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Volumn 64, Issue 1, 2004, Pages 162-168

Cell Surface-Dependent Generation of Angiostatin4.5

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANGIOSTATIN; ANGIOSTATIN 4.5; ANTIBODY; BETA ACTIN; ENOLASE; ISOPROTEIN; LIPOCORTIN 2; MEMBRANE RECEPTOR; PLASMIN; PLASMINOGEN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 1642494842     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-03-1862     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 0026083903 scopus 로고
    • Tumor angiogenesis and metastasis-correlation in invasive breast carcinoma
    • Weidner, N., Semple, J. P., Welch, W. R., and Folkman, J. Tumor angiogenesis and metastasis-correlation in invasive breast carcinoma. N. Engl. J. Med., 324: 1-8, 1991.
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1-8
    • Weidner, N.1    Semple, J.P.2    Welch, W.R.3    Folkman, J.4
  • 4
    • 0017335455 scopus 로고
    • Angiogenesis: A market for neoplastic transformation of mammary papillary hyperplasia
    • Brem, S. S., Gullino, P. M., and Medina, D. Angiogenesis: a market for neoplastic transformation of mammary papillary hyperplasia. Science (Wash. DC), 195: 880-882, 1977.
    • (1977) Science (Wash. DC) , vol.195 , pp. 880-882
    • Brem, S.S.1    Gullino, P.M.2    Medina, D.3
  • 6
    • 0025286753 scopus 로고
    • Tumor interactions with the vasculature: Angiogenesis and tumor metastasis
    • Blood, C. H., and Zetter, B. R. Tumor interactions with the vasculature: angiogenesis and tumor metastasis. Biochim. Biophys. Acta, 1032: 89-118, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1032 , pp. 89-118
    • Blood, C.H.1    Zetter, B.R.2
  • 7
    • 0025141337 scopus 로고
    • What is the evidence that tumors are angiogenesis dependent?
    • Folkman, J. What is the evidence that tumors are angiogenesis dependent? J. Natl. Cancer Inst., 82: 4-6, 1990.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 4-6
    • Folkman, J.1
  • 9
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat. Med., 1: 27-31, 1995.
    • (1995) Nat. Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 10
    • 0029944122 scopus 로고    scopus 로고
    • Angiostatin induces and sustains dormancy of human primary tumors in mice
    • O'Reilly, M. S., Holmgren, L., Chen, C., and Folkman, J. Angiostatin induces and sustains dormancy of human primary tumors in mice. Nat. Med., 2: 689-692, 1996.
    • (1996) Nat. Med. , vol.2 , pp. 689-692
    • O'Reilly, M.S.1    Holmgren, L.2    Chen, C.3    Folkman, J.4
  • 11
    • 0033617532 scopus 로고    scopus 로고
    • Effects of angiogenesis inhibitors on multistage carcinogenesis in mice
    • Bergers, G., Javaherian, K., Lo, K. M., Folkman, J., and Hanahan, D. Effects of angiogenesis inhibitors on multistage carcinogenesis in mice. Science (Wash. DC), 284: 808-812, 1999.
    • (1999) Science (Wash. DC) , vol.284 , pp. 808-812
    • Bergers, G.1    Javaherian, K.2    Lo, K.M.3    Folkman, J.4    Hanahan, D.5
  • 12
    • 0032577571 scopus 로고    scopus 로고
    • Vasculogenesis, angiogenesis, and growth factors: Ephrins enter the fray at the border
    • Yancopoulos, G. D., Klagsbrun, M., and Folkman, J. Vasculogenesis, angiogenesis, and growth factors: ephrins enter the fray at the border. Cell, 93: 661-664, 1998.
    • (1998) Cell , vol.93 , pp. 661-664
    • Yancopoulos, G.D.1    Klagsbrun, M.2    Folkman, J.3
  • 13
    • 0025147371 scopus 로고
    • A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin
    • Good, D. J., Polverini, P. J., Rastinejad, F., Le Beau, M. M., Lemons, R. S., Frazier, W. A., and Bouck, N. P. A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistinguishable from a fragment of thrombospondin. Proc. Natl. Acad. Sci. USA., 87: 6624-6628, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6624-6628
    • Good, D.J.1    Polverini, P.J.2    Rastinejad, F.3    Le Beau, M.M.4    Lemons, R.S.5    Frazier, W.A.6    Bouck, N.P.7
  • 14
    • 0029128416 scopus 로고
    • The modulation of thrombospondin and other naturally occurring inhibitors of angiogenesis during tumor progression
    • Volpert, O. V., Stellmach, V., and Bouck, N. The modulation of thrombospondin and other naturally occurring inhibitors of angiogenesis during tumor progression. Breast Cancer Res. Treat, 36: 119-126, 1995.
    • (1995) Breast Cancer Res. Treat. , vol.36 , pp. 119-126
    • Volpert, O.V.1    Stellmach, V.2    Bouck, N.3
  • 15
    • 0031690845 scopus 로고    scopus 로고
    • Increased expression of vascular endothelial growth factor is associated with tumor progression in hepatocellular carcinoma
    • Torimura, T., Sata, M., Ueno, T., Kin, M., Tsuji, R., Suzaku, K., Hashimoto, O., Sugawara, H., and Tanikawa, K. Increased expression of vascular endothelial growth factor is associated with tumor progression in hepatocellular carcinoma. Hum. Pathol., 29: 986-991, 1998.
    • (1998) Hum. Pathol. , vol.29 , pp. 986-991
    • Torimura, T.1    Sata, M.2    Ueno, T.3    Kin, M.4    Tsuji, R.5    Suzaku, K.6    Hashimoto, O.7    Sugawara, H.8    Tanikawa, K.9
  • 16
  • 18
    • 0030998660 scopus 로고    scopus 로고
    • Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma
    • Dong, Z., Kumar, R., Yang, X., and Fidler, I. J. Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma. Cell, 88: 801-810, 1997.
    • (1997) Cell , vol.88 , pp. 801-810
    • Dong, Z.1    Kumar, R.2    Yang, X.3    Fidler, I.J.4
  • 19
    • 0032492713 scopus 로고    scopus 로고
    • Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3)
    • Lijnen, H. R., Ugwu, F., Bini, A., and Collen, D. Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3). Biochemistry, 37: 4699-4702, 1998.
    • (1998) Biochemistry , vol.37 , pp. 4699-4702
    • Lijnen, H.R.1    Ugwu, F.2    Bini, A.3    Collen, D.4
  • 20
    • 15444352707 scopus 로고    scopus 로고
    • Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9)
    • Patterson, B. C., and Sang, Q. A. Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9). J. Biol. Chem., 272: 28823-28825, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28823-28825
    • Patterson, B.C.1    Sang, Q.A.2
  • 21
    • 0032832479 scopus 로고    scopus 로고
    • Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance
    • O'Reilly, M. S., Wiederschain, D., Steller-Stevenson, W. G., Folkman, J., and Moses, M. A. Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance. J. Biol. Chem., 274: 29568-29571, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29568-29571
    • O'Reilly, M.S.1    Wiederschain, D.2    Steller-Stevenson, W.G.3    Folkman, J.4    Moses, M.A.5
  • 24
    • 0034528886 scopus 로고    scopus 로고
    • Angiostatin and angiostatin-related proteins
    • Soff, G. A. Angiostatin and angiostatin-related proteins. Cancer Metastasis Rev., 19: 97-107, 2000.
    • (2000) Cancer Metastasis Rev. , vol.19 , pp. 97-107
    • Soff, G.A.1
  • 25
    • 0033605663 scopus 로고    scopus 로고
    • Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin
    • Stathakis, P., Lay, A. J., Fitzgerald, M., Schlieker, C., Matthias, L. J., and Hogg, P. J. Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin. J. Biol. Chem., 274: 8910-8916, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8910-8916
    • Stathakis, P.1    Lay, A.J.2    Fitzgerald, M.3    Schlieker, C.4    Matthias, L.J.5    Hogg, P.J.6
  • 26
    • 0030861045 scopus 로고    scopus 로고
    • Generation of angiostatin by reduction and proteolysis of plasmin. Catalysis by a plasmin reductase secreted by cultured cells
    • Stathakis, P., Fitzgerald, M., Matthias, L. J., Chesterman, C. N., and Hogg, P. J. Generation of angiostatin by reduction and proteolysis of plasmin. Catalysis by a plasmin reductase secreted by cultured cells. J. Biol. Chem., 272: 20641-20645, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20641-20645
    • Stathakis, P.1    Fitzgerald, M.2    Matthias, L.J.3    Chesterman, C.N.4    Hogg, P.J.5
  • 27
    • 0033545930 scopus 로고    scopus 로고
    • Suppression of angiogenesis and tumor growth by the inhibitor K1-5 generated by plasmin-mediated proteolysis
    • Cao, R., Wu, H. L., Veitonmaki, N., Linden, P., Farnebo, J., Shi, G. Y., and Cao, Y. Suppression of angiogenesis and tumor growth by the inhibitor K1-5 generated by plasmin-mediated proteolysis. Proc. Natl. Acad. Sci. USA, 96: 5728-5733, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5728-5733
    • Cao, R.1    Wu, H.L.2    Veitonmaki, N.3    Linden, P.4    Farnebo, J.5    Shi, G.Y.6    Cao, Y.7
  • 28
    • 0034181854 scopus 로고    scopus 로고
    • Elevated levels of urine angiostatin and plasminogen/plasmin in cancer patients
    • Cao, Y., Veitonmaki, N., Keough, K., Cheng, H., Lee, L. S., and Zurakowski, D. Elevated levels of urine angiostatin and plasminogen/plasmin in cancer patients. Int. J. Mol. Med., 5: 547-551, 2000.
    • (2000) Int. J. Mol. Med. , vol.5 , pp. 547-551
    • Cao, Y.1    Veitonmaki, N.2    Keough, K.3    Cheng, H.4    Lee, L.S.5    Zurakowski, D.6
  • 29
    • 0030692665 scopus 로고    scopus 로고
    • Human angiostatin inhibits murine hemangioendothelioma tumor growth in vivo
    • Lannutti, B. J., Gately, S. T., Quevedo, M. E., Soff, G. A., and Paller, A. S. Human angiostatin inhibits murine hemangioendothelioma tumor growth in vivo. Cancer Res., 57: 5277-5280, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 5277-5280
    • Lannutti, B.J.1    Gately, S.T.2    Quevedo, M.E.3    Soff, G.A.4    Paller, A.S.5
  • 31
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman, D. M. Annexin II tetramer: structure and function. Mol. Cell Biochem, 149-150: 301-322, 1995.
    • (1995) Mol. Cell Biochem. , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 32
    • 0028129557 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation
    • Cesarman, G. M., Guevara, C. A., and Hajjar, K. A. An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation. J. Biol. Chem., 269: 21198-21203, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21198-21203
    • Cesarman, G.M.1    Guevara, C.A.2    Hajjar, K.A.3
  • 33
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II
    • Hajjar, K. A., Jacovina, A. T., and Chacko, J. An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. J. Biol. Chem., 269: 21191-21197, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 34
    • 0033678175 scopus 로고    scopus 로고
    • Discriminating between cell surface and intracellular plasminogen-binding proteins: Heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells
    • Hawley, S. B., Green, M. A., and Miles, L. A. Discriminating between cell surface and intracellular plasminogen-binding proteins: heterogeneity in profibrinolytic plasminogen-binding proteins on monocytoid cells. Thromb. Haemost., 84: 882-890, 2000.
    • (2000) Thromb. Haemost. , vol.84 , pp. 882-890
    • Hawley, S.B.1    Green, M.A.2    Miles, L.A.3
  • 35
    • 0035937779 scopus 로고    scopus 로고
    • Purification and characterization of A61. An angiostatin-like plasminogen fragment produced by plasmin autodigestion in the absence of sulfhydryl donors
    • Kassam, G., Kwon, M., Yoon, C. S., Graham, K. S., Young, M. K., Gluck, S., and Waisman, D. M. Purification and characterization of A61. An angiostatin-like plasminogen fragment produced by plasmin autodigestion in the absence of sulfhydryl donors. J. Biol. Chem., 276: 8924-8933, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8924-8933
    • Kassam, G.1    Kwon, M.2    Yoon, C.S.3    Graham, K.S.4    Young, M.K.5    Gluck, S.6    Waisman, D.M.7
  • 37
    • 0028839088 scopus 로고
    • The role of an enolase-related molecule in plasminogen binding to cells
    • Redlitz, A., Fowler, B. J., Plow, E. F., and Miles, L. A. The role of an enolase-related molecule in plasminogen binding to cells. Eur. J. Biochem., 227: 407-415, 1995.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 38
    • 0030996010 scopus 로고    scopus 로고
    • Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner
    • Liu, L., Tao, J. Q., and Zimmerman, U. J. Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner. Cell Signalling, 9: 299-304, 1997.
    • (1997) Cell Signalling , vol.9 , pp. 299-304
    • Liu, L.1    Tao, J.Q.2    Zimmerman, U.J.3
  • 39
    • 0029817448 scopus 로고    scopus 로고
    • Endothelial cell surface actin serves as it binding site for plasminogen, tissue plasminogen activator and lipoprotein(a)
    • Dudani, A. K., and Ganz, P. R. Endothelial cell surface actin serves as it binding site for plasminogen, tissue plasminogen activator and lipoprotein(a). Br. J. Haematol., 95: 168-178, 1996.
    • (1996) Br. J. Haematol. , vol.95 , pp. 168-178
    • Dudani, A.K.1    Ganz, P.R.2
  • 40
    • 0035860127 scopus 로고    scopus 로고
    • The topology of plasminogen binding and activation on the surface of human breast cancer cells
    • Andronicos, N. M., and Ranson, M. The topology of plasminogen binding and activation on the surface of human breast cancer cells. Br. J. Cancer, 85: 909-916, 2001.
    • (2001) Br. J. Cancer , vol.85 , pp. 909-916
    • Andronicos, N.M.1    Ranson, M.2
  • 42
    • 0036366353 scopus 로고    scopus 로고
    • Measurement of reduction of disulfide bonds in plasmin by phosphoglycerate kinase
    • Lay, A. J., and Hogg, P. J. Measurement of reduction of disulfide bonds in plasmin by phosphoglycerate kinase. Methods Enzymol., 348: 87-92, 2002.
    • (2002) Methods Enzymol. , vol.348 , pp. 87-92
    • Lay, A.J.1    Hogg, P.J.2
  • 45
    • 0020607661 scopus 로고
    • A lymphocyte cell surface molecule that is antigenically related to actin
    • Sanders, S. K., and Craig, S. W. A lymphocyte cell surface molecule that is antigenically related to actin. J. Immunol., 131: 370-377, 1983.
    • (1983) J. Immunol. , vol.131 , pp. 370-377
    • Sanders, S.K.1    Craig, S.W.2
  • 46
    • 0024453809 scopus 로고
    • Brain capillary 46, 000 dalton protein is cytoplasmic actin and is localized to endothelial plasma membrane
    • Pardridge, W. M., Nowlin, D. M., Choi, T. B., Yang, J., Calaycay, J., and Shively, J. E. Brain capillary 46, 000 dalton protein is cytoplasmic actin and is localized to endothelial plasma membrane. J. Cereb. Blood Flow Metab., 9: 675-680, 1989.
    • (1989) J. Cereb. Blood Flow Metab. , vol.9 , pp. 675-680
    • Pardridge, W.M.1    Nowlin, D.M.2    Choi, T.B.3    Yang, J.4    Calaycay, J.5    Shively, J.E.6
  • 47
    • 0027189729 scopus 로고
    • Actin is a surface component of calf pulmonary artery endothelial cells in culture
    • Moroianu, J., Fett, J. W., Riordan, J. F., and Vallee, B. L. Actin is a surface component of calf pulmonary artery endothelial cells in culture. Proc. Natl. Acad. Sci. USA, 90: 3815-3819, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3815-3819
    • Moroianu, J.1    Fett, J.W.2    Riordan, J.F.3    Vallee, B.L.4
  • 49
    • 0027768660 scopus 로고
    • Angiogenin enhances actin acceleration of plasminogen activation
    • Hu, G. F., and Riordan, J. F. Angiogenin enhances actin acceleration of plasminogen activation. Biochem. Biophys. Res. Commun., 197: 682-687, 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 682-687
    • Hu, G.F.1    Riordan, J.F.2
  • 51
    • 0025246272 scopus 로고
    • Research on the mechanism of interaction between actin and membrane lipids
    • St-Onge, D., and Gicquaud, C. Research on the mechanism of interaction between actin and membrane lipids. Biochem. Biophys. Res. Commun., 167: 40-47, 1990.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 40-47
    • St-Onge, D.1    Gicquaud, C.2
  • 52
    • 0024385603 scopus 로고
    • Evidence of direct interaction between actin and membrane lipids
    • St-Onge, D., and Gicquaud, C. Evidence of direct interaction between actin and membrane lipids. Biochem. Cell Biol., 67: 297-300, 1989.
    • (1989) Biochem. Cell Biol. , vol.67 , pp. 297-300
    • St-Onge, D.1    Gicquaud, C.2
  • 53
    • 0027437479 scopus 로고
    • Actin conformation is drastically altered by direct interaction with membrane lipids: A differential scanning calorimetry study
    • Gicquaud, C. Actin conformation is drastically altered by direct interaction with membrane lipids: a differential scanning calorimetry study. Biochemistry, 32: 11873-11877, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11873-11877
    • Gicquaud, C.1
  • 54
    • 0028969850 scopus 로고
    • Does actin bind to membrane lipids under conditions compatible with those existing in vivo?
    • Gicquaud, C. Does actin bind to membrane lipids under conditions compatible with those existing in vivo? Biochem. Biophys. Res. Commun., 208: 1154-1158, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 1154-1158
    • Gicquaud, C.1
  • 55
    • 0028099208 scopus 로고
    • Mechanism of interaction between actin and membrane lipids: A pressure-tuning infrared spectroscopy study
    • Gicquaud, C., and Wong, P. Mechanism of interaction between actin and membrane lipids: a pressure-tuning infrared spectroscopy study. Biochem. J., 303 (Pt 3): 769-774, 1994.
    • (1994) Biochem. J. , vol.303 , Issue.PART 3 , pp. 769-774
    • Gicquaud, C.1    Wong, P.2
  • 56
    • 0028902319 scopus 로고
    • Tumor angiogenesis as a prognostic factor in cervical carcinoma
    • Wiggins, D. L., Granai, C. O., Steinhoff, M. M., and Calabresi, P. Tumor angiogenesis as a prognostic factor in cervical carcinoma. Gynecol Oncol, 56: 353-356, 1995.
    • (1995) Gynecol Oncol , vol.56 , pp. 353-356
    • Wiggins, D.L.1    Granai, C.O.2    Steinhoff, M.M.3    Calabresi, P.4
  • 57
    • 0038364216 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Recent advances and implication for prognosis and therapy
    • Sidenius, N., and Blasi, F. The urokinase plasminogen activator system in cancer: recent advances and implication for prognosis and therapy. Cancer Metastasis Rev., 22: 205-222, 2003.
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 205-222
    • Sidenius, N.1    Blasi, F.2
  • 58
    • 0002606253 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Implications for tumor angiogenesis and metastasis
    • Mazar, A. P., Henkin, J., and Goldfarb, R. H. The urokinase plasminogen activator system in cancer: implications for tumor angiogenesis and metastasis. Angiogenesis, 3: 15-32, 1999.
    • (1999) Angiogenesis , vol.3 , pp. 15-32
    • Mazar, A.P.1    Henkin, J.2    Goldfarb, R.H.3


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