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Volumn 314, Issue 13, 2008, Pages 2501-2514

MT1-MMP releases latent TGF-β1 from endothelial cell extracellular matrix via proteolytic processing of LTBP-1

Author keywords

ECM; Endothelial cells; LTBP; MT1 MMP; TGF

Indexed keywords

INTERSTITIAL COLLAGENASE; LATENT TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN; LATENT TRANSFORMING GROWTH FACTOR BETA1 BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHORBOL 13 ACETATE 12 MYRISTATE; PLASMIN; PROTEIN KINASE C; SHORT HAIRPIN RNA; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; UROKINASE;

EID: 47349086991     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.05.018     Document Type: Article
Times cited : (124)

References (67)
  • 2
    • 35448991324 scopus 로고    scopus 로고
    • Extracellular control of TGFbeta signalling in vascular development and disease
    • ten Dijke P., and Arthur H.M. Extracellular control of TGFbeta signalling in vascular development and disease. Nat. Rev. Mol. Cell Biol. 8 (2007) 857-869
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 857-869
    • ten Dijke, P.1    Arthur, H.M.2
  • 10
    • 0037007226 scopus 로고    scopus 로고
    • Balancing the activation state of the endothelium via two distinct TGF-beta type I receptors
    • Goumans M.J., Valdimarsdottir G., Itoh S., Rosendahl A., Sideras P., and ten Dijke P. Balancing the activation state of the endothelium via two distinct TGF-beta type I receptors. EMBO J. 21 (2002) 1743-1753
    • (2002) EMBO J. , vol.21 , pp. 1743-1753
    • Goumans, M.J.1    Valdimarsdottir, G.2    Itoh, S.3    Rosendahl, A.4    Sideras, P.5    ten Dijke, P.6
  • 11
    • 0031106404 scopus 로고    scopus 로고
    • Transforming growth factor-beta: vasculogenesis, angiogenesis, and vessel wall integrity
    • Pepper M.S. Transforming growth factor-beta: vasculogenesis, angiogenesis, and vessel wall integrity. Cytokine Growth Factor Rev. 8 (1997) 21-43
    • (1997) Cytokine Growth Factor Rev. , vol.8 , pp. 21-43
    • Pepper, M.S.1
  • 12
    • 0027176133 scopus 로고
    • Biphasic effect of transforming growth factor-beta 1 on in vitro angiogenesis
    • Pepper M.S., Vassalli J.D., Orci L., and Montesano R. Biphasic effect of transforming growth factor-beta 1 on in vitro angiogenesis. Exp. Cell Res. 204 (1993) 356-363
    • (1993) Exp. Cell Res. , vol.204 , pp. 356-363
    • Pepper, M.S.1    Vassalli, J.D.2    Orci, L.3    Montesano, R.4
  • 13
    • 0028952342 scopus 로고
    • Positive correlation of plasma transforming growth factor-beta 1 levels with tumor vascularity in hepatocellular carcinoma
    • Ito N., Kawata S., Tamura S., Shirai Y., Kiso S., Tsushima H., and Matsuzawa Y. Positive correlation of plasma transforming growth factor-beta 1 levels with tumor vascularity in hepatocellular carcinoma. Cancer Lett. 89 (1995) 45-48
    • (1995) Cancer Lett. , vol.89 , pp. 45-48
    • Ito, N.1    Kawata, S.2    Tamura, S.3    Shirai, Y.4    Kiso, S.5    Tsushima, H.6    Matsuzawa, Y.7
  • 14
    • 0026712153 scopus 로고
    • Excessive production of transforming growth-factor beta 1 can play an important role in the development of tumorigenesis by its action for angiogenesis: validity of neutralizing antibodies to block tumor growth
    • Ueki N., Nakazato M., Ohkawa T., Ikeda T., Amuro Y., Hada T., and Higashino K. Excessive production of transforming growth-factor beta 1 can play an important role in the development of tumorigenesis by its action for angiogenesis: validity of neutralizing antibodies to block tumor growth. Biochim. Biophys. Acta. 1137 (1992) 189-196
    • (1992) Biochim. Biophys. Acta. , vol.1137 , pp. 189-196
    • Ueki, N.1    Nakazato, M.2    Ohkawa, T.3    Ikeda, T.4    Amuro, Y.5    Hada, T.6    Higashino, K.7
  • 15
    • 0033032231 scopus 로고    scopus 로고
    • Role of interleukin 10 and transforming growth factor beta1 in the angiogenesis and metastasis of human prostate primary tumor lines from orthotopic implants in severe combined immunodeficiency mice
    • Stearns M.E., Garcia F.U., Fudge K., Rhim J., and Wang M. Role of interleukin 10 and transforming growth factor beta1 in the angiogenesis and metastasis of human prostate primary tumor lines from orthotopic implants in severe combined immunodeficiency mice. Clin. Cancer Res. 5 (1999) 711-720
    • (1999) Clin. Cancer Res. , vol.5 , pp. 711-720
    • Stearns, M.E.1    Garcia, F.U.2    Fudge, K.3    Rhim, J.4    Wang, M.5
  • 16
    • 0028956737 scopus 로고
    • Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J., Lohi J., Saarinen J., Kovanen P.T., and Keski-Oja J. Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J. Biol. Chem. 270 (1995) 4689-4696
    • (1995) J. Biol. Chem. , vol.270 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3    Kovanen, P.T.4    Keski-Oja, J.5
  • 17
    • 0025765844 scopus 로고
    • A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1
    • Miyazono K., Olofsson A., Colosetti P., and Heldin C.H. A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1. EMBO J. 10 (1991) 1091-1101
    • (1991) EMBO J. , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.H.4
  • 18
    • 0027976521 scopus 로고
    • Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein
    • Taipale J., Miyazono K., Heldin C.H., and Keski-Oja J. Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein. J. Cell Biol. 124 (1994) 171-181
    • (1994) J. Cell Biol. , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.H.3    Keski-Oja, J.4
  • 19
    • 3042838388 scopus 로고    scopus 로고
    • Latent TGF-beta binding proteins: extracellular matrix association and roles in TGF-beta activation
    • Hyytiainen M., Penttinen C., and Keski-Oja J. Latent TGF-beta binding proteins: extracellular matrix association and roles in TGF-beta activation. Crit. Rev. Clin. Lab. Sci. 41 (2004) 233-264
    • (2004) Crit. Rev. Clin. Lab. Sci. , vol.41 , pp. 233-264
    • Hyytiainen, M.1    Penttinen, C.2    Keski-Oja, J.3
  • 20
    • 26844519689 scopus 로고    scopus 로고
    • Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts
    • Koli K., Hyytiainen M., Ryynanen M.J., and Keski-Oja J. Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts. Exp. Cell Res. 310 (2005) 370-382
    • (2005) Exp. Cell Res. , vol.310 , pp. 370-382
    • Koli, K.1    Hyytiainen, M.2    Ryynanen, M.J.3    Keski-Oja, J.4
  • 21
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor beta 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils
    • Gibson M.A., Hatzinikolas G., Davis E.C., Baker E., Sutherland G.R., and Mecham R.P. Bovine latent transforming growth factor beta 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Mol. Cell. Biol. 15 (1995) 6932-6942
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 22
    • 0033840527 scopus 로고    scopus 로고
    • Specific sequence motif of 8-cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta
    • Saharinen J., and Keski-Oja J. Specific sequence motif of 8-cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta. Mol. Biol. Cell. 11 (2000) 2691-2704
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2691-2704
    • Saharinen, J.1    Keski-Oja, J.2
  • 23
    • 0026447801 scopus 로고
    • Release of transforming growth factor-beta 1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin
    • Taipale J., Koli K., and Keski-Oja J. Release of transforming growth factor-beta 1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin. J. Biol. Chem. 267 (1992) 25378-25384
    • (1992) J. Biol. Chem. , vol.267 , pp. 25378-25384
    • Taipale, J.1    Koli, K.2    Keski-Oja, J.3
  • 24
    • 0037077212 scopus 로고    scopus 로고
    • Proteolysis of latent transforming growth factor-beta (TGF-beta)-binding protein-1 by osteoclasts. A cellular mechanism for release of TGF-beta from bone matrix
    • Dallas S.L., Rosser J.L., Mundy G.R., and Bonewald L.F. Proteolysis of latent transforming growth factor-beta (TGF-beta)-binding protein-1 by osteoclasts. A cellular mechanism for release of TGF-beta from bone matrix. J. Biol. Chem. 277 (2002) 21352-21360
    • (2002) J. Biol. Chem. , vol.277 , pp. 21352-21360
    • Dallas, S.L.1    Rosser, J.L.2    Mundy, G.R.3    Bonewald, L.F.4
  • 25
    • 0030908028 scopus 로고    scopus 로고
    • Latent transforming growth factor-beta: structural features and mechanisms of activation
    • Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I., and Rifkin D.B. Latent transforming growth factor-beta: structural features and mechanisms of activation. Kidney Int. 51 (1997) 1376-1382
    • (1997) Kidney Int. , vol.51 , pp. 1376-1382
    • Munger, J.S.1    Harpel, J.G.2    Gleizes, P.E.3    Mazzieri, R.4    Nunes, I.5    Rifkin, D.B.6
  • 26
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes J.P., Munger J.S., and Rifkin D.B. Making sense of latent TGFbeta activation. J. Cell. Sci. 116 (2003) 217-224
    • (2003) J. Cell. Sci. , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 27
    • 21744437609 scopus 로고    scopus 로고
    • Apoptosis of human endothelial cells is accompanied by proteolytic processing of latent TGF-beta binding proteins and activation of TGF-beta
    • Solovyan V.T., and Keski-Oja J. Apoptosis of human endothelial cells is accompanied by proteolytic processing of latent TGF-beta binding proteins and activation of TGF-beta. Cell Death Differ. 12 (2005) 815-826
    • (2005) Cell Death Differ. , vol.12 , pp. 815-826
    • Solovyan, V.T.1    Keski-Oja, J.2
  • 28
    • 0027427964 scopus 로고
    • The mechanism for the activation of latent TGF-beta during co-culture of endothelial cells and smooth muscle cells: Cell-type specific targeting of latent TGF-beta to smooth muscle cells
    • Sato Y., Okada F., Abe M., Seguchi T., Kuwano M., Sato S., Furuya A., Hanai N., and Tamaoki T. The mechanism for the activation of latent TGF-beta during co-culture of endothelial cells and smooth muscle cells: Cell-type specific targeting of latent TGF-beta to smooth muscle cells. J. Cell Biol. 123 (1993) 1249-1254
    • (1993) J. Cell Biol. , vol.123 , pp. 1249-1254
    • Sato, Y.1    Okada, F.2    Abe, M.3    Seguchi, T.4    Kuwano, M.5    Sato, S.6    Furuya, A.7    Hanai, N.8    Tamaoki, T.9
  • 29
    • 33749538647 scopus 로고    scopus 로고
    • BMP1 controls TGFbeta1 activation via cleavage of latent TGFbeta-binding protein
    • Ge G., and Greenspan D.S. BMP1 controls TGFbeta1 activation via cleavage of latent TGFbeta-binding protein. J. Cell Biol. 175 (2006) 111-120
    • (2006) J. Cell Biol. , vol.175 , pp. 111-120
    • Ge, G.1    Greenspan, D.S.2
  • 30
    • 0032493659 scopus 로고    scopus 로고
    • Recombinant latent transforming growth factor beta-binding protein 2 assembles to fibroblast extracellular matrix and is susceptible to proteolytic processing and release
    • Hyytiainen M., Taipale J., Heldin C.H., and Keski-Oja J. Recombinant latent transforming growth factor beta-binding protein 2 assembles to fibroblast extracellular matrix and is susceptible to proteolytic processing and release. J. Biol. Chem. 273 (1998) 20669-20676
    • (1998) J. Biol. Chem. , vol.273 , pp. 20669-20676
    • Hyytiainen, M.1    Taipale, J.2    Heldin, C.H.3    Keski-Oja, J.4
  • 31
    • 0030800478 scopus 로고    scopus 로고
    • Interleukin-1 induces major phenotypic changes in human skin microvascular endothelial cells
    • Romero L.I., Zhang D.N., Herron G.S., and Karasek M.A. Interleukin-1 induces major phenotypic changes in human skin microvascular endothelial cells. J. Cell. Physiol. 173 (1997) 84-92
    • (1997) J. Cell. Physiol. , vol.173 , pp. 84-92
    • Romero, L.I.1    Zhang, D.N.2    Herron, G.S.3    Karasek, M.A.4
  • 32
    • 47349110186 scopus 로고    scopus 로고
    • Does transformation of microvascular endothelial cells into myofibroblasts play a key role in the etiology and pathology of fibrotic disease?
    • Karasek M.A. Does transformation of microvascular endothelial cells into myofibroblasts play a key role in the etiology and pathology of fibrotic disease?. Med. Hypotheses (2006)
    • (2006) Med. Hypotheses
    • Karasek, M.A.1
  • 33
    • 0021921463 scopus 로고
    • Human endothelial cell cultures: phenotypic modulation by leukocyte interleukins
    • Montesano R., Orci L., and Vassalli P. Human endothelial cell cultures: phenotypic modulation by leukocyte interleukins. J. Cell. Physiol. 122 (1985) 424-434
    • (1985) J. Cell. Physiol. , vol.122 , pp. 424-434
    • Montesano, R.1    Orci, L.2    Vassalli, P.3
  • 34
    • 0032946918 scopus 로고    scopus 로고
    • Modulation of PECAM-1 (CD31) expression in human endothelial cells: effect of IFNgamma and IL-10
    • Bujan J., Gimeno M.J., Prieto A., Pascual G., Bellon J.M., and Alvarez-Mon M. Modulation of PECAM-1 (CD31) expression in human endothelial cells: effect of IFNgamma and IL-10. J. Vasc. Res. 36 (1999) 106-113
    • (1999) J. Vasc. Res. , vol.36 , pp. 106-113
    • Bujan, J.1    Gimeno, M.J.2    Prieto, A.3    Pascual, G.4    Bellon, J.M.5    Alvarez-Mon, M.6
  • 35
    • 0032540880 scopus 로고    scopus 로고
    • Identification and characterization of a new latent transforming growth factor-beta-binding protein, LTBP-4
    • Saharinen J., Taipale J., Monni O., and Keski-Oja J. Identification and characterization of a new latent transforming growth factor-beta-binding protein, LTBP-4. J. Biol. Chem. 273 (1998) 18459-18469
    • (1998) J. Biol. Chem. , vol.273 , pp. 18459-18469
    • Saharinen, J.1    Taipale, J.2    Monni, O.3    Keski-Oja, J.4
  • 36
    • 0036711805 scopus 로고    scopus 로고
    • Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-beta
    • Penttinen C., Saharinen J., Weikkolainen K., Hyytiainen M., and Keski-Oja J. Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-beta. J. Cell. Sci. 115 (2002) 3457-3468
    • (2002) J. Cell. Sci. , vol.115 , pp. 3457-3468
    • Penttinen, C.1    Saharinen, J.2    Weikkolainen, K.3    Hyytiainen, M.4    Keski-Oja, J.5
  • 38
    • 0032440723 scopus 로고    scopus 로고
    • Distinct signal transduction pathways are utilized during the tube formation and survival phases of in vitro angiogenesis
    • Ilan N., Mahooti S., and Madri J.A. Distinct signal transduction pathways are utilized during the tube formation and survival phases of in vitro angiogenesis. J. Cell. Sci. 111 Pt 24 (1998) 3621-3631
    • (1998) J. Cell. Sci. , vol.111 , Issue.PART 24 , pp. 3621-3631
    • Ilan, N.1    Mahooti, S.2    Madri, J.A.3
  • 39
    • 33748990105 scopus 로고    scopus 로고
    • Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis
    • Taylor C.J., Motamed K., and Lilly B. Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis. Angiogenesis 9 (2006) 39-51
    • (2006) Angiogenesis , vol.9 , pp. 39-51
    • Taylor, C.J.1    Motamed, K.2    Lilly, B.3
  • 40
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q., and Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 14 (2000) 163-176
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 41
    • 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. Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate. Eur. J. Biochem. 239 (1996) 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
  • 42
    • 0036301176 scopus 로고    scopus 로고
    • Plasmin activates pro-matrix metalloproteinase-2 with a membrane-type 1 matrix metalloproteinase-dependent mechanism
    • Monea S., Lehti K., Keski-Oja J., and Mignatti P. Plasmin activates pro-matrix metalloproteinase-2 with a membrane-type 1 matrix metalloproteinase-dependent mechanism. J. Cell. Physiol. 192 (2002) 160-170
    • (2002) J. Cell. Physiol. , vol.192 , pp. 160-170
    • Monea, S.1    Lehti, K.2    Keski-Oja, J.3    Mignatti, P.4
  • 43
    • 0036433637 scopus 로고    scopus 로고
    • Notch activation during endothelial cell network formation in vitro targets the basic HLH transcription factor HESR-1 and downregulates VEGFR-2/KDR expression
    • Taylor K.L., Henderson A.M., and Hughes C.C. Notch activation during endothelial cell network formation in vitro targets the basic HLH transcription factor HESR-1 and downregulates VEGFR-2/KDR expression. Microvasc. Res. 64 (2002) 372-383
    • (2002) Microvasc. Res. , vol.64 , pp. 372-383
    • Taylor, K.L.1    Henderson, A.M.2    Hughes, C.C.3
  • 44
    • 0031025031 scopus 로고    scopus 로고
    • Expression of a disintegrin-like protein in cultured human vascular cells and in vivo
    • Herren B., Raines E.W., and Ross R. Expression of a disintegrin-like protein in cultured human vascular cells and in vivo. FASEB J. 11 (1997) 173-180
    • (1997) FASEB J. , vol.11 , pp. 173-180
    • Herren, B.1    Raines, E.W.2    Ross, R.3
  • 46
    • 33344466450 scopus 로고    scopus 로고
    • Making the cut: protease-mediated regulation of angiogenesis
    • Roy R., Zhang B., and Moses M.A. Making the cut: protease-mediated regulation of angiogenesis. Exp. Cell Res. 312 (2006) 608-622
    • (2006) Exp. Cell Res. , vol.312 , pp. 608-622
    • Roy, R.1    Zhang, B.2    Moses, M.A.3
  • 47
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: biological actions and therapeutic opportunities
    • Baker A.H., Edwards D.R., and Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell. Sci. 115 (2002) 3719-3727
    • (2002) J. Cell. Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 49
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis
    • Pepper M.S. Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis. Arterioscler. Thromb. Vasc. Biol. 21 (2001) 1104-1117
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1104-1117
    • Pepper, M.S.1
  • 50
    • 0036906177 scopus 로고    scopus 로고
    • uPAR: a versatile signalling orchestrator
    • Blasi F., and Carmeliet P. uPAR: a versatile signalling orchestrator. Nat. Rev. Mol. Cell Biol. 3 (2002) 932-943
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 52
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • Lee S., Jilani S.M., Nikolova G.V., Carpizo D., and Iruela-Arispe M.L. Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J. Cell Biol. 169 (2005) 681-691
    • (2005) J. Cell Biol. , vol.169 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3    Carpizo, D.4    Iruela-Arispe, M.L.5
  • 53
    • 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., and Keski-Oja J. Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface. Biochem. J. 334 Pt 2 (1998) 345-353
    • (1998) Biochem. J. , vol.334 , Issue.PART 2 , pp. 345-353
    • Lehti, K.1    Lohi, J.2    Valtanen, H.3    Keski-Oja, J.4
  • 54
    • 0018645774 scopus 로고
    • Rapid release of fibronectin from human lung fibroblasts by biologically active phorbol esters
    • Keski-Oja J., Shoyab M., De Larco J.E., and Todaro G.J. Rapid release of fibronectin from human lung fibroblasts by biologically active phorbol esters. Int. J. Cancer. 24 (1979) 218-224
    • (1979) Int. J. Cancer. , vol.24 , pp. 218-224
    • Keski-Oja, J.1    Shoyab, M.2    De Larco, J.E.3    Todaro, G.J.4
  • 57
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • Pei D., and Weiss S.J. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271 (1996) 9135-9140
    • (1996) J. Biol. Chem. , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 58
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion
    • Seiki M. Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. Cancer Lett. 194 (2003) 1-11
    • (2003) Cancer Lett. , vol.194 , pp. 1-11
    • Seiki, M.1
  • 59
    • 0038026913 scopus 로고    scopus 로고
    • Role of pericellular proteolysis by membrane-type 1 matrix metalloproteinase in cancer invasion and angiogenesis
    • Seiki M., Koshikawa N., and Yana I. Role of pericellular proteolysis by membrane-type 1 matrix metalloproteinase in cancer invasion and angiogenesis. Cancer Metastasis Rev. 22 (2003) 129-143
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 129-143
    • Seiki, M.1    Koshikawa, N.2    Yana, I.3
  • 60
    • 0842304200 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase regulates collagen-dependent mitogen-activated protein/extracellular signal-related kinase activation and cell migration
    • Takino T., Miyamori H., Watanabe Y., Yoshioka K., Seiki M., and Sato H. Membrane type 1 matrix metalloproteinase regulates collagen-dependent mitogen-activated protein/extracellular signal-related kinase activation and cell migration. Cancer Res. 64 (2004) 1044-1049
    • (2004) Cancer Res. , vol.64 , pp. 1044-1049
    • Takino, T.1    Miyamori, H.2    Watanabe, Y.3    Yoshioka, K.4    Seiki, M.5    Sato, H.6
  • 62
    • 0037114003 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis
    • Karsdal M.A., Larsen L., Engsig M.T., Lou H., Ferreras M., Lochter A., Delaisse J.M., and Foged N.T. Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J. Biol. Chem. 277 (2002) 44061-44067
    • (2002) J. Biol. Chem. , vol.277 , pp. 44061-44067
    • Karsdal, M.A.1    Larsen, L.2    Engsig, M.T.3    Lou, H.4    Ferreras, M.5    Lochter, A.6    Delaisse, J.M.7    Foged, N.T.8
  • 63
    • 33746602210 scopus 로고    scopus 로고
    • Integrin-mediated transforming growth factor-beta activation regulates homeostasis of the pulmonary epithelial-mesenchymal trophic unit
    • Araya J., Cambier S., Morris A., Finkbeiner W., and Nishimura S.L. Integrin-mediated transforming growth factor-beta activation regulates homeostasis of the pulmonary epithelial-mesenchymal trophic unit. Am. J. Pathol. 169 (2006) 405-415
    • (2006) Am. J. Pathol. , vol.169 , pp. 405-415
    • Araya, J.1    Cambier, S.2    Morris, A.3    Finkbeiner, W.4    Nishimura, S.L.5
  • 65
    • 0032500505 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase/Jun kinase cross-talk underlies vascular endothelial cell growth factor-induced endothelial cell proliferation
    • Pedram A., Razandi M., and Levin E.R. Extracellular signal-regulated protein kinase/Jun kinase cross-talk underlies vascular endothelial cell growth factor-induced endothelial cell proliferation. J. Biol. Chem. 273 (1998) 26722-26728
    • (1998) J. Biol. Chem. , vol.273 , pp. 26722-26728
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 66
    • 0141629668 scopus 로고    scopus 로고
    • Role of ephrin B2 in human retinal endothelial cell proliferation and migration
    • Steinle J.J., Meininger C.J., Chowdhury U., Wu G., and Granger H.J. Role of ephrin B2 in human retinal endothelial cell proliferation and migration. Cell. Signal. 15 (2003) 1011-1017
    • (2003) Cell. Signal. , vol.15 , pp. 1011-1017
    • Steinle, J.J.1    Meininger, C.J.2    Chowdhury, U.3    Wu, G.4    Granger, H.J.5
  • 67
    • 0036479137 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate inhibits death receptor-mediated apoptosis in Jurkat cells by disrupting recruitment of fas-associated polypeptide with death domain
    • Meng X.W., Heldebrant M.P., and Kaufmann S.H. Phorbol 12-myristate 13-acetate inhibits death receptor-mediated apoptosis in Jurkat cells by disrupting recruitment of fas-associated polypeptide with death domain. J. Biol. Chem. 277 (2002) 3776-3783
    • (2002) J. Biol. Chem. , vol.277 , pp. 3776-3783
    • Meng, X.W.1    Heldebrant, M.P.2    Kaufmann, S.H.3


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