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Volumn 50, Issue 15, 1990, Pages 4676-4684

Inhibition of Cancer Cell Urokinase Plasminogen Activator by Its Specific Inhibitor PAI-2 and Subsequent Effects on Extracellular Matrix Degradation

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR INHIBITOR 2; RADIOISOTOPE;

EID: 0025354463     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (116)

References (70)
  • 1
    • 0021045628 scopus 로고
    • Antibodies to plasminogen activator inhibit human tumor metastasis
    • Ossowski, L., and Reich, E. Antibodies to plasminogen activator inhibit human tumor metastasis. Cell, 35:611–619, 1983.
    • (1983) Cell , vol.35 , pp. 611-619
    • Ossowski, L.1    Reich, E.2
  • 2
    • 0021803789 scopus 로고
    • Localization of plasminogen activators in human colon cancer by immunoperoxidase staining
    • Kohga, S., Harvey, S. R., Weaver, R. M., and Markus, G. Localization of plasminogen activators in human colon cancer by immunoperoxidase staining. Cancer Res., 45:1787–1796, 1985.
    • (1985) Cancer Res. , vol.45 , pp. 1787-1796
    • Kohga, S.1    Harvey, S.R.2    Weaver, R.M.3    Markus, G.4
  • 3
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade
    • Mignatti, P., Robbins, E., and Rifkin, D. B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell, 47: 487–498, 1986.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 4
    • 0024238269 scopus 로고
    • In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase
    • Ossowski, L. In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase. J. Cell Biol., 107:2437–2445, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2437-2445
    • Ossowski, L.1
  • 5
    • 0023853553 scopus 로고
    • Plasminogen activator dependent pathways in dissemination of human tumor cells in the chick embryo
    • Ossowski, L. Plasminogen activator dependent pathways in dissemination of human tumor cells in the chick embryo. Cell, 52: 321–328, 1988.
    • (1988) Cell , vol.52 , pp. 321-328
    • Ossowski, L.1
  • 6
    • 0023836852 scopus 로고
    • Modulation of metastatic potential by cell surface urokinase of murine melanoma cells
    • Hearing, V. J., Law, L. W., Corti, A., Appella, E., and Blasi, F. Modulation of metastatic potential by cell surface urokinase of murine melanoma cells. Cancer Res., 48:1270–1278, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 1270-1278
    • Hearing, V.J.1    Law, L.W.2    Corti, A.3    Appella, E.4    Blasi, F.5
  • 7
    • 0023919232 scopus 로고
    • Effects of inhibitors of plasminogen activator, serine proteinases, and collagenase IV on the invasion of basement membranes by metastatic cells
    • Reich, R., Thompson, E. W., Iwamoto, Y., Martin, G. R., Deason, J. R., Fuller, G. C., and Miskin, R. Effects of inhibitors of plasminogen activator, serine proteinases, and collagenase IV on the invasion of basement membranes by metastatic cells. Cancer Res., 48:3307–3312, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 3307-3312
    • Reich, R.1    Thompson, E.W.2    Iwamoto, Y.3    Martin, G.R.4    Deason, J.R.5    Fuller, G.C.6    Miskin, R.7
  • 9
    • 0024539580 scopus 로고
    • Induction of urokinase activity and malignant phenotype in bladder carcinoma cells after transfection of the activated Ha-ras oncogene
    • Brunner, G., Pohl, J., Erkell, L. J., Radler-Pohl, A., and Schirrmacher, V. Induction of urokinase activity and malignant phenotype in bladder carcinoma cells after transfection of the activated Ha-ras oncogene. J. Cancer Res. Clin. Oncol., 115: 139–144, 1989.
    • (1989) J. Cancer Res. Clin. Oncol. , vol.115 , pp. 139-144
    • Brunner, G.1    Pohl, J.2    Erkell, L.J.3    Radler-Pohl, A.4    Schirrmacher, V.5
  • 10
    • 0023796586 scopus 로고
    • Urokinase-type plasminogen activator in colorectal carcinomas and adenomatous polyps: quantitative expression of active and proenzyme
    • Sim, P. S., Stephens, R. W., Fayle, D. R., and Doe, W. F. Urokinase-type plasminogen activator in colorectal carcinomas and adenomatous polyps: quantitative expression of active and proenzyme. Int. J. Cancer, 42: 483–488, 1988.
    • (1988) Int. J. Cancer , vol.42 , pp. 483-488
    • Sim, P.S.1    Stephens, R.W.2    Fayle, D.R.3    Doe, W.F.4
  • 11
    • 0024603151 scopus 로고
    • Inhibition by retinoic acid of type IV colla-genolysis and invasion through reconstituted basement membrane by metastatic rat mammary adenocarcinoma cells
    • Nakajima, M., Lotan, D., Baig, M. M., Carralero, R. M., Wood, W. R., Hendrix, M. J., and Lotan, R. Inhibition by retinoic acid of type IV colla-genolysis and invasion through reconstituted basement membrane by metastatic rat mammary adenocarcinoma cells. Cancer Res., 49: 1698–1706, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 1698-1706
    • Nakajima, M.1    Lotan, D.2    Baig, M.M.3    Carralero, R.M.4    Wood, W.R.5    Hendrix, M.J.6    Lotan, R.7
  • 12
    • 0024355284 scopus 로고
    • Mechanisms of cellular invasiveness: a comparison of amnion invasion in vitro and metastatic behavior in vivo
    • Yagel, S., Khokha, R., Denhardt, D. T., Kerbel, R. S., Parhar, R. S., and Lala, P. K. Mechanisms of cellular invasiveness: a comparison of amnion invasion in vitro and metastatic behavior in vivo. J. Natl. Cancer Inst., 81: 768–775, 1989.
    • (1989) J. Natl. Cancer Inst. , vol.81 , pp. 768-775
    • Yagel, S.1    Khokha, R.2    Denhardt, D.T.3    Kerbel, R.S.4    Parhar, R.S.5    Lala, P.K.6
  • 13
    • 0014216684 scopus 로고
    • The peptide chains of human plasmin: mechanism of activation of human plasminogen to plasmin
    • Robbins, K. C., Summaria, L., Hsieh, B., and Shah, R. J. The peptide chains of human plasmin: mechanism of activation of human plasminogen to plasmin. J. Biol. Chem., 242: 2333–2342, 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2333-2342
    • Robbins, K.C.1    Summaria, L.2    Hsieh, B.3    Shah, R.J.4
  • 14
    • 0019850184 scopus 로고
    • Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane
    • Liotta, L. A., Goldfarb, R. H., Brundage, R., Siegal, G. P., Terranova, V., and Garbisa, S. Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane. Cancer Res., 41:4629–4636, 1981.
    • (1981) Cancer Res. , vol.41 , pp. 4629-4636
    • Liotta, L.A.1    Goldfarb, R.H.2    Brundage, R.3    Siegal, G.P.4    Terranova, V.5    Garbisa, S.6
  • 15
    • 0023002645 scopus 로고
    • Degradation of glycoprotein and collagenous components of the basement membrane: studies with urokinase-type plasminogen activator, α-thrombin, and plasmin
    • Goldfarb, R. H., Murano, G., Brundage, R., Siegal, G. P., Terranova, V., Garbisa, S., and Liotta, L. A. Degradation of glycoprotein and collagenous components of the basement membrane: studies with urokinase-type plasminogen activator, α-thrombin, and plasmin. Semin. Thromb. Hemostasis, 12: 335–336, 1986.
    • (1986) Semin. Thromb. Hemostasis , vol.12 , pp. 335-336
    • Goldfarb, R.H.1    Murano, G.2    Brundage, R.3    Siegal, G.P.4    Terranova, V.5    Garbisa, S.6    Liotta, L.A.7
  • 16
    • 0020431191 scopus 로고
    • Secretion of basement membrane collagen degrading enzyme and plasminogen activator by transformed cells—role in metastasis
    • Salo, T., Liotta, L. A., Keski-Oja, J., Turpeenniemi-Hujanen, T., and Tryggvason, K. Secretion of basement membrane collagen degrading enzyme and plasminogen activator by transformed cells—role in metastasis. Int. J. Cancer, 30:669–673, 1982.
    • (1982) Int. J. Cancer , vol.30 , pp. 669-673
    • Salo, T.1    Liotta, L.A.2    Keski-Oja, J.3    Turpeenniemi-Hujanen, T.4    Tryggvason, K.5
  • 17
    • 0023034044 scopus 로고
    • The receptor for urokinase-plasminogen activator
    • Blasi, F., Stoppelli, M. P., and Cubellis, M. V. The receptor for urokinase-plasminogen activator. J. Cell. Biochem., 32:179–186, 1986.
    • (1986) J. Cell. Biochem. , vol.32 , pp. 179-186
    • Blasi, F.1    Stoppelli, M.P.2    Cubellis, M.V.3
  • 18
    • 0023840122 scopus 로고
    • A 55,000–60,000 Mr receptor protein for urokinase-type plasminogen activator. Identification in human tumor cell lines and partial purification
    • Nielsen, L. S., Kellerman, G. M., Behrendt, N., Picone, R., Dano, K., and Blasi, F. A 55,000–60,000 Mr receptor protein for urokinase-type plasminogen activator. Identification in human tumor cell lines and partial purification. J. Biol. Chem., 263: 2358–2363, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2358-2363
    • Nielsen, L.S.1    Kellerman, G.M.2    Behrendt, N.3    Picone, R.4    Dano, K.5    Blasi, F.6
  • 19
    • 0022494568 scopus 로고
    • The Mr 17,500 region of the A chain of urokinase is required for interaction with a specific receptor in A431 cells
    • Fibbi, G., Dini, G., Pasquali, F., Pucci, M., and Del Rosso, M. The Mr 17,500 region of the A chain of urokinase is required for interaction with a specific receptor in A431 cells. Biochim. Biophys. Acta, 885:301–308,1986.
    • (1986) Biochim. Biophys. Acta , vol.885 , pp. 301-308
    • Fibbi, G.1    Dini, G.2    Pasquali, F.3    Pucci, M.4    Del Rosso, M.5
  • 20
    • 0023025270 scopus 로고
    • The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type
    • Plow, E. F., Freaney, D. E., Plescia, J., and Miles, L. A. The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. J. Cell Biol., 103:2411–2420, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2411-2420
    • Plow, E.F.1    Freaney, D.E.2    Plescia, J.3    Miles, L.A.4
  • 21
    • 0024597669 scopus 로고
    • Characterization of the cellular binding site for the urokinase-type plasminogen activator
    • Estreicher, A., Wohlwend, A., Belin, D., Schleuning, W. D., and Vassalli, J. D. Characterization of the cellular binding site for the urokinase-type plasminogen activator. J. Biol. Chem., 264:1180–1189, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1180-1189
    • Estreicher, A.1    Wohlwend, A.2    Belin, D.3    Schleuning, W.D.4    Vassalli, J.D.5
  • 23
    • 0023818612 scopus 로고
    • Determination of the levels of urokinase and its receptor in human colon carcinoma cell lines
    • Boyd, D., Florent, G., Kim, P., and Brattain, M. Determination of the levels of urokinase and its receptor in human colon carcinoma cell lines. Cancer Res., 48: 3112–3116, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 3112-3116
    • Boyd, D.1    Florent, G.2    Kim, P.3    Brattain, M.4
  • 24
    • 0021801011 scopus 로고
    • Localization of plasminogen activators) in primary and secondary rat adenocarcinoma cells
    • Ng, R., Wong, A., and Kellen, J. A. Localization of plasminogen activators) in primary and secondary rat adenocarcinoma cells. Clin. Exp. Metastasis, 3: 73, 1985.
    • (1985) Clin. Exp. Metastasis , vol.3 , pp. 73
    • Ng, R.1    Wong, A.2    Kellen, J.A.3
  • 27
    • 0023130521 scopus 로고
    • Plasminogen activator inhibitors
    • Sprengers, E. D., and Kluft, C. Plasminogen activator inhibitors. Blood, 69: 381–387, 1987.
    • (1987) Blood , vol.69 , pp. 381-387
    • Sprengers, E.D.1    Kluft, C.2
  • 28
    • 0023677472 scopus 로고
    • Plasminogen activator inhibitors—a review
    • Kruithof, E. K. O. Plasminogen activator inhibitors—a review. Enzyme, 40: 113–121,1988.
    • (1988) Enzyme , vol.40 , pp. 113-121
    • Kruithof, E.K.O.1
  • 29
    • 0014423662 scopus 로고
    • Urokinase inhibitor in human placenta
    • Kawano, T., Morimoto, K., and Uemura, Y. Urokinase inhibitor in human placenta. Nature (Lond.), 217: 253, 1968.
    • (1968) Nature (Lond.) , vol.217 , pp. 253
    • Kawano, T.1    Morimoto, K.2    Uemura, Y.3
  • 30
    • 0021280323 scopus 로고
    • Differential inhibition of two molecular forms of melanoma cell plasminogen activator by a placental inhibitor
    • Lecander, I., Roblin, R., and Astedt, B. Differential inhibition of two molecular forms of melanoma cell plasminogen activator by a placental inhibitor. Br. J. Haematol., 57:407–412, 1984.
    • (1984) Br. J. Haematol. , vol.57 , pp. 407-412
    • Lecander, I.1    Roblin, R.2    Astedt, B.3
  • 31
    • 0023250615 scopus 로고
    • An inhibitor of plasminogen activator from human placenta
    • Wun, T. C., and Reich, E. An inhibitor of plasminogen activator from human placenta. J. Biol. Chem., 262: 3636–3653, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3636-3653
    • Wun, T.C.1    Reich, E.2
  • 32
    • 0021075737 scopus 로고
    • Minactivin: a human monocyte product which specifically inactivates urokinase-type plasminogen activator
    • Golder, J. P., and Stephens, R. W. Minactivin: a human monocyte product which specifically inactivates urokinase-type plasminogen activator. Eur. J. Biochem., 136: 517–522, 1983.
    • (1983) Eur. J. Biochem. , vol.136 , pp. 517-522
    • Golder, J.P.1    Stephens, R.W.2
  • 33
    • 0021320757 scopus 로고
    • Novel properties of human monocyte plasminogen activator
    • Stephens, R. W., and Golder, J. P. Novel properties of human monocyte plasminogen activator. Eur. J. Biochem., 139: 253–259, 1984.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 253-259
    • Stephens, R.W.1    Golder, J.P.2
  • 34
    • 0023148141 scopus 로고
    • Phorbol ester induces the biosynthesis of glycosylated and nonglycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells
    • Genton, C., Kruithof, E. K. O., and Schleuning, W-D. Phorbol ester induces the biosynthesis of glycosylated and nonglycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells. J. Cell Biol., 104: 705–712, 1987.
    • (1987) J. Cell Biol. , vol.104 , pp. 705-712
    • Genton, C.1    Kruithof, E.K.O.2    Schleuning, W.-D.3
  • 35
    • 0024551332 scopus 로고
    • Structure of the gene for human plasminogen activator inhibitor 2. The nearest mammalian homologue of chicken ovalbumin
    • Ye, R. D., Ahern, S. M., Le Beau, M. M., Lebo, R. V., and Sadler, J. E. Structure of the gene for human plasminogen activator inhibitor 2. The nearest mammalian homologue of chicken ovalbumin. J. Biol. Chem., 264: 5495–5502, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5495-5502
    • Ye, R.D.1    Ahern, S.M.2    Le Beau, M.M.3    Lebo, R.V.4    Sadler, J.E.5
  • 37
    • 0014932863 scopus 로고
    • Plasminogen: purification from human plasma by affinity chromatography
    • Deutsh, D. G., and Mertz, E. T. Plasminogen: purification from human plasma by affinity chromatography. Science (Wash. DC), 170: 1095–1096, 1970.
    • (1970) Science (Wash. DC) , vol.170 , pp. 1095-1096
    • Deutsh, D.G.1    Mertz, E.T.2
  • 38
    • 0016722309 scopus 로고
    • Subclasses of T-cells with different sensitivities to cytotoxic antibody in the presence of anesthetics
    • Lee, S. K., Singh, J., and Taylor, R. B. Subclasses of T-cells with different sensitivities to cytotoxic antibody in the presence of anesthetics. Eur. J. Immunol., 5: 259–262, 1975.
    • (1975) Eur. J. Immunol. , vol.5 , pp. 259-262
    • Lee, S.K.1    Singh, J.2    Taylor, R.B.3
  • 39
    • 0019729459 scopus 로고
    • A sensitive, coupled assay for plasminogen activator using a thiol ester substrate for plasmin
    • Coleman, P. L., and Green, G. D. J. A sensitive, coupled assay for plasminogen activator using a thiol ester substrate for plasmin. Ann. NY Acad. Sci., 570:617–626, 1981.
    • (1981) Ann. NY Acad. Sci. , vol.570 , pp. 617-626
    • Coleman, P.L.1    Green, G.D.J.2
  • 40
    • 0018193854 scopus 로고
    • A study of proteases and protease-inhibitor complexes in biological fluids
    • Granelli-Piperno, A., and Reich, E. A study of proteases and protease-inhibitor complexes in biological fluids. J. Exp. Med., 148: 223–234, 1978.
    • (1978) J. Exp. Med. , vol.148 , pp. 223-234
    • Granelli-Piperno, A.1    Reich, E.2
  • 41
    • 0022976041 scopus 로고
    • Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme
    • Andreasen, P. A., Nielsen, L. S., Kristensen, P., Grandahl-Hansen, J., Skriver, L., and Dano, K. Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme. J. Biol. Chem., 261: 7644–7651, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7644-7651
    • Andreasen, P.A.1    Nielsen, L.S.2    Kristensen, P.3    Grandahl-Hansen, J.4    Skriver, L.5    Dano, K.6
  • 42
    • 0023192040 scopus 로고
    • Poly-L-lysine dependent inactivation of tissue plasminogen activator by a class PAI-2 inhibitor (minactivin)
    • Leung, K.-C., Byatt, J. A., and Stephens, R. W. Poly-L-lysine dependent inactivation of tissue plasminogen activator by a class PAI-2 inhibitor (minactivin). Thromb. Res., 46:161–711, 1987.
    • (1987) Thromb. Res. , vol.46 , pp. 161-711
    • Leung, K.-C.1    Byatt, J.A.2    Stephens, R.W.3
  • 44
    • 0023084641 scopus 로고
    • Proenzyme to urokinase-type plasminogen activator in human colon cancer: in vitro inhibition by monocyte minactivin after proteolytic activation
    • Stephens, R. W., Fordham, C. J., and Doe, W. F. Proenzyme to urokinase-type plasminogen activator in human colon cancer: in vitro inhibition by monocyte minactivin after proteolytic activation. Eur. J. Cancer Clin. Oncol., 25:213–222,1987.
    • (1987) Eur. J. Cancer Clin. Oncol. , vol.25 , pp. 213-222
    • Stephens, R.W.1    Fordham, C.J.2    Doe, W.F.3
  • 45
    • 0024195895 scopus 로고
    • Proteolytic mechanisms operating at the surface of invasive cells
    • Pollanen, J., Stephens, R., Salonen, E. M., and Vaheri, A. Proteolytic mechanisms operating at the surface of invasive cells. Adv. Exp. Med. Biol., 233: 187–199, 1988.
    • (1988) Adv. Exp. Med. Biol. , vol.233 , pp. 187-199
    • Pollanen, J.1    Stephens, R.2    Salonen, E.M.3    Vaheri, A.4
  • 46
    • 0021962767 scopus 로고
    • Role for different cell proteinases in cancer invasion and cytolysis
    • Zucker, S., Beck, G., DiStefano, J. F., and Lysik, R. M. Role for different cell proteinases in cancer invasion and cytolysis. Br. J. Cancer, 52:223–232, 1985.
    • (1985) Br. J. Cancer , vol.52 , pp. 223-232
    • Zucker, S.1    Beck, G.2    DiStefano, J.F.3    Lysik, R.M.4
  • 48
    • 0021728249 scopus 로고
    • Cysteine proteinases and metastasis
    • Sloane, B. F., and Honn, K. V. Cysteine proteinases and metastasis. Cancer Metastasis Rev., 5: 249–263, 1984.
    • (1984) Cancer Metastasis Rev. , vol.5 , pp. 249-263
    • Sloane, B.F.1    Honn, K.V.2
  • 49
    • 0022834341 scopus 로고
    • Collagenase and elastase production by mouse mammary adenocarcinoma primary cultures and cloned cells
    • Zeydel, M., Nakagawa, S., Biempica, L., and Takahashi, S. Collagenase and elastase production by mouse mammary adenocarcinoma primary cultures and cloned cells. Cancer Res., 46:6438–6445, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 6438-6445
    • Zeydel, M.1    Nakagawa, S.2    Biempica, L.3    Takahashi, S.4
  • 50
    • 0022556525 scopus 로고
    • Selective inhibition of proteolytic enzymes in an in vivo mouse model for experimental metastasis
    • Ostrowski, L. E., Ahsan, A., Suthar, B. P., Pagast, P., Bain, D. L., Wong, C., Patel, A., and Schultz, R. M. Selective inhibition of proteolytic enzymes in an in vivo mouse model for experimental metastasis. Cancer Res., 46: 4121–4128, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 4121-4128
    • Ostrowski, L.E.1    Ahsan, A.2    Suthar, B.P.3    Pagast, P.4    Bain, D.L.5    Wong, C.6    Patel, A.7    Schultz, R.M.8
  • 51
    • 0022446125 scopus 로고
    • Inhibition of proteolytic enzymes in the in vitro amnion model for basement membrane invasion
    • Persky, B., Ostrowski, L. E., Pagast, P., Ahsan, A., and Schultz, R. M. Inhibition of proteolytic enzymes in the in vitro amnion model for basement membrane invasion. Cancer Res., 46: 4129–4134, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 4129-4134
    • Persky, B.1    Ostrowski, L.E.2    Pagast, P.3    Ahsan, A.4    Schultz, R.M.5
  • 52
    • 0024348296 scopus 로고
    • Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells
    • Yagel, S., Warner, A. H., Nellans, H. N., Lala, P. K., Waghorne, C., and Denhardt, D. T. Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res., 49: 3553–3557, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 3553-3557
    • Yagel, S.1    Warner, A.H.2    Nellans, H.N.3    Lala, P.K.4    Waghorne, C.5    Denhardt, D.T.6
  • 53
    • 0022967103 scopus 로고
    • Proteolytic enzymes in cancer invasion and metastasis
    • Goldfarb, R. H., and Liotta, L. A. Proteolytic enzymes in cancer invasion and metastasis. Semin. Thromb. Hemostasis, 12:294–307, 1986.
    • (1986) Semin. Thromb. Hemostasis , vol.12 , pp. 294-307
    • Goldfarb, R.H.1    Liotta, L.A.2
  • 54
    • 0021115222 scopus 로고
    • The role of proteinases in cellular invasiveness
    • Mullins, D. E., and Rohrlich, S. T. The role of proteinases in cellular invasiveness. Biochim. Biophys. Acta, 695: 177–214, 1983.
    • (1983) Biochim. Biophys. Acta , vol.695 , pp. 177-214
    • Mullins, D.E.1    Rohrlich, S.T.2
  • 55
    • 0018893682 scopus 로고
    • On the regulation and control of fibrinolysis
    • Collen, D. On the regulation and control of fibrinolysis. Thromb. Haemostasis,45:77, 1980.
    • (1980) Thromb. Haemostasis , vol.45 , pp. 77
    • Collen, D.1
  • 57
    • 0021195598 scopus 로고
    • Laminin interacts with plasminogen and its tissue-type activator
    • Salonen, E.-M., Zitting, A., and Vaheri, A. Laminin interacts with plasminogen and its tissue-type activator. FEBS Lett., 172: 29–32, 1984.
    • (1984) FEBS Lett. , vol.172 , pp. 29-32
    • Salonen, E.-M.1    Zitting, A.2    Vaheri, A.3
  • 58
    • 0022355907 scopus 로고
    • Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin
    • Salonen, E-M., Saksela, O., Vartio, T., Vaheri, A., Nielsen, L. S., and Zeuthen, J. Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin. J. Biol. Chem., 260: 12302–12307, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12302-12307
    • Salonen, E.-M.1    Saksela, O.2    Vartio, T.3    Vaheri, A.4    Nielsen, L.S.5    Zeuthen, J.6
  • 59
    • 0022548950 scopus 로고
    • Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I
    • Bergman, B. L., Scott, R. W., Bajpai, A., Watts, S., and Baker, J. B. Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I. Proc. Natl. Acad. Sei. USA, 83: 996–1000, 1986.
    • (1986) Proc. Natl. Acad. Sei. USA , vol.83 , pp. 996-1000
    • Bergman, B.L.1    Scott, R.W.2    Bajpai, A.3    Watts, S.4    Baker, J.B.5
  • 60
    • 0017106119 scopus 로고
    • Effects of acrosin inhibitor on the soluble and membrane-bound forms of ram acrosin, and a reappraisal of the role of the enzymes in fertilisation
    • Brown, C. R., and Hartree, E. F. Effects of acrosin inhibitor on the soluble and membrane-bound forms of ram acrosin, and a reappraisal of the role of the enzymes in fertilisation. Hoppe-Seyler's Z. Physiol. Chem., 357: 57–65, 1976.
    • (1976) Hoppe-Seyler's Z. Physiol. Chem. , vol.357 , pp. 57-65
    • Brown, C.R.1    Hartree, E.F.2
  • 61
    • 0020065698 scopus 로고
    • Macrophage fibrinolytic activity: Identification of two pathways of plasmin formation by intact cells and of a plasminogen activator inhibitor
    • Chapman, H. A., Varin, Z., and Hibbs, J. B. Macrophage fibrinolytic activity: Identification of two pathways of plasmin formation by intact cells and of a plasminogen activator inhibitor. Cell, 28:653–662, 1982.
    • (1982) Cell , vol.28 , pp. 653-662
    • Chapman, H.A.1    Varin, Z.2    Hibbs, J.B.3
  • 63
    • 0023711754 scopus 로고
    • Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator inhibitor type 1 and type 2
    • Thorsen, S., Philips, M., Selmer, J., Lecander, I., and Astedt, B. Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator inhibitor type 1 and type 2. Eur. J. Biochem., 175: 33–39, 1988.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 33-39
    • Thorsen, S.1    Philips, M.2    Selmer, J.3    Lecander, I.4    Astedt, B.5
  • 64
    • 0021082363 scopus 로고
    • The effects of fibrinogen and its cleavage product on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity
    • Lucas, M. A., Straight, D. L., Fretto, L. J., and McKee, P. A. The effects of fibrinogen and its cleavage product on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity. J. Biol. Chem., 258: 12171–12177, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12171-12177
    • Lucas, M.A.1    Straight, D.L.2    Fretto, L.J.3    McKee, P.A.4
  • 67
    • 0024334327 scopus 로고
    • Urokinase-type plasminogen activator biosynthesis is induced by the EJ-Ha-ras oncogene in CL26 mouse colon carcinoma cells
    • Testa, J. E., Medcalf, R. L., Cajot, J. F., Schleuning, W. D., and Sordat, B. Urokinase-type plasminogen activator biosynthesis is induced by the EJ-Ha-ras oncogene in CL26 mouse colon carcinoma cells. Int. J. Cancer., 43:816–822, 1989.
    • (1989) Int. J. Cancer. , vol.43 , pp. 816-822
    • Testa, J.E.1    Medcalf, R.L.2    Cajot, J.F.3    Schleuning, W.D.4    Sordat, B.5
  • 69
    • 0023109730 scopus 로고
    • Secretion of type IV collagenolytic protease and metastatic phenotype: induction by transfection with c-Ha-ras but not c-Ha-ras plus Ad2-Ela
    • Garbisa, S., Pozzatti, R., Muschel, R. J., Saffiotti, U., Ballin, M., Goldfarb, R. H., Khoury, G., and Liotta, L. A. Secretion of type IV collagenolytic protease and metastatic phenotype: induction by transfection with c-Ha-ras but not c-Ha-ras plus Ad2-Ela. Cancer Res., 47: 1523–1528, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 1523-1528
    • Garbisa, S.1    Pozzatti, R.2    Muschel, R.J.3    Saffiotti, U.4    Ballin, M.5    Goldfarb, R.H.6    Khoury, G.7    Liotta, L.A.8
  • 70
    • 0023869730 scopus 로고
    • Plasminogen activator inhibitor 1 and plasminogen activator inhibitor 2 in various disease states
    • Kruithof, E. K. O., Gudinchet, A., and Bachmann, F. Plasminogen activator inhibitor 1 and plasminogen activator inhibitor 2 in various disease states. Thromb. Haemostasis, 59: 7–12, 1988.
    • (1988) Thromb. Haemostasis , vol.59 , pp. 7-12
    • Kruithof, E.K.O.1    Gudinchet, A.2    Bachmann, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.