메뉴 건너뛰기




Volumn 82, Issue 12, 2002, Pages 1673-1684

Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase A activation

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM CHLORIDE; BAFILOMYCIN A1; CELL SURFACE RECEPTOR; CHLOROQUINE; CONCANAVALIN A; CYTOCHALASIN D; IODINE 125; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; PHORBOL 13 ACETATE 12 MYRISTATE; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 0036901565     PISSN: 00236837     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.LAB.0000041713.74852.2A     Document Type: Article
Times cited : (58)

References (47)
  • 1
    • 0030044503 scopus 로고    scopus 로고
    • Cellular activation of mesangial gelatinase A by cytochalasin D is accompanied by enhanced mRNA expression of both gelatinase A and its membrane-associated gelatinase A activator (MT-MMP)
    • Ailenberg M and Silverman M (1996). Cellular activation of mesangial gelatinase A by cytochalasin D is accompanied by enhanced mRNA expression of both gelatinase A and its membrane-associated gelatinase A activator (MT-MMP). Biochem J 313:879-884.
    • (1996) Biochem J , vol.313 , pp. 879-884
    • Ailenberg, M.1    Silverman, M.2
  • 3
    • 0032446984 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-2 (gelatinase A, MMP-2), membrane-type matrix metalloproteinase-1 (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) expression by elastin-derived peptides in human HT-1080 fibrosarcoma cell fine
    • Brassart B, Randoux A, Hornebeck W, and Emonard H (1998). Regulation of matrix metalloproteinase-2 (gelatinase A, MMP-2), membrane-type matrix metalloproteinase-1 (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) expression by elastin-derived peptides in human HT-1080 fibrosarcoma cell fine. Clin Exp Metastasis 16:489-500.
    • (1998) Clin Exp Metastasis , vol.16 , pp. 489-500
    • Brassart, B.1    Randoux, A.2    Hornebeck, W.3    Emonard, H.4
  • 5
    • 0032567429 scopus 로고    scopus 로고
    • The propeptide domain of membrane type I matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A
    • Cao J, Drews M, Lee HM, Conner C, Bahou WF, and Zucker S (1998). The propeptide domain of membrane type I matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A. J Biol Chem 273:34745-34752.
    • (1998) J Biol Chem , vol.273 , pp. 34745-34752
    • Cao, J.1    Drews, M.2    Lee, H.M.3    Conner, C.4    Bahou, W.F.5    Zucker, S.6
  • 6
    • 0034703025 scopus 로고    scopus 로고
    • The propeptide domain of membrane type 1-matrix metalloproteinase acts as an intramolecular chaperone when expressed in trans with the mature sequence in COS-1 cells
    • Cao J, Hymowitz M, Conner C, Bahou WF, and Zucker S (2000). The propeptide domain of membrane type 1-matrix metalloproteinase acts as an intramolecular chaperone when expressed in trans with the mature sequence in COS-1 cells. J Biol Chem 275:29648-29653.
    • (2000) J Biol Chem , vol.275 , pp. 29648-29653
    • Cao, J.1    Hymowitz, M.2    Conner, C.3    Bahou, W.F.4    Zucker, S.5
  • 7
    • 0032456751 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases in human dermal microvascular endothelial cells: Expression and morphogenic correlation
    • Chan VT, Zhang DN, Nagaravapu U, Hultquist K, Romero LI, and Herron GS (1998). Membrane-type matrix metalloproteinases in human dermal microvascular endothelial cells: Expression and morphogenic correlation. J Invest Dermatol 11:1153-1159.
    • (1998) J Invest Dermatol , vol.11 , pp. 1153-1159
    • Chan, V.T.1    Zhang, D.N.2    Nagaravapu, U.3    Hultquist, K.4    Romero, L.I.5    Herron, G.S.6
  • 8
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague MJ, Urbe S, Aniento F, and Gruenberg J (1994). Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J Biol Chem 269:21-24.
    • (1994) J Biol Chem , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg, J.4
  • 9
    • 0039843091 scopus 로고    scopus 로고
    • Trafficking of proteinase activated receptor-2 and β-arrestin-1 tagged with fluorescent protein: β-arrestin-1 dependent endocytosis of a proteinase receptor
    • Dery O, Thoma MS, Wong H, Grady EF, and Bunnett NW (1999). Trafficking of proteinase activated receptor-2 and β-arrestin-1 tagged with fluorescent protein: β-arrestin-1 dependent endocytosis of a proteinase receptor. J Biol Chem 274:18524-18535.
    • (1999) J Biol Chem , vol.274 , pp. 18524-18535
    • Dery, O.1    Thoma, M.S.2    Wong, H.3    Grady, E.F.4    Bunnett, N.W.5
  • 10
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach A, Louvard D, and Coudrier E (1996). Actin filaments facilitate two steps of endocytosis. J Cell Sci 109:457-465.
    • (1996) J Cell Sci , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 11
    • 0023910242 scopus 로고
    • Lectins modulate the internalization of recombinant interferon-α and the induction of 2′.5′-oligo(A) synthetase
    • Faltynek CR, Princler GL, Ruscetti FW, and Birchenall-Sparks M (1988). Lectins modulate the internalization of recombinant interferon-α and the induction of 2′.5′-oligo(A) synthetase. J Biol Chem 263:7112-7117.
    • (1988) J Biol Chem , vol.263 , pp. 7112-7117
    • Faltynek, C.R.1    Princler, G.L.2    Ruscetti, F.W.3    Birchenall-Sparks, M.4
  • 12
    • 0030045799 scopus 로고    scopus 로고
    • Activation of human umbilical vein endothelial cell progelatinase A by phorbol myristate acetate (PMA): A protein kinase C-dependent mechanism involving a membrane-type matrix metalloproteinase
    • Foda HD, George S, Conner C, Drews M, Tompkins DC, and Zucker S (1996). Activation of human umbilical vein endothelial cell progelatinase A by phorbol myristate acetate (PMA): A protein kinase C-dependent mechanism involving a membrane-type matrix metalloproteinase. Lab Invest 74: 538-545.
    • (1996) Lab Invest , vol.74 , pp. 538-545
    • Foda, H.D.1    George, S.2    Conner, C.3    Drews, M.4    Tompkins, D.C.5    Zucker, S.6
  • 13
    • 0034692498 scopus 로고    scopus 로고
    • Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a posttranslational MT1-MMP-dependent mechanism
    • Gingras D, Page M, Annabi B, and Beliveau R (2000). Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a posttranslational MT1-MMP-dependent mechanism. Biochim Biophys Acta 1497:341-350.
    • (2000) Biochim Biophys Acta , vol.1497 , pp. 341-350
    • Gingras, D.1    Page, M.2    Annabi, B.3    Beliveau, R.4
  • 14
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb TA, Ivanov IE, Adesnik M, and Sabatini DD (1993). Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J Cell Biol 120:695-710.
    • (1993) J Cell Biol , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 15
    • 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, Yurkova M, Gervasi DC, Raz Y, Sang QA, and Fridman R (2000). Binding of active (57 kDa) membrane type-1 matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J Biol Chem 275:12080-12089.
    • (2000) J Biol Chem , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.3    Yurkova, M.4    Gervasi, D.C.5    Raz, Y.6    Sang, Q.A.7    Fridman, R.8
  • 16
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka N, Allen E, Apel IJ, Gyetko MR, and 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
  • 17
    • 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 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
  • 18
    • 0032544524 scopus 로고    scopus 로고
    • Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP-2) specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface
    • Itoh Y, Ito A, Iwata K, Tanzawa K, Mori Y, and Nagase H (1998). Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP-2) specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface. J Biol Chem 273:24360-24367.
    • (1998) J Biol Chem , vol.273 , pp. 24360-24367
    • Itoh, Y.1    Ito, A.2    Iwata, K.3    Tanzawa, K.4    Mori, Y.5    Nagase, H.6
  • 19
    • 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, and 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
  • 20
    • 0034614939 scopus 로고    scopus 로고
    • Role of surface metalloproteinase MT1-MMP in epithelial migration over laminin-5
    • Koshikawa N, Giannelli G, Curculli V, Miyazaki K, and Qaranta V (2000). Role of surface metalloproteinase MT1-MMP in epithelial 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    Curculli, V.3    Miyazaki, K.4    Qaranta, V.5
  • 21
    • 0033597728 scopus 로고    scopus 로고
    • Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase (MT1-MMP) activity in high and low invasive melanoma cells
    • Kurschat P, Zigrino P, Nischt R, Breitkreutz D, Steurer P, Klein EC, Krieg T, and Mauch C (1999). Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase (MT1-MMP) activity in high and low invasive melanoma cells. J Biol Chem 274:21056-21062.
    • (1999) J Biol Chem , vol.274 , pp. 21056-21062
    • Kurschat, P.1    Zigrino, P.2    Nischt, R.3    Breitkreutz, D.4    Steurer, P.5    Klein, E.C.6    Krieg, T.7    Mauch, C.8
  • 22
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze C, Fujimoto M, Yin HL, and Schmid SL (1997). The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J Biol Chem 272:20332-20335.
    • (1997) J Biol Chem , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, M.2    Yin, H.L.3    Schmid, S.L.4
  • 23
    • 0032168205 scopus 로고    scopus 로고
    • Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase activation at the cell surface
    • Lehti K, Lohi J, Valtanen H, and Keski-Qja J (1998). Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase 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-Qja, J.4
  • 24
    • 0031835786 scopus 로고    scopus 로고
    • Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts
    • Li H, Bauzon DE, Xu X, Tschesche H, Cao J, and Sang QA. (1998) Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts. Mol Carcinog 22:84-94.
    • (1998) Mol Carcinog , vol.22 , pp. 84-94
    • Li, H.1    Bauzon, D.E.2    Xu, X.3    Tschesche, H.4    Cao, J.5    Sang, Q.A.6
  • 25
    • 0030055680 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate
    • Lohi J, Lehti K, Westermarck J, Kahari V-M, and Keski-Oja J (1996). Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate. Eur J Biochem 239:239-247.
    • (1996) Eur J Biochem , vol.239 , pp. 239-247
    • Lohi, J.1    Lehti, K.2    Westermarck, J.3    Kahari, V.-M.4    Keski-Oja, J.5
  • 26
    • 0031438076 scopus 로고    scopus 로고
    • G protein-coupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts: Shc phosphorylation and receptor endocytosis correlate with activation of Erk kinases
    • Luttrell LM, Daaka Y, Della Rocca GJ, and Lefkowitz RJ (1997). G protein-coupled receptors mediate two functionally distinct pathways of tyrosine phosphorylation in rat 1a fibroblasts: Shc phosphorylation and receptor endocytosis correlate with activation of Erk kinases. J Biol Chem 272: 31648-31656.
    • (1997) J Biol Chem , vol.272 , pp. 31648-31656
    • Luttrell, L.M.1    Daaka, Y.2    Della Rocca, G.J.3    Lefkowitz, R.J.4
  • 27
    • 0034646681 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase-associated degradation of tissue inhibitor of metalloproteinase 2 in human tumor cell lines
    • Maquoi E, Frankenne F, Baramova E, Munaut C, Sounni NE, Remacle A, Noel A, Murphy G, and Foidart J-M (2000). Membrane type I 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
  • 29
    • 0030791315 scopus 로고    scopus 로고
    • Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloproteinase docking to invadopodia is required for cell invasion
    • Nakahara H, Howard L, Thompson EW, Sato H, Seiki Y, Yeh Y, and Chen WT (1998). Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloproteinase docking to invadopodia is required for cell invasion. Proc Nati Acad Sci USA 94:7959-7964.
    • (1998) Proc Nati Acad Sci USA , vol.94 , pp. 7959-7964
    • Nakahara, H.1    Howard, L.2    Thompson, E.W.3    Sato, H.4    Seiki, Y.5    Yeh, Y.6    Chen, W.T.7
  • 30
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other matrix macromolecules
    • Ohuchi E, Imai K, Fuji Y, Sato H, Seiki M, and Okada Y (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other matrix macromolecules. J Biol Chem 272:2446-2451.
    • (1997) J Biol Chem , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fuji, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 31
    • 0030904444 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases during rat skin wound healing: Evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A
    • Okada A, Tomasetto C, Lutz Y, Bellocq J-P, Rio M-C, and Basset P (1997). Expression of matrix metalloproteinases during rat skin wound healing: Evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A. J Cell Biol 137:67-77.
    • (1997) J Cell Biol , vol.137 , pp. 67-77
    • Okada, A.1    Tomasetto, C.2    Lutz, Y.3    Bellocq, J.-P.4    Rio, M.-C.5    Basset, P.6
  • 32
    • 0025676432 scopus 로고
    • Concanavalin A produces a matrix-degradative phenotype in human fibroblasts: Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of tissue inhibitor of matrix metalloproteinases
    • Overall CM and Sodek J (1990). Concanavalin A produces a matrix-degradative phenotype in human fibroblasts: Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of tissue inhibitor of matrix metalloproteinases. J Biol Chem 265:21141-21151.
    • (1990) J Biol Chem , vol.265 , pp. 21141-21151
    • Overall, C.M.1    Sodek, J.2
  • 33
    • 0033605561 scopus 로고    scopus 로고
    • Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP
    • Pei D (1999). Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP. J Biol Chem 274:8925-8932.
    • (1999) J Biol Chem , vol.274 , pp. 8925-8932
    • Pei, D.1
  • 34
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase process progelatinase A and express intrinsic matrix-degrading activity
    • Pei D and Weiss SJ (1996). Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase 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
  • 35
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche A, Paris S, and Jackson CL (1996). Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384:479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 36
    • 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 of Glu-240 and furin cleavage motifs in oligomerization, processing and self-proteolysis of MT1-MMP expressed in breast cancer
    • Rozanov DV, Deryugina EI, Ratnikov BI, Monosov EZ, Marchenko GN, Machenko GN, Quigley JP, and Strongin AY (2001). Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP): The role of the cytoplasmic tail Cys-574, the active site of Glu-240 and furin cleavage motifs in oligomerization, processing and self-proteolysis of MT1-MMP expressed in breast cancer. J Biol Chem: 276:25705-25714.
    • (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    Machenko, G.N.6    Quigley, J.P.7    Strongin, A.Y.8
  • 37
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumor cells
    • Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, and Seiki M (1994). A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 370:61-65.
    • (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
  • 38
    • 0030022242 scopus 로고    scopus 로고
    • Inhibition of mitogen-induced DNA synthesis by bafilomycin A1 in Swiss 3T3 fibroblasts
    • Saurin AJ, Hamlett J, Clague MJ, and Pennington SR (1996). Inhibition of mitogen-induced DNA synthesis by bafilomycin A1 in Swiss 3T3 fibroblasts. Biochem J 313:65-70.
    • (1996) Biochem J , vol.313 , pp. 65-70
    • Saurin, A.J.1    Hamlett, J.2    Clague, M.J.3    Pennington, S.R.4
  • 39
    • 0031656621 scopus 로고    scopus 로고
    • Role of tissue inhibitor of metalloproteinase-2 (TIMP-2) in regulation of progelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells
    • Shofuda K-I, Moriyama K, Kishihashi A, Higashi S, Mizushima H, Yasumitsu H, Miki K, Sato H, Seiki M, and Miyazaki K (1998). Role of tissue inhibitor of metalloproteinase-2 (TIMP-2) in regulation of progelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells. J Biochem 124:462-470.
    • (1998) J Biochem , vol.124 , pp. 462-470
    • Shofuda, K.-I.1    Moriyama, K.2    Kishihashi, A.3    Higashi, S.4    Mizushima, H.5    Yasumitsu, H.6    Miki, K.7    Sato, H.8    Seiki, M.9    Miyazaki, K.10
  • 40
    • 0031727149 scopus 로고    scopus 로고
    • The activation of pro-MMP-2 (gelatinase A) by HT-1080 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 S, d'Ortho M-P, Yamada KM, Zardi L, and Murphy G (1998). The activation of pro-MMP-2 (gelatinase A) by HT-1080 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.3    D'Ortho, M.-P.4    Yamada, K.M.5    Zardi, L.6    Murphy, G.7
  • 41
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase: Isolation of the activated form of the membrane metalloproteinase
    • Strongin AY, Collier I, Bannicov G, Marmer BL, Grant GZ, and Goldberg GI (1995). Mechanism of cell surface activation of 72-kDa type IV collagenase: Isolation of the activated form of the membrane metalloproteinase. J Biol Chem 270:5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannicov, G.3    Marmer, B.L.4    Grant, G.Z.5    Goldberg, G.I.6
  • 42
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Taub LM and Kornfeld S (1997). The trans-Golgi network: A late secretory sorting station. Curr Opin Cell Biol 9:527-533.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 527-533
    • Taub, L.M.1    Kornfeld, S.2
  • 43
    • 0034731479 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2
    • Toth M, Bernardo MM, Gervasi DC, Soloway P, Wang Z, Bigg HF, Overall CM, DeClerck YA, Tschesche H, Cher ML, Brown S, Mobashery S, and Fridman R (2000). Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2. J Biol Chem 275:41415-41423.
    • (2000) J Biol Chem , vol.275 , pp. 41415-41423
    • Toth, M.1    Bernardo, M.M.2    Gervasi, D.C.3    Soloway, P.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
  • 44
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH terminal truncation
    • Vey M, Schafer W, Berghofer S, Klenk H-D, and Garten W (1993). Maturation of the trans-Golgi network furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH terminal truncation. J Cell Biol 121:1829-1842.
    • (1993) J Cell Biol , vol.121 , pp. 1829-1842
    • Vey, M.1    Schafer, W.2    Berghofer, S.3    Klenk, H.-D.4    Garten, W.5
  • 45
    • 0030694312 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mediates conA-induced membrane type 1-matrix metalloproteinase expression and matrix metalloproteinase-2 activation in MDA-MB-231 human breast carcinoma cells
    • Yu M, Bowden ET, Sitlani J, Sato H, Seiki M, Mueller SC, and Thompson EW (1998). Tyrosine phosphorylation mediates conA-induced membrane type 1-matrix metalloproteinase expression and matrix metalloproteinase-2 activation in MDA-MB-231 human breast carcinoma cells. Cancer Res 57:5028-5034.
    • (1998) Cancer Res , vol.57 , pp. 5028-5034
    • Yu, M.1    Bowden, E.T.2    Sitlani, J.3    Sato, H.4    Seiki, M.5    Mueller, S.C.6    Thompson, E.W.7
  • 46
    • 0034722898 scopus 로고    scopus 로고
    • Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment
    • Zucker S, Cao J, and Chen W-T (2000). Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment. Oncogene 19:6642-6650.
    • (2000) Oncogene , vol.19 , pp. 6642-6650
    • Zucker, S.1    Cao, J.2    Chen, W.-T.3
  • 47
    • 0031984868 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)
    • Zucker S, Drews M, Conner C, Foda HD, DeCLerck A, Langley KE, Bahou WF, Docherty AJP, and Cao J (1998). Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP). J Biol Chem 273: 1216-1222.
    • (1998) J Biol Chem , vol.273 , pp. 1216-1222
    • Zucker, S.1    Drews, M.2    Conner, C.3    Foda, H.D.4    DeCLerck, A.5    Langley, K.E.6    Bahou, W.F.7    Docherty, A.J.P.8    Cao, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.