메뉴 건너뛰기




Volumn 1, Issue 8, 2003, Pages 561-568

Amyloid endostatin induces endothelial cell detachment by stimulation of the plasminogen activation system

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CARBOXYPEPTIDASE B; COLLAGEN; COLLAGEN TYPE 18; ENDOSTATIN; LYSINE; PLASMIN; PLASMINOGEN; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 0037777699     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (41)

References (72)
  • 1
    • 0031469819 scopus 로고    scopus 로고
    • Antiangiogenic therapy of experimental cancer does not induce acquired drug resistance
    • Boehm, T., Folkman, J., Browder, T., and O'Reilly, M. S. Antiangiogenic therapy of experimental cancer does not induce acquired drug resistance. Nature, 390: 404-407, 1997.
    • (1997) Nature , vol.390 , pp. 404-407
    • Boehm, T.1    Folkman, J.2    Browder, T.3    O'Reilly, M.S.4
  • 2
    • 0033371860 scopus 로고    scopus 로고
    • Reality testing in cancer treatment: The phase I trial of endostatin
    • Ryan, D. P., Penson, R. T., Ahmed, S., Chabner, B. A., and Lynch, T. J., Jr. Reality testing in cancer treatment: the phase I trial of endostatin. Oncologist, 4: 501-508, 1999.
    • (1999) Oncologist , vol.4 , pp. 501-508
    • Ryan, D.P.1    Penson, R.T.2    Ahmed, S.3    Chabner, B.A.4    Lynch T.J., Jr.5
  • 4
  • 7
    • 0034528855 scopus 로고    scopus 로고
    • Angiostatin and endostatin: Endogenous inhibitors of tumor growth
    • Sim, B. K., MacDonald, N. J., and Gubish, E. R. Angiostatin and endostatin: endogenous inhibitors of tumor growth. Cancer Metastasis Rev., 19: 181-190, 2000.
    • (2000) Cancer Metastasis Rev. , vol.19 , pp. 181-190
    • Sim, B.K.1    MacDonald, N.J.2    Gubish, E.R.3
  • 9
    • 0034074561 scopus 로고    scopus 로고
    • Antitumor activity of endostatin against carcinogen-induced rat primary mammary tumors
    • Perletti, G., Concari, P., Giardini, R., Marras, E., Piccinini, F., Folkman, J., and Chen, L. Antitumor activity of endostatin against carcinogen-induced rat primary mammary tumors. Cancer Res., 60: 1793-1796, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 1793-1796
    • Perletti, G.1    Concari, P.2    Giardini, R.3    Marras, E.4    Piccinini, F.5    Folkman, J.6    Chen, L.7
  • 10
    • 0033565645 scopus 로고    scopus 로고
    • Liposomes complexed to plasmids encoding angiostatin and endostatin inhibit breast cancer in nude mice
    • Chen, Q. R., Kumar, D., Stass, S. A., and Mixson, A. J. Liposomes complexed to plasmids encoding angiostatin and endostatin inhibit breast cancer in nude mice. Cancer Res., 59: 3308-3312, 1999.
    • (1999) Cancer Res. , vol.59 , pp. 3308-3312
    • Chen, Q.R.1    Kumar, D.2    Stass, S.A.3    Mixson, A.J.4
  • 11
    • 0034654555 scopus 로고    scopus 로고
    • Antiangiogenic gene therapy of cancer utilizing a recombinant adenovirus to elevate systemic endostatin levels in mice
    • Feldman, A. L., Restifo, N. P., Alexander, H. R., Bartlett, D. L., Hwu, P., Seth, P., and Libutti, S. K. Antiangiogenic gene therapy of cancer utilizing a recombinant adenovirus to elevate systemic endostatin levels in mice. Cancer Res., 60: 1503-1506, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 1503-1506
    • Feldman, A.L.1    Restifo, N.P.2    Alexander, H.R.3    Bartlett, D.L.4    Hwu, P.5    Seth, P.6    Libutti, S.K.7
  • 12
    • 0036228636 scopus 로고    scopus 로고
    • Can "negative" be positive?
    • Steele, F. R. Can "negative" be positive? Mol. Ther., 5: 338-339, 2002.
    • (2002) Mol. Ther. , vol.5 , pp. 338-339
    • Steele, F.R.1
  • 13
    • 0036222328 scopus 로고    scopus 로고
    • Unfulfilled promise of endostatin in a gene therapy-xenotransplant model of human acute lymphocytic leukemia
    • Eisterer, W., Jiang, X., Bachelot, T., Pawliuk, R., Abramovich, C., Leboulch, P., Hogge, D., and Eaves, C. Unfulfilled promise of endostatin in a gene therapy-xenotransplant model of human acute lymphocytic leukemia. Mol. Ther., 5: 352-359, 2002.
    • (2002) Mol. Ther. , vol.5 , pp. 352-359
    • Eisterer, W.1    Jiang, X.2    Bachelot, T.3    Pawliuk, R.4    Abramovich, C.5    Leboulch, P.6    Hogge, D.7    Eaves, C.8
  • 14
    • 0036222277 scopus 로고    scopus 로고
    • Continuous intravascular secretion of endostatin in mice from transduced hematopoietic stem cells
    • Pawliuk, R., Bachelot, T., Zurkiya, O., Eriksson, A., Cao, Y., and Leboulch, P. Continuous intravascular secretion of endostatin in mice from transduced hematopoietic stem cells. Mol. Ther., 5: 345-351, 2002.
    • (2002) Mol. Ther. , vol.5 , pp. 345-351
    • Pawliuk, R.1    Bachelot, T.2    Zurkiya, O.3    Eriksson, A.4    Cao, Y.5    Leboulch, P.6
  • 16
    • 0037155610 scopus 로고    scopus 로고
    • Cancer therapy. Setbacks for endostatin
    • Marshall, E. Cancer therapy. Setbacks for endostatin. Science, 295: 2198-2199, 2002.
    • (2002) Science , vol.295 , pp. 2198-2199
    • Marshall, E.1
  • 17
    • 0037008721 scopus 로고    scopus 로고
    • Endostatin blocks vascular endothelial growth factor-mediated signaling via direct interaction with KDR/Flk-1
    • Kim, Y. M., Hwang, S., Kim, Y. M., Pyun, B. J., Kim, T. Y., Lee, S. T., Gho, Y. S., and Kwon, Y. G. Endostatin blocks vascular endothelial growth factor-mediated signaling via direct interaction with KDR/Flk-1. J. Biol. Chem., 277: 27872-27879, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27872-27879
    • Kim, Y.M.1    Hwang, S.2    Kim, Y.M.3    Pyun, B.J.4    Kim, T.Y.5    Lee, S.T.6    Gho, Y.S.7    Kwon, Y.G.8
  • 20
    • 0036242559 scopus 로고    scopus 로고
    • Endostatin inhibits adhesion of endothelial cells to collagen I via α(2)β(1) integrin, a possible cause of prevention of chondrosarcoma growth
    • Furumatsu, T., Yamaguchi, N., Nishida, K., Kawai, A., Kunisada, T., Namba, M., Inoue, H., and Ninomiya, Y. Endostatin inhibits adhesion of endothelial cells to collagen I via α(2)β(1) integrin, a possible cause of prevention of chondrosarcoma growth. J. Biochem. (Tokyo), 131: 619-626, 2002.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 619-626
    • Furumatsu, T.1    Yamaguchi, N.2    Nishida, K.3    Kawai, A.4    Kunisada, T.5    Namba, M.6    Inoue, H.7    Ninomiya, Y.8
  • 22
    • 0034307327 scopus 로고    scopus 로고
    • Endostatin inhibits endotheliat and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase
    • Kim, Y. M., Jang, J. W., Lee, O. H., Yeon, J., Choi, E. Y., Kim, K. W., Lee, S. T., and Kwon, Y. G. Endostatin inhibits endotheliat and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase. Cancer Res., 60: 5410-5413, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 5410-5413
    • Kim, Y.M.1    Jang, J.W.2    Lee, O.H.3    Yeon, J.4    Choi, E.Y.5    Kim, K.W.6    Lee, S.T.7    Kwon, Y.G.8
  • 23
    • 0037157106 scopus 로고    scopus 로고
    • Endostatin binds to the catalytic domain of matrix metalloproteinase-2
    • Lee, S. J., Jang, J. W., Kim, Y. M., Lee, H. I., Jeon, J. Y., Kwon, Y. G., and Lee, S. T. Endostatin binds to the catalytic domain of matrix metalloproteinase-2. FEBS Lett., 519: 147-152, 2002.
    • (2002) FEBS Lett. , vol.519 , pp. 147-152
    • Lee, S.J.1    Jang, J.W.2    Kim, Y.M.3    Lee, H.I.4    Jeon, J.Y.5    Kwon, Y.G.6    Lee, S.T.7
  • 24
    • 0035419429 scopus 로고    scopus 로고
    • Endostatin-induced modulation of plasminogen activation with concomitant loss of focal adhesions and actin stress fibers in cultured human endothelial cells
    • Wickstrom, S. A., Veikkola, T., Rehn, M, Pihlajaniemi, T., Alitalo, K., and Keski-Oja, J. Endostatin-induced modulation of plasminogen activation with concomitant loss of focal adhesions and actin stress fibers in cultured human endothelial cells. Cancer Res., 61: 6511-6516, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 6511-6516
    • Wickstrom, S.A.1    Veikkola, T.2    Rehn, M.3    Pihlajaniemi, T.4    Alitalo, K.5    Keski-Oja, J.6
  • 25
    • 0032536859 scopus 로고    scopus 로고
    • Crystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolution
    • Hohenester, E., Sasaki, T., Olsen, B. R., and Timpl, R. Crystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolution. EMBO J., 17: 1656-1664, 1998.
    • (1998) EMBO J. , vol.17 , pp. 1656-1664
    • Hohenester, E.1    Sasaki, T.2    Olsen, B.R.3    Timpl, R.4
  • 28
    • 0037468686 scopus 로고    scopus 로고
    • Recombinant endostatin forms amyloid fibrils that bind and are cytotoxic to murine neuroblastoma cells in vitro
    • Kranenburg, O., Kroon-Batenburg, L. M., Reijerkerk, A., Wu, Y. P., Voest, E. E., and Gebbink, M. F. Recombinant endostatin forms amyloid fibrils that bind and are cytotoxic to murine neuroblastoma cells in vitro. FEBS Lett., 539: 149-155, 2003.
    • (2003) FEBS Lett. , vol.539 , pp. 149-155
    • Kranenburg, O.1    Kroon-Batenburg, L.M.2    Reijerkerk, A.3    Wu, Y.P.4    Voest, E.E.5    Gebbink, M.F.6
  • 29
    • 0025718644 scopus 로고
    • Characterization of the binding of plasminogen to fibrin surfaces: The role of carboxy-terminal lysines
    • Fleury, V. and Angles-Cano, E. Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. Biochemistry, 30: 7630-7638, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7630-7638
    • Fleury, V.1    Angles-Cano, E.2
  • 30
    • 0027076351 scopus 로고
    • Fibrinogen degradation product fragment D induces endothelial cell detachment by activation of cell-mediated fibrinolysis
    • Ge, M., Tang, G., Ryan, T. J., and Malik, A. B. Fibrinogen degradation product fragment D induces endothelial cell detachment by activation of cell-mediated fibrinolysis. J. Clin. Invest., 90: 2508-2516, 1992.
    • (1992) J. Clin. Invest. , vol.90 , pp. 2508-2516
    • Ge, M.1    Tang, G.2    Ryan, T.J.3    Malik, A.B.4
  • 31
    • 0028982346 scopus 로고
    • Plasmin abrogates α v β 5-mediated adhesion of a human keratinocyte cell line (HaCaT) to vitronectin
    • Reinartz, J., Schafer, B., Batrla, R., Klein, C. E., and Kramer, M. D. Plasmin abrogates α v β 5-mediated adhesion of a human keratinocyte cell line (HaCaT) to vitronectin. Exp. Cell Res., 220: 274-282, 1995.
    • (1995) Exp. Cell Res. , vol.220 , pp. 274-282
    • Reinartz, J.1    Schafer, B.2    Batrla, R.3    Klein, C.E.4    Kramer, M.D.5
  • 32
    • 0028204301 scopus 로고
    • Plasmin modulators, aprotinin and anti-catalytic plasmin antibody, efficiently inhibit destruction of bovine vascular endothelial cells by choriocarcinoma cells
    • Sugimura, M., Kobayashi, H., and Terao, T. Plasmin modulators, aprotinin and anti-catalytic plasmin antibody, efficiently inhibit destruction of bovine vascular endothelial cells by choriocarcinoma cells. Gynecol. Oncol., 52: 337-346, 1994.
    • (1994) Gynecol. Oncol. , vol.52 , pp. 337-346
    • Sugimura, M.1    Kobayashi, H.2    Terao, T.3
  • 33
    • 0035060384 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 and -9 activation by plasmin regulates a novel endothelial cell-mediated mechanism of collagen gel contraction and capillary tube regression in three-dimensional collagen matrices
    • Davis, G. E., Pintar Allen, K. A., Salazar, R., and Maxwell, S. A. Matrix metalloproteinase-1 and -9 activation by plasmin regulates a novel endothelial cell-mediated mechanism of collagen gel contraction and capillary tube regression in three-dimensional collagen matrices. J. Cell Sci., 114: 917-930, 2001.
    • (2001) J. Cell Sci. , vol.114 , pp. 917-930
    • Davis, G.E.1    Pintar Allen, K.A.2    Salazar, R.3    Maxwell, S.A.4
  • 34
    • 0025911764 scopus 로고
    • Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1
    • Chain, D., Kreizman, T., Shapira, H., and Shaltiel, S. Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1. FEBS Lett., 285: 251-256, 1991.
    • (1991) FEBS Lett. , vol.285 , pp. 251-256
    • Chain, D.1    Kreizman, T.2    Shapira, H.3    Shaltiel, S.4
  • 35
    • 0025527558 scopus 로고
    • Plasminogen activators and cancer
    • Duffy, M. J. Plasminogen activators and cancer. Blood Coagul. Fibrinolysis, 1: 681-687, 1990.
    • (1990) Blood Coagul. Fibrinolysis , vol.1 , pp. 681-687
    • Duffy, M.J.1
  • 38
    • 0030469517 scopus 로고    scopus 로고
    • The fibrinolytic system in neoplasia
    • Bell, W. R. The fibrinolytic system in neoplasia. Semin. Thromb. Hemost., 22: 459-478, 1996.
    • (1996) Semin. Thromb. Hemost. , vol.22 , pp. 459-478
    • Bell, W.R.1
  • 39
    • 0033121275 scopus 로고    scopus 로고
    • The role of αv integrins during angiogenesis: Insights into potential mechanisms of action and clinical development
    • Eliceiri, B. P. and Cheresh, D. A. The role of αv integrins during angiogenesis: insights into potential mechanisms of action and clinical development. J. Clin. Invest., 103: 1227-1230, 1999.
    • (1999) J. Clin. Invest. , vol.103 , pp. 1227-1230
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 41
    • 0028268212 scopus 로고
    • Requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-β to TGF-β
    • Odekon, L. E., Blasi, F., and Rifkin, D. B. Requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-β to TGF-β. J. Cell. Physiol., 158: 398-407, 1994.
    • (1994) J. Cell. Physiol. , vol.158 , pp. 398-407
    • Odekon, L.E.1    Blasi, F.2    Rifkin, D.B.3
  • 43
    • 0032524046 scopus 로고    scopus 로고
    • Expression of urokinase-type plasminogen activator (u-PA), u-PA receptor, and tissue-type PA messenger RNAs in human hepatocellular carcinoma
    • De Petro, G., Tavian, D., Copeta, A., Portolani, N., Giulini, S. M., and Barlati, S. Expression of urokinase-type plasminogen activator (u-PA), u-PA receptor, and tissue-type PA messenger RNAs in human hepatocellular carcinoma. Cancer Res., 58: 2234-2239, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 2234-2239
    • De Petro, G.1    Tavian, D.2    Copeta, A.3    Portolani, N.4    Giulini, S.M.5    Barlati, S.6
  • 45
    • 1842294627 scopus 로고    scopus 로고
    • Expression of plasminogen activators and plasminogen activator inhibitor 1 in dedifferentiated chondrosarcoma
    • Hackel, C., Czerniak, B., Ayala, A. G., Radig, K., and Roessner, A. Expression of plasminogen activators and plasminogen activator inhibitor 1 in dedifferentiated chondrosarcoma. Cancer, 79: 53-58, 1997.
    • (1997) Cancer , vol.79 , pp. 53-58
    • Hackel, C.1    Czerniak, B.2    Ayala, A.G.3    Radig, K.4    Roessner, A.5
  • 46
    • 0027234087 scopus 로고
    • Immunohistochemical study of tumor cell-associated plasminogen activators and plasminogen activator inhibitors in lung carcinomas
    • Gris, J. C., Schved, J. F., Marty-Double, C., Mauboussin, J. M., and Balmes, P. Immunohistochemical study of tumor cell-associated plasminogen activators and plasminogen activator inhibitors in lung carcinomas. Chest, 104: 8-13, 1993.
    • (1993) Chest , vol.104 , pp. 8-13
    • Gris, J.C.1    Schved, J.F.2    Marty-Double, C.3    Mauboussin, J.M.4    Balmes, P.5
  • 47
    • 0026450652 scopus 로고
    • Tissue-type plasminogen activator is involved in skeletal metastasis from human breast cancer
    • Yamashita, J., Inada, K., Yamashita, S., Nakashima, Y., Matsuo, S., and Ogawa, M. Tissue-type plasminogen activator is involved in skeletal metastasis from human breast cancer. Int. J. Clin. Lab. Res., 21: 227-230, 1992.
    • (1992) Int. J. Clin. Lab. Res. , vol.21 , pp. 227-230
    • Yamashita, J.1    Inada, K.2    Yamashita, S.3    Nakashima, Y.4    Matsuo, S.5    Ogawa, M.6
  • 48
    • 0026321129 scopus 로고
    • Vascular endothelial growth factor (VEGF) induces plasminogen activators and plasminogen activator inhibitor-1 in microvascular endothelial cells
    • Pepper, M. S., Ferrara, N., Orci, L., and Montesano, R. Vascular endothelial growth factor (VEGF) induces plasminogen activators and plasminogen activator inhibitor-1 in microvascular endothelial cells. Biochem. Biophys. Res. Commun., 181: 902-906, 1991.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 902-906
    • Pepper, M.S.1    Ferrara, N.2    Orci, L.3    Montesano, R.4
  • 50
    • 0033578910 scopus 로고    scopus 로고
    • Antiangiogenic activity of the cleaved conformation of the serpin antithrombin
    • O'Reilly, M. S., Pirie-Shepherd, S., Lane, W. S., and Folkman, J. Antiangiogenic activity of the cleaved conformation of the serpin antithrombin. Science, 285: 1926-1928, 1999.
    • (1999) Science , vol.285 , pp. 1926-1928
    • O'Reilly, M.S.1    Pirie-Shepherd, S.2    Lane, W.S.3    Folkman, J.4
  • 51
    • 0031571604 scopus 로고    scopus 로고
    • Denatured proteins as cofactors for plasminogen activation
    • Machovich, R. and Owen, W. G. Denatured proteins as cofactors for plasminogen activation. Arch. Biochem. Biophys., 344: 343-349, 1997.
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 343-349
    • Machovich, R.1    Owen, W.G.2
  • 52
    • 0032545037 scopus 로고    scopus 로고
    • Human prothrombin fragment 1 and 2 inhibit bFGF-induced BCE cell growth
    • Rhim, T. Y., Park, C. S., Kim, E., and Kim, S. S. Human prothrombin fragment 1 and 2 inhibit bFGF-induced BCE cell growth. Biochem. Biophys. Res. Commun., 252: 513-516, 1998.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 513-516
    • Rhim, T.Y.1    Park, C.S.2    Kim, E.3    Kim, S.S.4
  • 53
    • 0033564868 scopus 로고    scopus 로고
    • Facilitation of plasminogen activation by denatured prothrombin
    • Machovich, R., Komorowicz, E., Kolev, K., and Owen, W. G. Facilitation of plasminogen activation by denatured prothrombin. Thromb. Res., 94: 389-394, 1999.
    • (1999) Thromb. Res. , vol.94 , pp. 389-394
    • Machovich, R.1    Komorowicz, E.2    Kolev, K.3    Owen, W.G.4
  • 54
    • 0032568607 scopus 로고    scopus 로고
    • A human fibrosarcoma inhibits systemic angiogenesis and the growth of experimental metastases via thrombospondin-1
    • Volpert, O. V., Lawler, J., and Bouck, N. P. A human fibrosarcoma inhibits systemic angiogenesis and the growth of experimental metastases via thrombospondin-1. Proc. Natl. Acad. Sci. USA, 95: 6343-6348, 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6343-6348
    • Volpert, O.V.1    Lawler, J.2    Bouck, N.P.3
  • 55
    • 0021721455 scopus 로고
    • Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator
    • Silverstein, R. L., Leung, L. L., Harpel, P. C., and Nachman, R. L. Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator. J. Clin. Invest., 74: 1625-1633, 1984.
    • (1984) J. Clin. Invest. , vol.74 , pp. 1625-1633
    • Silverstein, R.L.1    Leung, L.L.2    Harpel, P.C.3    Nachman, R.L.4
  • 56
    • 0022376430 scopus 로고
    • Activation of immobilized plasminogen by tissue activator. Multimolecular complex formation
    • Silverstein, R. L., Nachman, R. L., Leung, L. L., and Harpel, P. C. Activation of immobilized plasminogen by tissue activator. Multimolecular complex formation. J. Biol. Chem., 260: 10346-10352, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10346-10352
    • Silverstein, R.L.1    Nachman, R.L.2    Leung, L.L.3    Harpel, P.C.4
  • 57
    • 0023028858 scopus 로고
    • Tissue plasminogen activator and urokinase enhance the binding of plasminogen to thrombospondin
    • Silverstein, R. L., Harpel, P. C., and Nachman, R. L. Tissue plasminogen activator and urokinase enhance the binding of plasminogen to thrombospondin. J. Biol. Chem., 261: 9959-9965, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9959-9965
    • Silverstein, R.L.1    Harpel, P.C.2    Nachman, R.L.3
  • 60
    • 0037102393 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products-binding COOH-terminal motif of Amphoterin inhibits invasive migration and metastasis
    • Huttunen, H. J., Fages, C., Kuja-Panula, J., Ridley, A. J., and Rauvala, H. Receptor for advanced glycation end products-binding COOH-terminal motif of Amphoterin inhibits invasive migration and metastasis. Cancer Res., 62: 4805-4811, 2002.
    • (2002) Cancer Res. , vol.62 , pp. 4805-4811
    • Huttunen, H.J.1    Fages, C.2    Kuja-Panula, J.3    Ridley, A.J.4    Rauvala, H.5
  • 61
    • 0026080007 scopus 로고
    • Interactions of plasminogen and tissue plasminogen activator (t-PA) with amphoterin. Enhancement of t-PA-catalyzed plasminogen activation by amphoterin
    • Parkkinen, J. and Rauvala, H. Interactions of plasminogen and tissue plasminogen activator (t-PA) with amphoterin. Enhancement of t-PA-catalyzed plasminogen activation by amphoterin. J. Biol. Chem., 266: 16730-16735, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16730-16735
    • Parkkinen, J.1    Rauvala, H.2
  • 63
    • 0030916215 scopus 로고    scopus 로고
    • A sensitive and robust assay for urokinase and tissuetype plasminogen activators (uPA and tPA) and their inhibitor type I (PAI-1) in breast tumor cytosols
    • Grebenschikov, N., Geurts-Moespot, A., De Witte, H., Heuvel, J., Leake, R., Sweep, F., and Benraad, T. A sensitive and robust assay for urokinase and tissuetype plasminogen activators (uPA and tPA) and their inhibitor type I (PAI-1) in breast tumor cytosols. Int. J. Biol. Markers, 12: 6-14, 1997.
    • (1997) Int. J. Biol. Markers , vol.12 , pp. 6-14
    • Grebenschikov, N.1    Geurts-Moespot, A.2    De Witte, H.3    Heuvel, J.4    Leake, R.5    Sweep, F.6    Benraad, T.7
  • 64
    • 2642705008 scopus 로고    scopus 로고
    • Prognostic impact of urokinase-type plasminogen activator (PA), PA inhibitor type-1, and tissue-type PA antigen levels in node-negative breast cancer: A prospective study on multicenter basis
    • Kim, S. J., Shiba, E., Kobayashi, T., Yayoi, E., Furukawa, J., Takatsuka, Y., Shin, E., Koyama, H., Inaji, H., and Takai, S. Prognostic impact of urokinase-type plasminogen activator (PA), PA inhibitor type-1, and tissue-type PA antigen levels in node-negative breast cancer: a prospective study on multicenter basis. Clin. Cancer Res., 4: 177-182, 1998.
    • (1998) Clin. Cancer Res. , vol.4 , pp. 177-182
    • Kim, S.J.1    Shiba, E.2    Kobayashi, T.3    Yayoi, E.4    Furukawa, J.5    Takatsuka, Y.6    Shin, E.7    Koyama, H.8    Inaji, H.9    Takai, S.10
  • 65
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar, L., Manuel, R., and Nesheim, M. E. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J. Biol. Chem., 270: 14477-14484, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 66
    • 0034711272 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor attenuates (DD)E-mediated stimulation of plasminogen activation by reducing the affinity of (DD)E for tissue plasminogen activator. A potential mechanism for enhancing the fibrin specificity of tissue plasminogen activator
    • Stewart, R. J., Fredenburgh, J. C., Rischke, J. A., Bajzar, L., and Weitz, J. I. Thrombin-activable fibrinolysis inhibitor attenuates (DD)E-mediated stimulation of plasminogen activation by reducing the affinity of (DD)E for tissue plasminogen activator. A potential mechanism for enhancing the fibrin specificity of tissue plasminogen activator. J. Biol. Chem., 275: 36612-36620, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36612-36620
    • Stewart, R.J.1    Fredenburgh, J.C.2    Rischke, J.A.3    Bajzar, L.4    Weitz, J.I.5
  • 70
  • 71
    • 0033852790 scopus 로고    scopus 로고
    • No grip, no growth: The conceptual basis of excessive proteolysis in the treatment of cancer
    • Reijerkerk, A., Voest, E. E., and Gebbink, M. F. No grip, no growth: the conceptual basis of excessive proteolysis in the treatment of cancer. Eur. J. Cancer, 36: 1695-1705, 2000.
    • (2000) Eur. J. Cancer , vol.36 , pp. 1695-1705
    • Reijerkerk, A.1    Voest, E.E.2    Gebbink, M.F.3
  • 72
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • Deutsch, D. G. and Mertz, E. T. Plasminogen: purification from human plasma by affinity chromatography. Science, 170: 1095-1096, 1970.
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.