wang X, Weiss SJ, Keski-Oja J, Pei D. 2001. Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis. Proc Natl Acad Sci USA 98:13693-13698.
    • (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
  • 30
    • 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, Seiki M. 2001. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol 153:893-904.
    • (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
  • 31
    • 0032568932 scopus 로고    scopus 로고
    • TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads
    • Kinoshita T, Sato H, Okada A, Ohuchi E, Imai K, Okada Y, Seiki M. 1998. TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 273:16098-16103.
    • (1998) J Biol Chem , vol.273 , pp. 16098-16103
    • Kinoshita, T.1    Sato, H.2    Okada, A.3    Ohuchi, E.4    Imai, K.5    Okada, Y.6    Seiki, M.7
  • 32
    • 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
    • Knäuper V, Will H, López-Otín C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G. 1996. 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 271:17124-17131.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knäuper, V.1    Will, H.2    López-Otín, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 33
    • 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, 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
  • 34
    • 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, Quaranta V. 2000. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol 148:615-624.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 35
    • 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, 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
  • 36
    • 0036712828 scopus 로고    scopus 로고
    • Endothelial tubulogenesis within fibrin gels specifically requires the activity of membrane-type-matrix metalloproteinases (MT-MMPs)
    • Lafleur MA, Handsley MM, Knauper V, Murphy G, Edwards DR. 2002. Endothelial tubulogenesis within fibrin gels specifically requires the activity of membrane-type-matrix metalloproteinases (MT-MMPs). J Cell Sci 115: 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
  • 37
    • 0032168205 scopus 로고    scopus 로고
    • Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface
    • Lehti K, Lohi J, Valtanen H, Keski-Oja J. 1998. Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface. Biochem J 334:345-353.
    • (1998) Biochem J , vol.334 , pp. 345-353
    • Lehti, K.1    Lohi, J.2    Valtanen, H.3    Keski-Oja, J.4
  • 38
    • 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 MM, Pei D, 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
  • 39
    • 4944233738 scopus 로고    scopus 로고
    • Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar
    • Li Y, Aoki T, Mori Y, Ahmad M, Miyamori H, Takino T, Sato H. 2004. Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar. Cancer Res 64:7058-7064.
    • (2004) Cancer Res , vol.64 , pp. 7058-7064
    • Li, Y.1    Aoki, T.2    Mori, Y.3    Ahmad, M.4    Miyamori, H.5    Takino, T.6    Sato, H.7
  • 40
    • 13444310742 scopus 로고    scopus 로고
    • Intracellular processing and activation of membrane type 1 matrix metalloprotease depends on its partitioning into lipid domains
    • Mazzone M, Baldassarre M, Beznoussenko G, Giacchetti G, Cao J, Zucker S, Luini A, Buccione R. 2004. Intracellular processing and activation of membrane type 1 matrix metalloprotease depends on its partitioning into lipid domains. J Cell Sci 117:6275-6287.
    • (2004) J Cell Sci , vol.117 , pp. 6275-6287
    • Mazzone, M.1    Baldassarre, M.2    Beznoussenko, G.3    Giacchetti, G.4    Cao, J.5    Zucker, S.6    Luini, A.7    Buccione, R.8
  • 41
    • 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, 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
  • 42
    • 0032820711 scopus 로고    scopus 로고
    • Proteolysis and cell migration: Creating a path
    • Murphy G, Gavrilovic J. 1999. Proteolysis and cell migration: Creating a path. Curr Opin Cell Biol 11:614-621.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 614-621
    • Murphy, G.1    Gavrilovic, J.2
  • 43
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. 1997. Activation mechanisms of matrix metalloproteinases. Biol Chem 378:151-160.
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 44
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF, Jr. 1999. Matrix metalloproteinases. J Biol Chem 274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 45
    • 0035893764 scopus 로고    scopus 로고
    • Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes
    • Nakada M, Yamada A, Takino T, Miyamori H, Takahashi T, Yamashita J, Sato H. 2001. Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes. Cancer Res 61:8896-8902.
    • (2001) Cancer Res , vol.61 , pp. 8896-8902
    • Nakada, M.1    Yamada, A.2    Takino, T.3    Miyamori, H.4    Takahashi, T.5    Yamashita, J.6    Sato, H.7
  • 46
    • 0030966842 scopus 로고    scopus 로고
    • CD44: Structure, function, and association with the malignant process
    • Naot D, Sionov RV, Ish-Shalom D. 1997. CD44: Structure, function, and association with the malignant process. Adv Cancer Res 71:241-319.
    • (1997) Adv Cancer Res , vol.71 , pp. 241-319
    • Naot, D.1    Sionov, R.V.2    Ish-Shalom, D.3
  • 48
    • 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, 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
  • 49
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • Osenkowski P, Toth M, Fridman R. 2004. Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). J Cell Physiol 200:2-10.
    • (2004) J Cell Physiol , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 50
    • 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
    • Remade A, Murphy G, Roghi C. 2003. Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface. J Cell Sci 116:3905-3916.
    • (2003) J Cell Sci , vol.116 , pp. 3905-3916
    • Remade, A.1    Murphy, G.2    Roghi, C.3
  • 51
    • 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 DV, Hahn-Dantona E, Strickland DK, Strongin AY. 2004. 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 279:4260-4268.
    • (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
  • 53
  • 54
    • 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, Seiki M. 1996. 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 393:101-104.
    • (1996) FEBS Lett , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 56
    • 0037437146 scopus 로고    scopus 로고
    • Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution
    • Schenk S, Hintermann E, Bilban M, Koshikawa N, Hojilla C, Khokha R, Quarante V. 2003. Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J Cell Biol 161: 197-209.
    • (2003) J Cell Biol , vol.161 , pp. 197-209
    • Schenk, S.1    Hintermann, E.2    Bilban, M.3    Koshikawa, N.4    Hojilla, C.5    Khokha, R.6    Quarante, V.7
  • 57
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • Seiki M. 1999. Membrane-type matrix metalloproteinases. Apmis 107:137-143.
    • (1999) Apmis , vol.107 , pp. 137-143
    • Seiki, M.1
  • 58
    • 0036775766 scopus 로고    scopus 로고
    • The cell surface: The stage for matrix metalloproteinase regulation of migration
    • Seiki M. 2002. The cell surface: The stage for matrix metalloproteinase regulation of migration. Curr Opin Cell Biol 14:624-632.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 624-632
    • Seiki, M.1
  • 59
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • Seiki M. 2003. Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion. Cancer Lett 194:1-11.
    • (2003) Cancer Lett , vol.194 , pp. 1-11
    • Seiki, M.1
  • 60
    • 0035793037 scopus 로고    scopus 로고
    • Disruption of matrix metalloproteinase 2 binding to integrin αvβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo
    • Silletti S, Kessler T, Goldberg J, Boger DL, Cheresh DA. 2001. Disruption of matrix metalloproteinase 2 binding to integrin αvβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc Natl Acad Sci USA 98:119-124.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 119-124
    • Silletti, S.1    Kessler, T.2    Goldberg, J.3    Boger, D.L.4    Cheresh, D.A.5
  • 63
    • 0031727149 scopus 로고    scopus 로고
    • The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form
    • Stanton H, Gavrilovic J, Atkinson SJ, d'Ortho MP, Yamada KM, Zardi L, Murphy G. 1998. The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form. J Cell Sci 111:2789-2798.
    • (1998) J Cell Sci , vol.111 , pp. 2789-2798
    • Stanton, H.1    Gavrilovic, J.2    Atkinson, S.J.3    D'Ortho, M.P.4    Yamada, K.M.5    Zardi, L.6    Murphy, G.7
  • 64
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. 2001. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17:463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 65
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson WG, Aznavoorian S, Liotta LA. 1993. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu Rev Cell Biol 9:541-573.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 66
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. 1995. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 270:5331-5338.
    • (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
  • 67
    • 13444273084 scopus 로고    scopus 로고
    • CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase
    • Suenaga N, Mori H, Itoh Y, Seiki M. 2005. CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase. Oncogene 24:859-868.
    • (2005) Oncogene , vol.24 , pp. 859-868
    • Suenaga, N.1    Mori, H.2    Itoh, Y.3    Seiki, M.4
  • 69
    • 0037466459 scopus 로고    scopus 로고
    • Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase
    • Takino T, Miyamori H, Kawaguchi N, Uekita T, Seiki M, Sato H. 2003. Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase. Biochem Biophys Res Commun 304:160-166.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 160-166
    • Takino, T.1    Miyamori, H.2    Kawaguchi, N.3    Uekita, T.4    Seiki, M.5    Sato, H.6
  • 70
    • 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, Sato H. 2004. Membrane type 1 matrix metalloproteinase regulates collagen-dependent mitogen-activated protein/extracellular signal-related kinase activation and cell migration. Cancer Res 64:1044-1049.
    • (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
  • 72
    • 17644390235 scopus 로고    scopus 로고
    • Cleavage at the stem region releases an active ectodomain of the membrane type 1-matrix metalloproteinase
    • Toth M, Osenkowski P, Hesek D, Brown S, Meroueh S, Sakr W, Mobashery S, Fridman R. 2004. Cleavage at the stem region releases an active ectodomain of the membrane type 1-matrix metalloproteinase. Biochem J 387:497-506.
    • (2004) Biochem J , vol.387 , pp. 497-506
    • Toth, M.1    Osenkowski, P.2    Hesek, D.3    Brown, S.4    Meroueh, S.5    Sakr, W.6    Mobashery, S.7    Fridman, R.8
  • 73
    • 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, Seiki M. 1996. Expression of membrane-type matrix metalloproteinase 1 (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis assay. Cancer Res 56:5678-5683.
    • (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
  • 74
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration
    • Udayakumar TS, Chen ML, Bair EL, Von Bredow DC, Cress AE, Nagle RB, Bowden GT. 2003. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res 63:2292-2299.
    • (2003) Cancer Res , vol.63 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 75
    • 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, Seiki M. 2003. 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 22:8716-8722.
    • (2003) Oncogene , vol.22 , pp. 8716-8722
    • Ueda, J.1    Kajita, M.2    Suenaga, N.3    Fujii, K.4    Seiki, M.5
  • 76
    • 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, 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
  • 77
    • 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, Seiki M. 2004. 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 279:12734-12743.
    • (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
  • 78
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 80
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H. 2003. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry. Circ Res 92:827-839.
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 81
    • 0034714202 scopus 로고    scopus 로고
    • TIMP-2 is required for efficient activation of proMMP-2 in vivo
    • Wang Z, Juttermann R, Soloway PD. 2000. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem 275:26411-26415.
    • (2000) J Biol Chem , vol.275 , pp. 26411-26415
    • Wang, Z.1    Juttermann, R.2    Soloway, P.D.3
  • 82
    • 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, Pei D. 2004a. 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
  • 83
    • 2442561408 scopus 로고    scopus 로고
    • Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV
    • Wang P, Wang X, Pei D. 2004b. Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV. J Biol Chem 279:20461-20470.
    • (2004) J Biol Chem , vol.279 , pp. 20461-20470
    • Wang, P.1    Wang, X.2    Pei, D.3
  • 84
    • 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, Pei D. 2004c. Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal. J Biol Chem 279:9331-9336.
    • (2004) J Biol Chem , vol.279 , pp. 9331-9336
    • Wang, X.1    Ma, D.2    Keski-Oja, J.3    Pei, D.4
  • 85
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb Z. 1997. ECM and cell surface proteolysis: Regulating cellular ecology. Cell 91:439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 86
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. 1996. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem 271:17119-17123.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 89
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana I, Weiss SJ. 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
  • 90
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu Q, Stamenkovic I. 1999. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev 13:35-48.
    • (1999) Genes Dev , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.