메뉴 건너뛰기




Volumn 49, Issue 10, 1989, Pages 2533-2553

Growth Factors in the Regulation of Pericellular Proteolysis: A Review

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; PLASMINOGEN ACTIVATOR;

EID: 0024309860     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (313)

References (337)
  • 1
    • 0021336875 scopus 로고
    • Plasminogen activators, activation inhibitors and α2-macroglobulin produced by cultured normal and malignant cells
    • Saksela, O., Vaheri, A., Schleuning, W.-D., Mignatti, P., and Barlati, S. Plasminogen activators, activation inhibitors and α2-macroglobulin produced by cultured normal and malignant cells. Int. J. Cancer, 33: 609-616, 1984.
    • (1984) Int. J. Cancer , vol.33 , pp. 609-616
    • Saksela, O.1    Vaheri, A.2    Schleuning, W.-D.3    Mignatti, P.4    Barlati, S.5
  • 2
    • 0023031062 scopus 로고
    • Plasminogen activators, plasminogen activator inhibitors and pro-coagulant analyzed in twenty human tumor cell lines
    • Cajot, J.-F., Kruithof, E. K. O., Schleuning, W.-D., Sordat, B., and Bachman, F. Plasminogen activators, plasminogen activator inhibitors and pro-coagulant analyzed in twenty human tumor cell lines. Int. J. Cancer, 38: 719-727,1986.
    • (1986) Int. J. Cancer , vol.38 , pp. 719-727
    • Cajot, J.-F.1    Kruithof, E.K.O.2    Schleuning, W.-D.3    Sordat, B.4    Bachman, F.5
  • 7
    • 0020490792 scopus 로고
    • A proenzyme form of human urokinase
    • Wun, T.-C., Ossowski, L., and Reich, E. A proenzyme form of human urokinase. J. Biol. Chem., 257: 7262-7268, 1982.
    • (1982) J. Biol. Chem , vol.257 , pp. 7262-7268
    • Wun, T.-C.1    Ossowski, L.2    Reich, E.3
  • 8
    • 0021261963 scopus 로고
    • Concomitant secretion of prourokinase and of a plasminogen activator-specific inhibitor by cultured human monocytes-macrophages
    • Vassalli, J.-D., Dayer, J.-M., Wohlwend, A., and Belin, D. Concomitant secretion of prourokinase and of a plasminogen activator-specific inhibitor by cultured human monocytes-macrophages. J. Exp. Med., 159: 1653-1668, 1984.
    • (1984) J. Exp. Med , vol.159 , pp. 1653-1668
    • Vassalli, J.-D.1    Dayer, J.-M.2    Wohlwend, A.3    Belin, D.4
  • 9
    • 0021315179 scopus 로고
    • Inactive proenzyme to tissue-type plasminogen activator from human melanoma cells, identified after affinity purification with a monoclonal antibody
    • Andreasen, P. A., Nielsen, L. S., Grondahl-Hansen, J., Skriver, L., Zeuthen, J., Stephens, R. W., and Dano, K. Inactive proenzyme to tissue-type plasminogen activator from human melanoma cells, identified after affinity purification with a monoclonal antibody. EMBO J., 3: 51-56, 1984.
    • (1984) EMBO J , vol.3 , pp. 51-56
    • Andreasen, P.A.1    Nielsen, L.S.2    Grondahl-Hansen, J.3    Skriver, L.4    Zeuthen, J.5    Stephens, R.W.6    Dano, K.7
  • 10
    • 0021254064 scopus 로고
    • Purification of human fibroblast urokinase proenzyme and analysis of its regulation by proteases and protease nexin
    • Eaton, D. L., Scott, R. W., and Baker, J. B. Purification of human fibroblast urokinase proenzyme and analysis of its regulation by proteases and protease nexin. J. Biol. Chem., 259: 6241-6247, 1984.
    • (1984) J. Biol. Chem , vol.259 , pp. 6241-6247
    • Eaton, D.L.1    Scott, R.W.2    Baker, J.B.3
  • 11
    • 0021826499 scopus 로고
    • Proenzyme to urokinase-type plasminogen activator in the mouse in vivo
    • Kielberg, V., Andreasen, P. A., Grendahl-Hansen, J., Skriver, L., and Dano, K. Proenzyme to urokinase-type plasminogen activator in the mouse in vivo. FEBS Lett., 182: 441-445, 1985.
    • (1985) FEBS Lett , vol.182 , pp. 441-445
    • Kielberg, V.1    Andreasen, P.A.2    Grendahl-Hansen, J.3    Skriver, L.4    Dano, K.5
  • 12
    • 0021723844 scopus 로고
    • Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors
    • Blomquist, M. C., Hunt, L. T., and Baker, W. C. Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. USA, 81: 7363-7367, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7363-7367
    • Blomquist, M.C.1    Hunt, L.T.2    Baker, W.C.3
  • 13
    • 0023022473 scopus 로고
    • The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin
    • Ichinose, A., Fujikawa, K., and Suyama, T. The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin. J. Biol. Chem., 261: 3486–3489, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 3486-3489
    • Ichinose, A.1    Fujikawa, K.2    Suyama, T.3
  • 15
    • 0023199478 scopus 로고
    • Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study
    • Ellis, V., Scully, M. F., and Kakkar, V. V. Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study. J. Biol. Chem., 262: 14998–15003, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 14998-15003
    • Ellis, V.1    Scully, M.F.2    Kakkar, V.V.3
  • 16
    • 0022632219 scopus 로고
    • Urokinase-related proteins in human urine. Isolation and characterization of single-chain urokinase (pro-urokinase) and urokinase-inhibitor complex
    • Stump, D. C., Thienpont, M., and Collen, D. Urokinase-related proteins in human urine. Isolation and characterization of single-chain urokinase (pro-urokinase) and urokinase-inhibitor complex. J. Biol. Chem., 261: 1267-1273,1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 1267-1273
    • Stump, D.C.1    Thienpont, M.2    Collen, D.3
  • 17
    • 0022648246 scopus 로고
    • Purification and characterization of single-chain urokinase-type plasminogen activator from human cell cultures
    • Stump, D. C., Lijnen, H. R., and Collen, D. Purification and characterization of single-chain urokinase-type plasminogen activator from human cell cultures. J. Biol. Chem., 261: 1274-1278, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 1274-1278
    • Stump, D.C.1    Lijnen, H.R.2    Collen, D.3
  • 18
    • 0001149917 scopus 로고
    • Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes
    • Stoppelli, M. P., Corti, A., Soffientini, A., Cassani, G., Blasi, F., and Assoian, R. K. Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proc. Natl. Acad. Sci. USA, 82: 4939-4943, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4939-4943
    • Stoppelli, M.P.1    Corti, A.2    Soffientini, A.3    Cassani, G.4    Blasi, F.5    Assoian, R.K.6
  • 20
    • 0021984227 scopus 로고
    • r55,000 form of the human plasminogen activator, urokinase
    • r55,000 form of the human plasminogen activator, urokinase. J. Cell Biol., 100: 86-92, 1985.
    • (1985) J. Cell Biol , vol.100 , pp. 86-92
    • Vassalli, J.-D.1    Baccino, D.2    Belin, D.3
  • 21
    • 0022494568 scopus 로고
    • r 17,500 region of the A chain of urokinase is required for interaction with a specific receptor in A431 cells
    • r 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
  • 22
    • 0021950820 scopus 로고
    • Receptors for plasminogen activator, urokinase, in normal and Rous sarcoma virus-transformed mouse fibroblasts
    • Del Rosso, M., Dini, G., and Fibbi, G. Receptors for plasminogen activator, urokinase, in normal and Rous sarcoma virus-transformed mouse fibroblasts. Cancer Res., 45: 630-636, 1985.
    • (1985) Cancer Res , vol.45 , pp. 630-636
    • Del Rosso, M.1    Dini, G.2    Fibbi, G.3
  • 23
    • 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
  • 24
    • 0023197175 scopus 로고
    • Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors
    • Blasi, F., Vassalli, J.-D., and Dano, K. Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors. J. Cell Biol., 104: 801–804, 1987.
    • (1987) J. Cell Biol , vol.104 , pp. 801-804
    • Blasi, F.1    Vassalli, J.-D.2    Dano, K.3
  • 25
    • 0023840122 scopus 로고
    • r receptor protein for urokinase-type plasminogen activator. Identification in human tumor cell lines and partial purification
    • r 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
  • 27
    • 0023603282 scopus 로고
    • Proliferation of a human epidermal tumor cell line stimulated by urokinase
    • Kirchheimer, J. C., Wojta, J., Christ, G., and Binder, B. R. Proliferation of a human epidermal tumor cell line stimulated by urokinase. FASEB J., 1: 125-128, 1987.
    • (1987) FASEB J , vol.1 , pp. 125-128
    • Kirchheimer, J.C.1    Wojta, J.2    Christ, G.3    Binder, B.R.4
  • 28
    • 0023515489 scopus 로고
    • Binding of tissue plasminogen activator to cultured human endothelial cells
    • Hajjar, K. A., Hamel, N. M., Harpel, P. C., and Nachman, R. L. Binding of tissue plasminogen activator to cultured human endothelial cells. J. Clin. Invest., 80: 1712-1719, 1987.
    • (1987) J. Clin. Invest , vol.80 , pp. 1712-1719
    • Hajjar, K.A.1    Hamel, N.M.2    Harpel, P.C.3    Nachman, R.L.4
  • 29
    • 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
  • 30
    • 0021074276 scopus 로고
    • Modulation of plasminogen activator in rodent mammary tumors by hormones and other effectors
    • Mira-y-Lopez, R., Reich, E., and Ossowski, L. Modulation of plasminogen activator in rodent mammary tumors by hormones and other effectors. Cancer Res., 43: 5467–5477, 1983.
    • (1983) Cancer Res , vol.43 , pp. 5467-5477
    • Mira-y-Lopez, R.1    Reich, E.2    Ossowski, L.3
  • 31
    • 0022404962 scopus 로고
    • Plasminogen activation and regulation of pericellular proteolysis
    • Saksela, O. Plasminogen activation and regulation of pericellular proteolysis. Biochim. Biophys. Acta, 823: 35-65, 1985.
    • (1985) Biochim. Biophys. Acta , vol.823 , pp. 35-65
    • Saksela, O.1
  • 32
    • 0019987224 scopus 로고
    • Studies on the kinetics of plasminogen activation by tissue plasminogen activator
    • Ranby, M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim. Biophys. Acta, 704: 461-469, 1982.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 461-469
    • Ranby, M.1
  • 35
    • 0023576670 scopus 로고
    • Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells
    • Pepper, M. S., Vassalli, J.-D., Montesano, R., and Orci, L. Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells. J. Cell Biol., 105: 2535-2541, 1987.
    • (1987) J. Cell Biol , vol.105 , pp. 2535-2541
    • Pepper, M.S.1    Vassalli, J.-D.2    Montesano, R.3    Orci, L.4
  • 36
    • 0020662367 scopus 로고
    • Plasminogen activator in differentiating mouse keratinocytes
    • Isseroff, R. R., Fusenig, N. E., and Rifkin, D. B. Plasminogen activator in differentiating mouse keratinocytes. J. Invest. Dermatol., 80: 217–222, 1983.
    • (1983) J. Invest. Dermatol , vol.80 , pp. 217-222
    • Isseroff, R.R.1    Fusenig, N.E.2    Rifkin, D.B.3
  • 37
    • 0018832744 scopus 로고
    • Plasminogen activator of islets of Langerhans: modulation by glucose and correlation with insulin production
    • Virji, M. A. G., Vassalli, J.-D., Estensen, R. D., and Reich, E. Plasminogen activator of islets of Langerhans: modulation by glucose and correlation with insulin production. Proc. Natl. Acad. Sci. USA, 77: 875–879, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 875-879
    • Virji, M.A.G.1    Vassalli, J.-D.2    Estensen, R.D.3    Reich, E.4
  • 38
    • 0020609834 scopus 로고
    • Plasminogen activators of the pituitary gland: enzyme characterization and hormonal modulation
    • Granelli-Piperno, A., and Reich, E. Plasminogen activators of the pituitary gland: enzyme characterization and hormonal modulation. J. Cell Biol., 97: 1029-1037, 1983.
    • (1983) J. Cell Biol , vol.97 , pp. 1029-1037
    • Granelli-Piperno, A.1    Reich, E.2
  • 39
    • 0023916551 scopus 로고
    • Proteolytic activation of latent transforming growth factor-β from fibroblast conditioned medium
    • Lyons, R. M., Keski-Oja, J., and Moses, H. L. Proteolytic activation of latent transforming growth factor-β from fibroblast conditioned medium. J. Cell Biol., 106: 1659-1665, 1988.
    • (1988) J. Cell Biol , vol.106 , pp. 1659-1665
    • Lyons, R.M.1    Keski-Oja, J.2    Moses, H.L.3
  • 40
  • 41
    • 0024203073 scopus 로고
    • Proteolytic processing of Mullerian inhibiting substance produces a transforming growth factor-β-like fragment
    • Pepinsky, R. B., Sinclair, L. K., Chow, E. P., Mattaliano, R. J., Manganaro, T. F., Donahoe, P. K., and Cate, R. L. Proteolytic processing of Mullerian inhibiting substance produces a transforming growth factor-β-like fragment. J. Biol. Chem., 263: 18961-18964, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 18961-18964
    • Pepinsky, R.B.1    Sinclair, L.K.2    Chow, E.P.3    Mattaliano, R.J.4    Manganaro, T.F.5    Donahoe, P.K.6    Cate, R.L.7
  • 42
    • 27144495545 scopus 로고
    • Activation of latent cell-derived transforming growth factor-β by the plasminogen activator urokinase. 28th Annual Meeting, American Society for Cell Biology, San Francisco, CA
    • Part 3
    • Keski-Oja, J., Laiho, M., and Lohi, J. Activation of latent cell-derived transforming growth factor-β by the plasminogen activator urokinase. 28th Annual Meeting, American Society for Cell Biology, San Francisco, CA. J. Cell. Biol., 107 (Part 3): 50a, 1989.
    • (1989) J. Cell. Biol , vol.107 , pp. 50a
    • Keski-Oja, J.1    Laiho, M.2    Lohi, J.3
  • 43
    • 0016677955 scopus 로고
    • Ovarian plasminogen activator: relationship to ovulation and hormonal regulation
    • Beers, W. H., Strickland, S., and Reich, E. Ovarian plasminogen activator: relationship to ovulation and hormonal regulation. Cell, 6: 387-394, 1975.
    • (1975) Cell , vol.6 , pp. 387-394
    • Beers, W.H.1    Strickland, S.2    Reich, E.3
  • 44
    • 0016679759 scopus 로고
    • Follicular plasminogen and plasminogen activator and the effect of plasmin on ovarian follicle wall
    • Beers, W. H. Follicular plasminogen and plasminogen activator and the effect of plasmin on ovarian follicle wall. Cell, 6: 379-386, 1975.
    • (1975) Cell , vol.6 , pp. 379-386
    • Beers, W.H.1
  • 45
    • 0023251025 scopus 로고
    • Plasminogen activator and mouse spermatozoa: urokinase synthesis in the male genital tract and binding of the enzyme to the sperm cell surface
    • Huarte, J., Belin, D., Bosco, D., Sappino, A.-P., and Vassalli, J.-D. Plasminogen activator and mouse spermatozoa: urokinase synthesis in the male genital tract and binding of the enzyme to the sperm cell surface. J. Cell Biol., 104: 1281-1289, 1987.
    • (1987) J. Cell Biol , vol.104 , pp. 1281-1289
    • Huarte, J.1    Belin, D.2    Bosco, D.3    Sappino, A.-P.4    Vassalli, J.-D.5
  • 46
    • 0017183196 scopus 로고
    • Plasminogen activator in early embryogenesis: enzyme production by trophoblast and parietal endoderm
    • Strickland, S., Reich, E., and Sherman, M. I. Plasminogen activator in early embryogenesis: enzyme production by trophoblast and parietal endoderm. Cell, 9: 231-240, 1976.
    • (1976) Cell , vol.9 , pp. 231-240
    • Strickland, S.1    Reich, E.2    Sherman, M.I.3
  • 47
    • 0018757458 scopus 로고
    • Mammary plasminogen activator: correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue
    • Ossowski, L., Biegel, D., and Reich, E. Mammary plasminogen activator: correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell, 16: 929-940, 1979.
    • (1979) Cell , vol.16 , pp. 929-940
    • Ossowski, L.1    Biegel, D.2    Reich, E.3
  • 48
    • 84965844668 scopus 로고
    • Activation of plasminogen. A general mechanism for producing localized extracellular proteolysis
    • R. D. Berlin, L. Herrman, I. H. Lepow, and J. M. Tanzer (eds.) New York: Academic Press
    • Reich, E. Activation of plasminogen. A general mechanism for producing localized extracellular proteolysis. In: R. D. Berlin, L. Herrman, I. H. Lepow, and J. M. Tanzer (eds.), Molecular Basis of Biological Degradative Processes, New York: Academic Press, pp. 155-169, 1980.
    • (1980) Molecular Basis of Biological Degradative Processes , pp. 155-169
    • Reich, E.1
  • 49
    • 0021115222 scopus 로고
    • The role of proteinases in cellular invasiveness
    • Mullins, D. E., and Rorlich, 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    Rorlich, S.T.2
  • 50
    • 0015545381 scopus 로고
    • An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses
    • Ossowski, L., Unkeless, J. C., Tobia, A., Quigley, J. P., Rifkin, D. B., and Reich, E. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses. J. Exp. Med., 137: 112-126, 1973.
    • (1973) J. Exp. Med , vol.137 , pp. 112-126
    • Ossowski, L.1    Unkeless, J.C.2    Tobia, A.3    Quigley, J.P.4    Rifkin, D.B.5    Reich, E.6
  • 51
    • 0015548765 scopus 로고
    • An enzymatic function associated with transformation of fibroblasts by oncogenic viruses
    • Unkeless, J. C., Tobia, A., Ossowski, L., Quigley, J. P., Rifkin, D. B., and Reich, E. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. J. Exp. Med., 137: 85-111, 1973.
    • (1973) J. Exp. Med , vol.137 , pp. 85-111
    • Unkeless, J.C.1    Tobia, A.2    Ossowski, L.3    Quigley, J.P.4    Rifkin, D.B.5    Reich, E.6
  • 52
    • 0016370111 scopus 로고
    • Plasminogen activator production accompanies loss of anchorage regulation in transformation of primary rat embryo cells by Simian virus 40
    • Pollack, R., Risser, R., Conlon, S., and Rifkin, D. Plasminogen activator production accompanies loss of anchorage regulation in transformation of primary rat embryo cells by Simian virus 40. Proc. Natl. Acad. Sci. USA, 71: 4792-4796, 1974.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4792-4796
    • Pollack, R.1    Risser, R.2    Conlon, S.3    Rifkin, D.4
  • 53
    • 0019877129 scopus 로고
    • Purification and characterization of the plasminogen activator secreted by human melanoma cell lines in culture
    • Rijken, D. C., and Collen, D. Purification and characterization of the plasminogen activator secreted by human melanoma cell lines in culture. J. Biol. Chem., 256: 7035-7041, 1981.
    • (1981) J. Biol. Chem , vol.256 , pp. 7035-7041
    • Rijken, D.C.1    Collen, D.2
  • 54
    • 0018168479 scopus 로고
    • Lack of correlation between tumorigenicity and level of plasminogen activator in fibroblasts transformed by Rous sarcoma virus
    • Wolf, B. A., and Goldberg, A. R. Lack of correlation between tumorigenicity and level of plasminogen activator in fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA, 75: 4967-4971, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4967-4971
    • Wolf, B.A.1    Goldberg, A.R.2
  • 55
    • 0016611797 scopus 로고
    • Relationships between fibrinolysis of cultured cells and malignancy
    • Laug, W. E., Jones, P. A., and Benedict, W. F. Relationships between fibrinolysis of cultured cells and malignancy. J. Natl. Cancer Inst., 54: 173-179, 1975.
    • (1975) J. Natl. Cancer Inst , vol.54 , pp. 173-179
    • Laug, W.E.1    Jones, P.A.2    Benedict, W.F.3
  • 56
    • 0018857418 scopus 로고
    • Plasminogen activator synthesis accompanying chemical carcinogen induced in vitro transformation of Syrian hamster and guinea-pig fetal cells
    • Sisskin, E. E., Weinstein, I. B., Evans, C. H., and DiPaolo, J. A. Plasminogen activator synthesis accompanying chemical carcinogen induced in vitro transformation of Syrian hamster and guinea-pig fetal cells. Int. J. Cancer, 26: 331-335, 1980.
    • (1980) Int. J. Cancer , vol.26 , pp. 331-335
    • Sisskin, E.E.1    Weinstein, I.B.2    Evans, C.H.3    DiPaolo, J.A.4
  • 58
    • 0018762701 scopus 로고
    • Phorbol ester-induced morphological changes in transformed chick fibroblasts: evidence for direct catalytic involvement of plasminogen activator
    • Quigley, J. P. Phorbol ester-induced morphological changes in transformed chick fibroblasts: evidence for direct catalytic involvement of plasminogen activator. Cell, 17: 131-141, 1979.
    • (1979) Cell , vol.17 , pp. 131-141
    • Quigley, J.P.1
  • 60
    • 0023053525 scopus 로고
    • An anticatalytic monoclonal antibody to avian plasminogen activator its effect on behavior of RSV-transformed chick fibroblasts
    • Sullivan, L. M., and Quigley, J. P. An anticatalytic monoclonal antibody to avian plasminogen activator its effect on behavior of RSV-transformed chick fibroblasts. Cell, 45: 905-915, 1986.
    • (1986) Cell , vol.45 , pp. 905-915
    • Sullivan, L.M.1    Quigley, J.P.2
  • 61
    • 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
  • 62
    • 0023853553 scopus 로고
    • Plasminogen activator dependent pathways in the dissemination of human tumor cells in the chick embryo
    • Ossowski, L. Plasminogen activator dependent pathways in the dissemination of human tumor cells in the chick embryo. Cell, 52: 321-328, 1988.
    • (1988) Cell , vol.52 , pp. 321-328
    • Ossowski, L.1
  • 63
    • 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
  • 64
    • 0023192953 scopus 로고
    • Distinct localizations of urokinase-type plasminogen activator and its type-1 inhibitor under cultured human fibroblasts and sarcoma cells
    • Pollanen, J., Saksela, O., Salonen, E.-M., Andreasen, P. A., Nielsen, L. S., Dano, K., and Vaheri, A. Distinct localizations of urokinase-type plasminogen activator and its type-1 inhibitor under cultured human fibroblasts and sarcoma cells. J. Cell Biol., 104: 1085-1096, 1987.
    • (1987) J. Cell Biol , vol.104 , pp. 1085-1096
    • Pollanen, J.1    Saksela, O.2    Salonen, E.-M.3    Andreasen, P.A.4    Nielsen, L.S.5    Dano, K.6    Vaheri, A.7
  • 65
    • 0023819126 scopus 로고
    • Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contact
    • Pollanen, J., Hedman, K., Nielsen, L. S., Dano, K., and Vaheri, A. Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contact. J. Cell Biol., 106: 87-95, 1988.
    • (1988) J. Cell Biol , vol.106 , pp. 87-95
    • Pollanen, J.1    Hedman, K.2    Nielsen, L.S.3    Dano, K.4    Vaheri, A.5
  • 66
    • 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
  • 67
    • 0022351973 scopus 로고
    • The extracellular matrix of normal chick embryo fibroblasts: its effect on transformed chick fibroblasts and its proteolytic degradation by the trans-formants
    • Fairbairn, S., Gilbert, R., Ojakian, G., Schwimmer, R., and Quigley, J. P. The extracellular matrix of normal chick embryo fibroblasts: its effect on transformed chick fibroblasts and its proteolytic degradation by the trans-formants. J. Cell Biol., 101: 1790-1798, 1985.
    • (1985) J. Cell Biol , vol.101 , pp. 1790-1798
    • Fairbairn, S.1    Gilbert, R.2    Ojakian, G.3    Schwimmer, R.4    Quigley, J.P.5
  • 68
    • 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
  • 70
    • 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: 2437-2447,1988.
    • (1988) J. Cell Biol , vol.107 , pp. 2437-2447
    • Ossowski, L.1
  • 71
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J., and Salvesen, G. S. Human plasma proteinase inhibitors. Annu. Rev. Biochem., 52: 655-709, 1983.
    • (1983) Annu. Rev. Biochem , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 72
    • 0018193854 scopus 로고
    • A study of proteases and protease-inhibitor complexes in biological fluids
    • Granelli-Pipemo, A., and Reich, E. A study of proteases and protease-inhibitor complexes in biological fluids. J. Exp. Med., 146: 223-234, 1978.
    • (1978) J. Exp. Med , vol.146 , pp. 223-234
    • Granelli-Pipemo, A.1    Reich, E.2
  • 73
    • 0021985069 scopus 로고
    • 1-antitrypsin and the serpins: variation and countervariation
    • 1-antitrypsin and the serpins: variation and countervariation. Trends Biochem. Sci., 10: 20-24, 1985.
    • (1985) Trends Biochem. Sci , vol.10 , pp. 20-24
    • Carrell, R.1    Travis, J.2
  • 74
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill, R. E., and Hastie, N. D. Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature (Lond.), 326: 96-99, 1987.
    • (1987) Nature (Lond.) , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 75
    • 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
  • 76
    • 0021235999 scopus 로고
    • Protease nexins: cell-secreted proteins which regulate extracellular serine proteinases
    • Knauer, D. J., and Cunningham, D. D. Protease nexins: cell-secreted proteins which regulate extracellular serine proteinases. Trends Biochem. Sci., 9: 231-233, 1984.
    • (1984) Trends Biochem. Sci , vol.9 , pp. 231-233
    • Knauer, D.J.1    Cunningham, D.D.2
  • 77
    • 0021689228 scopus 로고
    • Human endothelial cells produce a plasminogen activator inhibitor and a tissue-type plasminogen activator-inhibitor complex
    • Phillips, M., Juul, A.-G., and Thorsen, S. Human endothelial cells produce a plasminogen activator inhibitor and a tissue-type plasminogen activator-inhibitor complex. Biochim. Biophys. Acta, 802: 99-110, 1984.
    • (1984) Biochim. Biophys. Acta , vol.802 , pp. 99-110
    • Phillips, M.1    Juul, A.-G.2    Thorsen, S.3
  • 78
    • 0021130318 scopus 로고
    • Evidence for the presence of two different fibrinolytic inhibitors in human endothelial cell conditioned medium
    • Sprengers, E. D., Verheijen, J. H., van Hinsbergh, V. W. M., and Emeis, J. J. Evidence for the presence of two different fibrinolytic inhibitors in human endothelial cell conditioned medium. Biochim. Biophys. Acta, 801: 163-170,1984.
    • (1984) Biochim. Biophys. Acta , vol.801 , pp. 163-170
    • Sprengers, E.D.1    Verheijen, J.H.2    van Hinsbergh, V.W.M.3    Emeis, J.J.4
  • 79
    • 0343759135 scopus 로고
    • Synthesis of a fibrinolytic activator and inhibitor by endothelial cells
    • Loskutoff, D. J., and Edgington, T. S. Synthesis of a fibrinolytic activator and inhibitor by endothelial cells. Proc. Natl. Acad. Sci. USA, 74: 3903-3907,1977.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3903-3907
    • Loskutoff, D.J.1    Edgington, T.S.2
  • 80
    • 0020625088 scopus 로고
    • Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells
    • Loskutoff, D. J., van Mourik, J. A., Erickson, L. A., and Lawrence, D. Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells. Proc. Natl. Acad. Sci. USA, 80: 2956-2960, 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2956-2960
    • Loskutoff, D.J.1    van Mourik, J.A.2    Erickson, L.A.3    Lawrence, D.4
  • 81
    • 0021046716 scopus 로고
    • Latent tissue plasminogen activator produced by human endothelial cells in culture: evidence for an enzyme-inhibitor complex
    • Levin, E. G. Latent tissue plasminogen activator produced by human endothelial cells in culture: evidence for an enzyme-inhibitor complex. Proc. Natl. Acad. Sci. USA, 80: 6804-6808, 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6804-6808
    • Levin, E.G.1
  • 82
    • 0021687079 scopus 로고
    • Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells
    • van Mourik, J. A., Lawrence, D. A., and Loskutoff, D. J. Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells. J. Biol. Chem., 259: 14914-14921, 1984.
    • (1984) J. Biol. Chem , vol.259 , pp. 14914-14921
    • van Mourik, J.A.1    Lawrence, D.A.2    Loskutoff, D.J.3
  • 83
    • 0021821154 scopus 로고
    • Vascular smooth muscle cells inhibit plasminogen activators secreted by endothelial cells
    • Laug, W. E. Vascular smooth muscle cells inhibit plasminogen activators secreted by endothelial cells. Thromb. Haemostasis, 53: 165-170, 1985.
    • (1985) Thromb. Haemostasis , vol.53 , pp. 165-170
    • Laug, W.E.1
  • 84
    • 0021824566 scopus 로고
    • Cultured granulosa cells produce two plasminogen activators and an antiactivator, each regulated differently by gonadotropins
    • Ny, T., Bjersing, L., Hsueh, A. J. W., and Loskutoff, D. J. Cultured granulosa cells produce two plasminogen activators and an antiactivator, each regulated differently by gonadotropins. Endocrinology, 116: 1666-1668,1985.
    • (1985) Endocrinology , vol.116 , pp. 1666-1668
    • Ny, T.1    Bjersing, L.2    Hsueh, A.J.W.3    Loskutoff, D.J.4
  • 85
    • 0021230086 scopus 로고
    • Dexamethasone induction of an inhibitor of plasminogen activator in HTC hepatoma cells
    • Cwikel, B. J., Barouski-Miller, P. A., Coleman, P. L., and Gelehrter, T. Dexamethasone induction of an inhibitor of plasminogen activator in HTC hepatoma cells. J. Biol. Chem., 259: 6847-6851, 1984.
    • (1984) J. Biol. Chem , vol.259 , pp. 6847-6851
    • Cwikel, B.J.1    Barouski-Miller, P.A.2    Coleman, P.L.3    Gelehrter, T.4
  • 86
    • 0023000195 scopus 로고
    • Characterization of the dexamethasone-induced inhibitor of plasminogen activator in HTC hepatoma cells
    • Coleman, P. L., Patel, P. D., Cwikel, B. J., Rafferty, U. M., Sznycer-Laszuk, R., and Gelehrter, T. D. Characterization of the dexamethasone-induced inhibitor of plasminogen activator in HTC hepatoma cells. J. Biol. Chem., 261: 4352-4357, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 4352-4357
    • Coleman, P.L.1    Patel, P.D.2    Cwikel, B.J.3    Rafferty, U.M.4    Sznycer-Laszuk, R.5    Gelehrter, T.D.6
  • 87
    • 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., Grondahl-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    Grondahl-Hansen, J.4    Skriver, L.5    Dano, K.6
  • 88
    • 0022252043 scopus 로고
    • Identification of a reversible inhibitor of plasminogen activators in blood plasma
    • Kluft, C., Jie, A. F. H., Sprengers, E. D., and Verheijen, J. H. Identification of a reversible inhibitor of plasminogen activators in blood plasma. FEBS Lett., 190: 315-318, 1985.
    • (1985) FEBS Lett , vol.190 , pp. 315-318
    • Kluft, C.1    Jie, A.F.H.2    Sprengers, E.D.3    Verheijen, J.H.4
  • 89
    • 0021677450 scopus 로고
    • Detection and partial characterization of an inhibitor of plasminogen activator in human platelets
    • Erickson, L. A., Ginsberg, M. H., and Loskutoff, D. J. Detection and partial characterization of an inhibitor of plasminogen activator in human platelets. J. Clin. Invest., 74: 1465-1472, 1984.
    • (1984) J. Clin. Invest , vol.74 , pp. 1465-1472
    • Erickson, L.A.1    Ginsberg, M.H.2    Loskutoff, D.J.3
  • 90
    • 0345693050 scopus 로고
    • Cloning and sequence of a cDNA coding for the human β-migrating endothelial-cell-type plasminogen activator inhibitor
    • Ny, T., Sawdey, M., Lawrence, D., Millan, J. L., and Loskutoff, D. J. Cloning and sequence of a cDNA coding for the human β-migrating endothelial-cell-type plasminogen activator inhibitor. Proc. Natl. Acad. Sci. USA, 83: 6776-6780, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6776-6780
    • Ny, T.1    Sawdey, M.2    Lawrence, D.3    Millan, J.L.4    Loskutoff, D.J.5
  • 93
    • 0022887824 scopus 로고
    • Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing
    • Andreasen, P. A., Riccio, A., Welinder, K. G., Douglas, R., Sartorio, R., Nielsen, L. S., Oppenheimer, C., Blasi, F., and Dano, K. Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing. FEBS Lett., 209: 213–218, 1986.
    • (1986) FEBS Lett , vol.209 , pp. 213-218
    • Andreasen, P.A.1    Riccio, A.2    Welinder, K.G.3    Douglas, R.4    Sartorio, R.5    Nielsen, L.S.6    Oppenheimer, C.7    Blasi, F.8    Dano, K.9
  • 95
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman, C. M., and Loskutoff, D. J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J. Biol. Chem., 260: 11581-11587, 1985.
    • (1985) J. Biol. Chem , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 96
    • 0022550933 scopus 로고
    • The active and inactive plasminogen activator inhibitor from human endothelial cell conditioned medium are immunologically and functionally related to each other
    • Sprengers, E. D., van Hinsberg, V. W. M., and Jansen, B. G. The active and inactive plasminogen activator inhibitor from human endothelial cell conditioned medium are immunologically and functionally related to each other. Biochim. Biophys. Acta, 883: 233-241, 1986.
    • (1986) Biochim. Biophys. Acta , vol.883 , pp. 233-241
    • Sprengers, E.D.1    van Hinsberg, V.W.M.2    Jansen, B.G.3
  • 97
    • 0022495150 scopus 로고
    • Quantitation and properties of the active and latent plasminogen activator inhibitors in cultures of human endothelial cells
    • Levin, E. G. Quantitation and properties of the active and latent plasminogen activator inhibitors in cultures of human endothelial cells. Blood, 67: 1309-1313,1986.
    • (1986) Blood , vol.67 , pp. 1309-1313
    • Levin, E.G.1
  • 98
    • 0023612924 scopus 로고
    • Conversion of the active to latent plasminogen activator inhibitor from human endothelial cells
    • Levin, E. G., and Santell, L. Conversion of the active to latent plasminogen activator inhibitor from human endothelial cells. Blood, 70: 1090–1098, 1987.
    • (1987) Blood , vol.70 , pp. 1090-1098
    • Levin, E.G.1    Santell, L.2
  • 99
    • 0022312075 scopus 로고
    • The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related
    • Erickson, L. A., Hekman, C. M., and Loskutoff, D. J. The primary plasminogen-activator inhibitors in endothelial cells, platelets, serum, and plasma are immunologically related. Proc. Natl. Acad. Sci. USA, 82: 8710-8714, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8710-8714
    • Erickson, L.A.1    Hekman, C.M.2    Loskutoff, D.J.3
  • 100
    • 0022826059 scopus 로고
    • Rapid inactivation of the plasminogen-activator inhibitor upon secretion from cultured human endothelial cells
    • Kooistra, T., Sprengers, E. D., and van Hinsberg, V. W. M. Rapid inactivation of the plasminogen-activator inhibitor upon secretion from cultured human endothelial cells. Biochem. J., 239: 497-503, 1986.
    • (1986) Biochem. J , vol.239 , pp. 497-503
    • Kooistra, T.1    Sprengers, E.D.2    van Hinsberg, V.W.M.3
  • 101
    • 0023637141 scopus 로고
    • Activation of human endothelial cell-type plasminogen activator inhibitor (PAI-1) by negatively charged phospholipids
    • Lambers, J. W. J., Cammenga, M., Konig, B. W., Mertens, K., Pannekoek, H., and van Mourik, J. A. Activation of human endothelial cell-type plasminogen activator inhibitor (PAI-1) by negatively charged phospholipids. J. Biol. Chem., 262: 17492-17496, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 17492-17496
    • Lambers, J.W.J.1    Cammenga, M.2    Konig, B.W.3    Mertens, K.4    Pannekoek, H.5    van Mourik, J.A.6
  • 102
    • 0022549709 scopus 로고
    • Plasminogen activators catalyse conversion of inhibitor from fibrosarcoma cells to an inactive form with a lower apparent molecular mass
    • Nielsen, L. S., Andreasen, P. A., Grondahl-Hansen, J., Skriver, L., and Dano, K. Plasminogen activators catalyse conversion of inhibitor from fibrosarcoma cells to an inactive form with a lower apparent molecular mass. FEBS Lett., 196: 269-273, 1986.
    • (1986) FEBS Lett , vol.196 , pp. 269-273
    • Nielsen, L.S.1    Andreasen, P.A.2    Grondahl-Hansen, J.3    Skriver, L.4    Dano, K.5
  • 103
    • 0022599303 scopus 로고
    • Thrombin induction of plasminogen activator-inhibitor in cultured endothelial cells
    • Gelehrter, T. D., and Sznycer-Laszuk, R. Thrombin induction of plasminogen activator-inhibitor in cultured endothelial cells. J. Clin. Invest., 77: 165-169,1986.
    • (1986) J. Clin. Invest , vol.77 , pp. 165-169
    • Gelehrter, T.D.1    Sznycer-Laszuk, R.2
  • 104
    • 0022637312 scopus 로고
    • Endotoxin induction of an inhibitor of plasminogen activator in bovine pulmonary artery endothelial cells
    • Crutchley, D. J., and Conanan, L. B. Endotoxin induction of an inhibitor of plasminogen activator in bovine pulmonary artery endothelial cells. J. Biol. Chem., 261: 154-159, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 154-159
    • Crutchley, D.J.1    Conanan, L.B.2
  • 105
    • 0022525897 scopus 로고
    • Interleukin 1 and lipopolysaccharide induce an inhibitor of tissue-type plasminogen activator in vivo and in cultured endothelial cells
    • Emeis, J. J., and Kooistra, T. Interleukin 1 and lipopolysaccharide induce an inhibitor of tissue-type plasminogen activator in vivo and in cultured endothelial cells. J. Exp. Med., 163: 1260-1266, 1986.
    • (1986) J. Exp. Med , vol.163 , pp. 1260-1266
    • Emeis, J.J.1    Kooistra, T.2
  • 106
    • 0014423662 scopus 로고
    • Urokinase inhibitor in human placenta
    • Kawano, T., Morimoto, K., and Uemura, Y. Urokinase inhibitor in human placenta. Nature (Lond.), 217: 253-254, 1968.
    • (1968) Nature (Lond.) , vol.217 , pp. 253-254
    • Kawano, T.1    Morimoto, K.2    Uemura, Y.3
  • 107
    • 0022003765 scopus 로고
    • Purification of a specific placental plasminogen activator inhibitor by monoclonal antibody and its complex formation with plasminogen activator
    • Astedt, B., Lecander, I., Brodin, T., Lundblad, A., and Low, K. Purification of a specific placental plasminogen activator inhibitor by monoclonal antibody and its complex formation with plasminogen activator. Thromb. Haemostasis, 55: 122-125, 1985.
    • (1985) Thromb. Haemostasis , vol.55 , pp. 122-125
    • Astedt, B.1    Lecander, I.2    Brodin, T.3    Lundblad, A.4    Low, K.5
  • 108
    • 0023899838 scopus 로고
    • Epidermal plasminogen activator inhibitor (PAI) is immunologically identical to placental-type PAI-2
    • Hibino, T., Izaki, S., Ohkuma, M., Kon, S., Thorsen, S., and Astedt, B. Epidermal plasminogen activator inhibitor (PAI) is immunologically identical to placental-type PAI-2. FEBS Lett, 231: 202-206, 1988.
    • (1988) FEBS Lett , vol.231 , pp. 202-206
    • Hibino, T.1    Izaki, S.2    Ohkuma, M.3    Kon, S.4    Thorsen, S.5    Astedt, B.6
  • 109
    • 0021075737 scopus 로고
    • Minactivin: a human monocyte product which specifically inactivates urokinase-type plasminogen activators
    • Golder, J. P., and Stephens, R. W. Minactivin: a human monocyte product which specifically inactivates urokinase-type plasminogen activators. Eur. J. Biochem., 136: 517-522, 1983.
    • (1983) Eur. J. Biochem , vol.136 , pp. 517-522
    • Golder, J.P.1    Stephens, R.W.2
  • 110
    • 0021996968 scopus 로고
    • Urokinase-type plasminogen activator and its inhibitor secreted by cultured human monocyte-macrophages
    • Saksela, O., Hovi, T., and Vaheri, A. Urokinase-type plasminogen activator and its inhibitor secreted by cultured human monocyte-macrophages. J. Cell. Physiol., 122: 125-132,1985.
    • (1985) J. Cell. Physiol , vol.122 , pp. 125-132
    • Saksela, O.1    Hovi, T.2    Vaheri, A.3
  • 111
    • 0022979217 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor from the histiocytic lymphoma cell line U-937
    • Kruithof, E. K. O., Vassalli, J.-D., Schleuning, W.-D., Mattaliano, R. J., and Bachman, F. Purification and characterization of a plasminogen activator inhibitor from the histiocytic lymphoma cell line U-937. J. Biol. Chem., 261: 11207-11213, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 11207-11213
    • Kruithof, E.K.O.1    Vassalli, J.-D.2    Schleuning, W.-D.3    Mattaliano, R.J.4    Bachman, F.5
  • 112
    • 0023856372 scopus 로고
    • Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type-2 and urokinases
    • Kiso, U., Kaudewitz, H., Henschen, A., Astedt, B., Kruithof, E. K. O., and Bachmann, F. Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type-2 and uroki-nases. FEBS Lett., 230: 51-56, 1988.
    • (1988) FEBS Lett , vol.230 , pp. 51-56
    • Kiso, U.1    Kaudewitz, H.2    Henschen, A.3    Astedt, B.4    Kruithof, E.K.O.5    Bachmann, F.6
  • 113
    • 0023654279 scopus 로고
    • cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta
    • Ye, R. D., Wun, T.-C., and Sadler, J. E. cDNA cloning and expression in Escherichia coli of a plasminogen activator inhibitor from human placenta. J. Biol. Chem., 262: 3718-3725, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 3718-3725
    • Ye, R.D.1    Wun, T.-C.2    Sadler, J.E.3
  • 114
    • 0023637406 scopus 로고
    • Plasminogen activator inhibitor 2: Regulation of gene transcription during phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma cells
    • Schleuning, W.-D., Medcalf, R. L., Hession, C., Rothenbuhler, R., Shaw, A., and Kruithof, E. K. O. Plasminogen activator inhibitor 2: Regulation of gene transcription during phorbol ester-mediated differentiation of U-937 human histiocytic lymphoma cells. Mol. Cell. Biol., 7: 4564-4567, 1987.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 4564-4567
    • Schleuning, W.-D.1    Medcalf, R.L.2    Hession, C.3    Rothenbuhler, R.4    Shaw, A.5    Kruithof, E.K.O.6
  • 116
    • 0023267551 scopus 로고
    • Plasminogen activator-specific inhibitors in mouse macrophages: in vivo and in vitro modulation of their synthesis and secretion
    • Wohlwend, A., Belin, D., and Vassalli, J.-D. Plasminogen activator-specific inhibitors in mouse macrophages: in vivo and in vitro modulation of their synthesis and secretion. J. Immunol., 139: 1278-1284, 1987.
    • (1987) J. Immunol , vol.139 , pp. 1278-1284
    • Wohlwend, A.1    Belin, D.2    Vassalli, J.-D.3
  • 118
    • 0023917559 scopus 로고
    • Increased release of plasminogen activator inhibitor type 2 accompanies the human mononuclear cell tissue factor response to lipopolysaccharide
    • Schwartz, B. S., Monroe, M. C., and Levin, E. G. Increased release of plasminogen activator inhibitor type 2 accompanies the human mononuclear cell tissue factor response to lipopolysaccharide. Blood, 71: 734-741, 1988.
    • (1988) Blood , vol.71 , pp. 734-741
    • Schwartz, B.S.1    Monroe, M.C.2    Levin, E.G.3
  • 119
    • 0021091544 scopus 로고
    • Purification of human protease nexin
    • Scott, R. W., and Baker, J. B. Purification of human protease nexin. J. Biol. Chem., 258: 10439-10444, 1983.
    • (1983) J. Biol. Chem , vol.258 , pp. 10439-10444
    • Scott, R.W.1    Baker, J.B.2
  • 121
    • 0023664516 scopus 로고
    • Purification of protease nexin II from human fibroblasts
    • Van Nostrand, W. E., and Cunningham, D. D. Purification of protease nexin II from human fibroblasts. J. Biol. Chem., 262: 8508-8514, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 8508-8514
    • Van Nostrand, W.E.1    Cunningham, D.D.2
  • 122
    • 0018932068 scopus 로고
    • Protease nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells
    • Baker, J. B., Low, D. A., Simmer, R. L., and Cunningham, D. D. Protease nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells. Cell, 21: 37-45, 1980.
    • (1980) Cell , vol.21 , pp. 37-45
    • Baker, J.B.1    Low, D.A.2    Simmer, R.L.3    Cunningham, D.D.4
  • 123
    • 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. Sci. USA, 83: 996-1000, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 996-1000
    • Bergman, B.L.1    Scott, R.W.2    Bajpai, A.3    Watts, S.4    Baker, J.B.5
  • 124
    • 0023838288 scopus 로고
    • Localization of protease nexin-1 on the fibroblast extracellular matrix
    • Farrell, D. H., Wagner, S. L., Yuan, R. H., and Cunningham, D. D. Localization of protease nexin-1 on the fibroblast extracellular matrix. J. Cell. Physiol., 134: 179-188, 1988.
    • (1988) J. Cell. Physiol , vol.134 , pp. 179-188
    • Farrell, D.H.1    Wagner, S.L.2    Yuan, R.H.3    Cunningham, D.D.4
  • 126
    • 0021353283 scopus 로고
    • Plasma levels of a specific inhibitor of tissue-type plasminogen activator (and urokinase) in normal and pathological conditions
    • Juhan-Vague, I., Moerman, B., De Cock, F., Aillaud, M. F., and Collen, D. Plasma levels of a specific inhibitor of tissue-type plasminogen activator (and urokinase) in normal and pathological conditions. Thromb. Res., 33: 523-530,1984.
    • (1984) Thromb. Res , vol.33 , pp. 523-530
    • Juhan-Vague, I.1    Moerman, B.2    De Cock, F.3    Aillaud, M.F.4    Collen, D.5
  • 127
    • 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. Blood, 59: 7-12, 1988.
    • (1988) Blood , vol.59 , pp. 7-12
    • Kruithof, E.K.O.1    Gudinchet, A.2    Bachmann, F.3
  • 128
    • 0022353583 scopus 로고
    • Postoperative changes in the plasmatic levels of tissue-type plasminogen activator and its fast-acting inhibitor-relationship to deep vein thrombosis and influence of prophylaxis
    • Paramo, J. A., Alfaro, M. J., and Rocha, E. Postoperative changes in the plasmatic levels of tissue-type plasminogen activator and its fast-acting inhibitor-relationship to deep vein thrombosis and influence of prophylaxis. Thromb. Haemostasis, 54: 713-716, 1985.
    • (1985) Thromb. Haemostasis , vol.54 , pp. 713-716
    • Paramo, J.A.1    Alfaro, M.J.2    Rocha, E.3
  • 129
    • 0023574958 scopus 로고
    • Plasminogen activator inhibitor 1: development of a radioimmunoassay and observations on its plasma concentration during venous occlusion and after platelet aggregation
    • Kruithof, E. K. O., Nicolosa, G., and Bachmann, F. Plasminogen activator inhibitor 1: development of a radioimmunoassay and observations on its plasma concentration during venous occlusion and after platelet aggregation. Blood, 70: 1645-1653, 1987.
    • (1987) Blood , vol.70 , pp. 1645-1653
    • Kruithof, E.K.O.1    Nicolosa, G.2    Bachmann, F.3
  • 130
    • 0007394174 scopus 로고
    • An ordered sequence of events is required before BALB/c-3T3 cells become committed to DNA synthesis
    • Pledger, W. J., Stiles, C. D., Antoniades, H. N., and Scher, C. D. An ordered sequence of events is required before BALB/c-3T3 cells become committed to DNA synthesis. Proc. Natl. Acad. Sci. USA, 75: 2839-2843, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2839-2843
    • Pledger, W.J.1    Stiles, C.D.2    Antoniades, H.N.3    Scher, C.D.4
  • 131
    • 0019170218 scopus 로고
    • Serum-free cell culture: a unifying approach
    • Barnes, D., and Sato, G. Serum-free cell culture: a unifying approach. Cell, 22: 649-655, 1980.
    • (1980) Cell , vol.22 , pp. 649-655
    • Barnes, D.1    Sato, G.2
  • 132
    • 0007990001 scopus 로고
    • Defined media and studies of growth factors
    • G. Guroff (ed.) New York: John Wiley & Sons, Inc
    • Bottenstein, J. E. Defined media and studies of growth factors. In: G. Guroff (ed.), Growth and Maturation Factors, New York: John Wiley & Sons, Inc., Vol. 1, pp. 249-266,1983.
    • (1983) Growth and Maturation Factors , vol.1 , pp. 249-266
    • Bottenstein, J.E.1
  • 133
    • 0020546295 scopus 로고
    • Mitogenic response to epidermal growth factor (EGF) modulated by platelet-derived growth factor in cultured fibroblasts
    • Wharton, W., Leof, E., Olashaw, N., O’Keefe, E. J., and Pledger, W. J. Mitogenic response to epidermal growth factor (EGF) modulated by platelet-derived growth factor in cultured fibroblasts. Exp. Cell Res., 147: 443-448, 1983.
    • (1983) Exp. Cell Res , vol.147 , pp. 443-448
    • Wharton, W.1    Leof, E.2    Olashaw, N.3    O’Keefe, E.J.4    Pledger, W.J.5
  • 135
    • 0016714582 scopus 로고
    • Control of growth of mammalian cells in cell culture
    • Holley, R. W. Control of growth of mammalian cells in cell culture. Nature (Lond.), 258: 487-490, 1975.
    • (1975) Nature (Lond.) , vol.258 , pp. 487-490
    • Holley, R.W.1
  • 136
    • 0022553189 scopus 로고
    • Epidermal growth factor, its receptor, and related proteins
    • Carpenter, G., and Zendegui, J. G. Epidermal growth factor, its receptor, and related proteins. Exp. Cell Res., 164: 1-10, 1986.
    • (1986) Exp. Cell Res , vol.164 , pp. 1-10
    • Carpenter, G.1    Zendegui, J.G.2
  • 139
    • 0020319268 scopus 로고
    • Human transforming growth factor. Production by a melanoma cell line, purification, and initial characterization
    • Marquardt, H., and Todaro, G. J. Human transforming growth factor. Production by a melanoma cell line, purification, and initial characterization. J. Biol. Chem., 257: 5220-5225, 1982.
    • (1982) J. Biol. Chem , vol.257 , pp. 5220-5225
    • Marquardt, H.1    Todaro, G.J.2
  • 140
    • 0021752924 scopus 로고
    • Human transforming growth factor-α: precursor structure and expression in E. coli
    • Derynck, R., Roberts, A. B., Winkler, M. E., Chen, E. Y., and Goeddel, D. V. Human transforming growth factor-α: precursor structure and expression in E. coli. Cell, 38: 287-297, 1984.
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1    Roberts, A.B.2    Winkler, M.E.3    Chen, E.Y.4    Goeddel, D.V.5
  • 142
    • 0023066224 scopus 로고
    • The genome of Shope fibroma virus, a tumorigenic poxvirus, contains a growth factor gene sequence similarity to those encoding epidermal growth factor and transforming growth factor a
    • Chang, W., Upton, C., Hu, S.-L., Purchio, A. F., and McFadden, G. The genome of Shope fibroma virus, a tumorigenic poxvirus, contains a growth factor gene sequence similarity to those encoding epidermal growth factor and transforming growth factor a. Mol. Cell. Biol., 7: 535-540, 1987.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 535-540
    • Chang, W.1    Upton, C.2    Hu, S.-L.3    Purchio, A.F.4    McFadden, G.5
  • 143
    • 0023117551 scopus 로고
    • Mapping and sequencing of a gene from myxoma virus that is related to those encoding epidermal growth factor and transforming growth factor a
    • Upton, C., Macen, J. L., and McFadden, G. Mapping and sequencing of a gene from myxoma virus that is related to those encoding epidermal growth factor and transforming growth factor a. J. Virol., 61: 1271–1275, 1987.
    • (1987) J. Virol , vol.61 , pp. 1271-1275
    • Upton, C.1    Macen, J.L.2    McFadden, G.3
  • 144
    • 0018886725 scopus 로고
    • Sarcoma growth factor (SGF): specific binding to epidermal growth factor (EGF) membrane receptors
    • DeLarco, J. E., and Todaro, G. J. Sarcoma growth factor (SGF): specific binding to epidermal growth factor (EGF) membrane receptors. J. Cell. Physiol., 102: 267-277, 1980.
    • (1980) J. Cell. Physiol , vol.102 , pp. 267-277
    • DeLarco, J.E.1    Todaro, G.J.2
  • 145
    • 0019359370 scopus 로고
    • Human transforming growth factors induce tyrosine phosphorylation of EGF receptors
    • Reynolds, F. H., Jr., Todaro, G. J., Fryling, C., and Stephenson, J. R. Human transforming growth factors induce tyrosine phosphorylation of EGF receptors. Nature (Lond.), 292: 259-262, 1981.
    • (1981) Nature (Lond.) , vol.292 , pp. 259-262
    • Reynolds, F.H.1    Todaro, G.J.2    Fryling, C.3    Stephenson, J.R.4
  • 146
    • 0021013896 scopus 로고
    • Epidermal growth factor-like transforming growth factor. II. Interaction with epidermal growth factor receptors in human placenta membranes and A431 cells
    • Massague, J. Epidermal growth factor-like transforming growth factor. II. Interaction with epidermal growth factor receptors in human placenta membranes and A431 cells. J. Biol. Chem., 258: 13614–13620, 1983.
    • (1983) J. Biol. Chem , vol.258 , pp. 13614-13620
    • Massague, J.1
  • 147
    • 0020053847 scopus 로고
    • Mouse embryonic transforming growth factors related to those isolated from tumor cells
    • Twardzik, D. R., Ranchalis, J. E., and Todaro, G. J. Mouse embryonic transforming growth factors related to those isolated from tumor cells. Cancer Res., 42: 590-593, 1982.
    • (1982) Cancer Res , vol.42 , pp. 590-593
    • Twardzik, D.R.1    Ranchalis, J.E.2    Todaro, G.J.3
  • 148
    • 0022351809 scopus 로고
    • Differential expression of transforming growth factor-α during prenatal development of the mouse
    • Twardzik, D. R. Differential expression of transforming growth factor-α during prenatal development of the mouse. Cancer Res., 45: 5413–5416, 1985.
    • (1985) Cancer Res , vol.45 , pp. 5413-5416
    • Twardzik, D.R.1
  • 149
    • 0023100052 scopus 로고
    • Synthesis of messenger RNAs for transforming growth factors α and β and the epidermal growth factor receptor by human tumors
    • Derynck, R., Goeddel, D. V., Ullrich, A., Gutterman, J. U., Williams, R. D., Bringman, T. S., and Berger, W. H. Synthesis of messenger RNAs for transforming growth factors α and β and the epidermal growth factor receptor by human tumors. Cancer Res., 47: 707-712, 1987.
    • (1987) Cancer Res , vol.47 , pp. 707-712
    • Derynck, R.1    Goeddel, D.V.2    Ullrich, A.3    Gutterman, J.U.4    Williams, R.D.5    Bringman, T.S.6    Berger, W.H.7
  • 151
    • 0020613199 scopus 로고
    • Tumor-derived growth factor increases bone resorption in a tumor associated with humoral hypercalcemia of malignancy
    • Ibbotson, K. J., D’Souza, S. M., Ng, K. W., Osborne, C. K., Niall, M., Martin, T. J., and Mundy, G. R. Tumor-derived growth factor increases bone resorption in a tumor associated with humoral hypercalcemia of malignancy. Science (Wash. DC), 221: 1292-1294, 1983.
    • (1983) Science (Wash. DC) , vol.221 , pp. 1292-1294
    • Ibbotson, K.J.1    D’Souza, S.M.2    Ng, K.W.3    Osborne, C.K.4    Niall, M.5    Martin, T.J.6    Mundy, G.R.7
  • 153
    • 0022501030 scopus 로고
    • Transforming growth factor-α: a more potent angiogenic mediator than epidermal growth factor
    • Schreiber, A. B., Winkler, M. E., and Derynck, R. Transforming growth factor-α: a more potent angiogenic mediator than epidermal growth factor. Science (Wash. DC), 232: 1250-1253, 1986.
    • (1986) Science (Wash. DC) , vol.232 , pp. 1250-1253
    • Schreiber, A.B.1    Winkler, M.E.2    Derynck, R.3
  • 155
    • 0023335817 scopus 로고
    • Structural characterization and biological functions of fibroblast growth factor
    • Gospodarowicz, D., Ferrara, N., Schweigerer, L., and Neufeld, G. Structural characterization and biological functions of fibroblast growth factor. Endocr. Rev., 8: 95-114, 1987.
    • (1987) Endocr. Rev , vol.8 , pp. 95-114
    • Gospodarowicz, D.1    Ferrara, N.2    Schweigerer, L.3    Neufeld, G.4
  • 156
    • 0023392238 scopus 로고
    • Astroglial and fibroblast growth factors have neurotrophic functions for cultured peripheral and central nervous system neurons
    • Unsicker, K., Reichert-Preibsch, H., Schmidt, R., Pettmann, B., Labourdette, G., and Sensenbrenner, M. Astroglial and fibroblast growth factors have neurotrophic functions for cultured peripheral and central nervous system neurons. Proc. Natl. Acad. Sci. USA, 84: 5459-5463, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5459-5463
    • Unsicker, K.1    Reichert-Preibsch, H.2    Schmidt, R.3    Pettmann, B.4    Labourdette, G.5    Sensenbrenner, M.6
  • 157
    • 0021962617 scopus 로고
    • Purification of two astroglial growth factors from bovine brain
    • Pettmann, B., Weibel, M., Sensenbrenner, M., and Labourdette, G. Purification of two astroglial growth factors from bovine brain. FEBS Lett., 189: 102-108,1985.
    • (1985) FEBS Lett , vol.189 , pp. 102-108
    • Pettmann, B.1    Weibel, M.2    Sensenbrenner, M.3    Labourdette, G.4
  • 158
    • 0006974089 scopus 로고
    • cDNA sequence of human transforming gene hst and identification of the coding sequence required for transforming activity
    • Taira, M., Yoshida, T., Miyagawa, K., Sakamoto, H., Terada, M., and Sugimura, T. cDNA sequence of human transforming gene hst and identification of the coding sequence required for transforming activity. Proc. Natl. Acad. Sci. USA, 84: 2980-2984, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2980-2984
    • Taira, M.1    Yoshida, T.2    Miyagawa, K.3    Sakamoto, H.4    Terada, M.5    Sugimura, T.6
  • 159
    • 0023613622 scopus 로고
    • An oncogene isolated by transfection of Kaposi sarcoma DNA encodes a growth factor that is member of the FGF family
    • Delli Bovi, P., Curatola, A., Kern, F.G., Greco, A., Ittman, M., and Basilico, C. An oncogene isolated by transfection of Kaposi sarcoma DNA encodes a growth factor that is member of the FGF family. Cell, 50: 729-737, 1987.
    • (1987) Cell , vol.50 , pp. 729-737
    • Delli Bovi, P.1    Curatola, A.2    Kern, F.G.3    Greco, A.4    Ittman, M.5    Basilico, C.6
  • 162
    • 0023901511 scopus 로고
    • Modulation of fibroblast functions by interleukin 1: increased steady-state accumulation of type 1 procollagen messenger RNAs and stimulation of other functions but not chemotaxis by human recombinant interleukin 1 α and β
    • Postlethwaite, A. E., Raghow, R., Stricklin, G. P., Poppleton, H., Seyer, J. M., and Kang, A. H. Modulation of fibroblast functions by interleukin 1: increased steady-state accumulation of type 1 procollagen messenger RNAs and stimulation of other functions but not chemotaxis by human recombinant interleukin 1 α and β. J. Cell Biol., 106: 311-318, 1988.
    • (1988) J. Cell Biol , vol.106 , pp. 311-318
    • Postlethwaite, A.E.1    Raghow, R.2    Stricklin, G.P.3    Poppleton, H.4    Seyer, J.M.5    Kang, A.H.6
  • 164
    • 0023506438 scopus 로고
    • Hemopoietic growth factors and their interactions with specific receptors
    • Suppl
    • Nicola, N. A. Hemopoietic growth factors and their interactions with specific receptors. J. Cell. Physiol. Suppl., 5: 9-14, 1987.
    • (1987) J. Cell. Physiol , vol.5 , pp. 9-14
    • Nicola, N.A.1
  • 165
    • 0023928595 scopus 로고
    • Heparan sulfate bound growth factors: a mechanism for stromal cell mediated haemopoiesis
    • Roberts, R., Gallagher, J., Spooncer, E., Allen, T. D., Bloomfield, F., and Dexter, T. M. Heparan sulfate bound growth factors: a mechanism for stromal cell mediated haemopoiesis. Nature (Lond.), 332: 376-378, 1988.
    • (1988) Nature (Lond.) , vol.332 , pp. 376-378
    • Roberts, R.1    Gallagher, J.2    Spooncer, E.3    Allen, T.D.4    Bloomfield, F.5    Dexter, T.M.6
  • 166
    • 0021933641 scopus 로고
    • The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor
    • Sherr, C. J., Rettenmeier, C. W., Sacca, R., Roussel, M. F., Look, A. T., and Stanley, E. R. The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor. Cell, 41: 665–676, 1985.
    • (1985) Cell , vol.41 , pp. 665-676
    • Sherr, C.J.1    Rettenmeier, C.W.2    Sacca, R.3    Roussel, M.F.4    Look, A.T.5    Stanley, E.R.6
  • 168
    • 0023626214 scopus 로고
    • Secretion of interleukin-1 by acute myeloblastic leukemia cells in vitro induces endothelial cells to secrete colony stimulating factors
    • Griffin, J. D., Rambaldi, A., Vellenga, E., Young, D. C., Ostapovicz, D., and Cannistra, S. A. Secretion of interleukin-1 by acute myeloblastic leukemia cells in vitro induces endothelial cells to secrete colony stimulating factors. Blood, 70: 1218-1221, 1987.
    • (1987) Blood , vol.70 , pp. 1218-1221
    • Griffin, J.D.1    Rambaldi, A.2    Vellenga, E.3    Young, D.C.4    Ostapovicz, D.5    Cannistra, S.A.6
  • 169
    • 0001127173 scopus 로고
    • Quantitative studies on viral interference in suspended L cells. III. Effect of interfering viruses and interferon on the growth rate of cells
    • Paucker, K., Cantell, K., and Henle, W. Quantitative studies on viral interference in suspended L cells. III. Effect of interfering viruses and interferon on the growth rate of cells. Virology, 17: 324-334, 1962.
    • (1962) Virology , vol.17 , pp. 324-334
    • Paucker, K.1    Cantell, K.2    Henle, W.3
  • 170
    • 0021271410 scopus 로고
    • Selective induction of c-myc mRNA in Daudi cells by human β-interferon
    • Jonak, G. J., and Knight, E. Selective induction of c-myc mRNA in Daudi cells by human β-interferon. Proc. Natl. Acad. Sci. USA, 81: 1747–1750, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1747-1750
    • Jonak, G.J.1    Knight, E.2
  • 171
    • 0021984245 scopus 로고
    • β-interferon alters the pattern of proteins secreted from quiescent and platelet-derived growth factor-treated BALB/c-3T3 cells
    • Tominaga, S., and Lengyel, P. β-interferon alters the pattern of proteins secreted from quiescent and platelet-derived growth factor-treated BALB/c-3T3 cells. J. Biol. Chem., 260: 1975-1978, 1985.
    • (1985) J. Biol. Chem , vol.260 , pp. 1975-1978
    • Tominaga, S.1    Lengyel, P.2
  • 172
    • 0022296660 scopus 로고
    • Platelet-derived growth factor and double-stranded ribonucleic acids stimulate the expression of the same genes in 3T3 cells
    • Zullo, J. N., Cochran, B. H., Huang, A. S., and Stiles, C. D. Platelet-derived growth factor and double-stranded ribonucleic acids stimulate the expression of the same genes in 3T3 cells. Cell, 43: 793-800, 1985.
    • (1985) Cell , vol.43 , pp. 793-800
    • Zullo, J.N.1    Cochran, B.H.2    Huang, A.S.3    Stiles, C.D.4
  • 173
    • 0023118407 scopus 로고
    • Cachectin: more than a tumor necrosis factor
    • Beutler, B., and Cerami, A. Cachectin: more than a tumor necrosis factor. N. Engl. J. Med., 316: 379–385, 1987.
    • (1987) N. Engl. J. Med , vol.316 , pp. 379-385
    • Beutler, B.1    Cerami, A.2
  • 175
  • 176
    • 0022607023 scopus 로고
    • Fibroblast growth-enhancing activity of tumor necrosis factor and its relationship to other polypeptide growth factors
    • Vilcek, J., Palombella, V. J., Henriksen-DeStefano, D., Swenson, C., Fein-man, R., Hirai, M., and Tsujimoto, M. Fibroblast growth-enhancing activity of tumor necrosis factor and its relationship to other polypeptide growth factors. J. Exp. Med., 163: 632-643, 1986.
    • (1986) J. Exp. Med , vol.163 , pp. 632-643
    • Vilcek, J.1    Palombella, V.J.2    Henriksen-DeStefano, D.3    Swenson, C.4    Fein-man, R.5    Hirai, M.6    Tsujimoto, M.7
  • 178
    • 0017097271 scopus 로고
    • Transformation by murine and feline sarcoma viruses specifically blocks binding of epidermal growth factor to cells
    • Todaro, G. J., De Larco, J. E., and Cohen, S. Transformation by murine and feline sarcoma viruses specifically blocks binding of epidermal growth factor to cells. Nature (Lond.), 264: 26-31, 1976.
    • (1976) Nature (Lond.) , vol.264 , pp. 26-31
    • Todaro, G.J.1    De Larco, J.E.2    Cohen, S.3
  • 179
    • 0018069488 scopus 로고
    • Growth factors produced by sarcoma virus-transformed cells
    • Todaro, G. J., and De Larco, J. E. Growth factors produced by sarcoma virus-transformed cells. Cancer Res., 38: 4147-4154, 1978.
    • (1978) Cancer Res , vol.38 , pp. 4147-4154
    • Todaro, G.J.1    De Larco, J.E.2
  • 180
    • 0000201238 scopus 로고
    • Growth factors from murine sarcoma virus-transformed cells
    • De Larco, J. E., and Todaro, G. J. Growth factors from murine sarcoma virus-transformed cells. Proc. Natl. Acad. Sci. USA, 75: 4001-4005, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4001-4005
    • De Larco, J.E.1    Todaro, G.J.2
  • 181
    • 0019320348 scopus 로고
    • Autocrine secretion and malignant transformation of cells
    • Sporn, M. B., and Todaro, G. J. Autocrine secretion and malignant transformation of cells. N. Engl. J. Med., 303: 878-880, 1980.
    • (1980) N. Engl. J. Med , vol.303 , pp. 878-880
    • Sporn, M.B.1    Todaro, G.J.2
  • 182
    • 0023192594 scopus 로고
    • Transforming growth factor a and β expression in human colon cancer lines: implications for an autocrine model
    • Coffey, R. J., Jr., Goustin, A. S., Soderquist, A. M., Shipley, G. D., Wolfshohl, J., Carpenter, G., and Moses, H. L. Transforming growth factor a and β expression in human colon cancer lines: implications for an autocrine model. Cancer Res., 47: 4590-4594, 1987.
    • (1987) Cancer Res , vol.47 , pp. 4590-4594
    • Coffey, R.J.1    Goustin, A.S.2    Soderquist, A.M.3    Shipley, G.D.4    Wolfshohl, J.5    Carpenter, G.6    Moses, H.L.7
  • 183
    • 0023118074 scopus 로고
    • Transformation of normal rat kidney (NRK) cells by an infectious retrovirus carrying a synthetic rat type a transforming growth factor gene
    • Watanabe, S., Lazar, E., and Sporn, M. B. Transformation of normal rat kidney (NRK) cells by an infectious retrovirus carrying a synthetic rat type a transforming growth factor gene. Proc. Natl. Acad. Sci. USA, 84: 1258-1262, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1258-1262
    • Watanabe, S.1    Lazar, E.2    Sporn, M.B.3
  • 184
    • 0020567863 scopus 로고
    • Cellular responsiveness to growth factors correlates with a cell’s ability to express the transformed phenotype
    • Kaplan, P. L., and Ozanne, B. Cellular responsiveness to growth factors correlates with a cell’s ability to express the transformed phenotype. Cell, 33: 931-938, 1983.
    • (1983) Cell , vol.33 , pp. 931-938
    • Kaplan, P.L.1    Ozanne, B.2
  • 185
    • 0023030919 scopus 로고
    • Induction of anchorage-independent growth by epidermal growth factor and altered sensitivity to type β transforming growth factor in partially transformed rat kidney cells
    • Newman, M. J., Lane, E. A., Nugent, M. A., and Racker, E. Induction of anchorage-independent growth by epidermal growth factor and altered sensitivity to type β transforming growth factor in partially transformed rat kidney cells. Cancer Res., 46: 5842-5850, 1986.
    • (1986) Cancer Res , vol.46 , pp. 5842-5850
    • Newman, M.J.1    Lane, E.A.2    Nugent, M.A.3    Racker, E.4
  • 186
    • 0018148854 scopus 로고
    • Epidermal growth factor, like phorbol esters, induces plasminogen activator in HeLa cells
    • Lee, L.-S., and Weinstein, I. B. Epidermal growth factor, like phorbol esters, induces plasminogen activator in HeLa cells. Nature (Lond.), 274: 696-697,1978.
    • (1978) Nature (Lond.) , vol.274 , pp. 696-697
    • Lee, L.-S.1    Weinstein, I.B.2
  • 187
    • 0020514671 scopus 로고
    • Phorbol esters and mitogens stimulate human fibroblast secretions of plasmin-activatable plasminogen activator and protease nexin, an antiactivator/antiplasmin
    • Eaton, D. L., and Baker, J. B. Phorbol esters and mitogens stimulate human fibroblast secretions of plasmin-activatable plasminogen activator and protease nexin, an antiactivator/antiplasmin. J. Cell Biol., 97: 323-328, 1983.
    • (1983) J. Cell Biol , vol.97 , pp. 323-328
    • Eaton, D.L.1    Baker, J.B.2
  • 188
    • 0020567374 scopus 로고
    • Action of epidermal growth factor and retinoids on anchorage-dependent and -independent growth of non-trans-formed rat kidney cells
    • Jetten, A. M., and Goldfarb, R. H. Action of epidermal growth factor and retinoids on anchorage-dependent and -independent growth of non-trans-formed rat kidney cells. Cancer Res., 43: 2094-2099, 1983.
    • (1983) Cancer Res , vol.43 , pp. 2094-2099
    • Jetten, A.M.1    Goldfarb, R.H.2
  • 189
    • 0021245603 scopus 로고
    • Stimulation of plasminogen activator in osteoblast-like cells by bone-resorbing hormones
    • Hamilton, J. A., Lingelbach, S., Partridge, N. C., and Martin, T. J. Stimulation of plasminogen activator in osteoblast-like cells by bone-resorbing hormones. Biochem. Biophys. Res. Commun., 122: 230-236, 1984.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 230-236
    • Hamilton, J.A.1    Lingelbach, S.2    Partridge, N.C.3    Martin, T.J.4
  • 190
    • 0022553431 scopus 로고
    • Increase in urokinase plasminogen activator mRNA synthesis in human carcinoma cells is a primary effect of the potent tumor-promoter phorbol myristate acetate
    • Stoppelli, M. P., Verde, P., Grimaldi, G., Locatelli, E. K., and Blasi, F. Increase in urokinase plasminogen activator mRNA synthesis in human carcinoma cells is a primary effect of the potent tumor-promoter phorbol myristate acetate. J. Cell Biol., 102: 1235-1244, 1986.
    • (1986) J. Cell Biol , vol.102 , pp. 1235-1244
    • Stoppelli, M.P.1    Verde, P.2    Grimaldi, G.3    Locatelli, E.K.4    Blasi, F.5
  • 191
    • 0022976357 scopus 로고
    • Enhanced production and extracellular deposition of the endothelial-type plasminogen activator inhibitor in cultured human lung fibroblasts by transforming growth factor-β
    • Laiho, M., Saksela, O., Andreasen, P. A., and Keski-Oja, J. Enhanced production and extracellular deposition of the endothelial-type plasminogen activator inhibitor in cultured human lung fibroblasts by transforming growth factor-β. J. Cell Biol., 103: 2403-2410, 1986.
    • (1986) J. Cell Biol , vol.103 , pp. 2403-2410
    • Laiho, M.1    Saksela, O.2    Andreasen, P.A.3    Keski-Oja, J.4
  • 193
    • 0342312351 scopus 로고
    • Purification of a factor from human placenta that stimulates capillary endothelial cell protease production, DNA synthesis and migration
    • Moscatelli, D., Presta, M., and Rifkin, D. B. Purification of a factor from human placenta that stimulates capillary endothelial cell protease production, DNA synthesis and migration. Proc. Natl. Acad. Sci. USA, 83: 2091-2095, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2091-2095
    • Moscatelli, D.1    Presta, M.2    Rifkin, D.B.3
  • 194
    • 0022820965 scopus 로고
    • Purification from a hepatoma cell line a basic fibroblast growth factor-like molecule which stimulates capillary endothelial cell plasminogen activator production, DNA synthesis, and migration
    • Presta, M., Moscatelli, D., Joseph-Silverstein, J., and Rifkin, D. B. Purification from a hepatoma cell line a basic fibroblast growth factor-like molecule which stimulates capillary endothelial cell plasminogen activator production, DNA synthesis, and migration. Mol. Cell. Biol., 6: 4060-4066, 1986.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 4060-4066
    • Presta, M.1    Moscatelli, D.2    Joseph-Silverstein, J.3    Rifkin, D.B.4
  • 195
    • 0023630085 scopus 로고
    • Transforming growth factor-β induction of type-1 plasminogen activator inhibitor. Pericellular deposition and sensitivity to exogenous urokinase
    • Laiho, M., Saksela, O., and Keski-Oja, J. Transforming growth factor-β induction of type-1 plasminogen activator inhibitor. Pericellular deposition and sensitivity to exogenous urokinase. J. Biol. Chem., 262: 17467-17474, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 17467-17474
    • Laiho, M.1    Saksela, O.2    Keski-Oja, J.3
  • 196
    • 0023689973 scopus 로고
    • Regulation of expression of type 1 plasminogen activator inhibitor in Hep G2 cells by epidermal growth factor
    • Lucore, C. L., Fujii, S., Wun, T.-C., Sobel, B. E., and Billadello, J. J. Regulation of expression of type 1 plasminogen activator inhibitor in Hep G2 cells by epidermal growth factor. J. Biol. Chem., 263: 15845–15848, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 15845-15848
    • Lucore, C.L.1    Fujii, S.2    Wun, T.-C.3    Sobel, B.E.4    Billadello, J.J.5
  • 197
    • 0023573994 scopus 로고
    • The opposing effects of basic fibroblast growth factor and transforming growth factor-β on the regulation of plasminogen activator activity in capillary endothelial cells
    • Saksela, O., Moscatelli, D., and Rifkin, D. B. The opposing effects of basic fibroblast growth factor and transforming growth factor-β on the regulation of plasminogen activator activity in capillary endothelial cells. J. Cell Biol., 105: 957-963, 1987.
    • (1987) J. Cell Biol , vol.105 , pp. 957-963
    • Saksela, O.1    Moscatelli, D.2    Rifkin, D.B.3
  • 198
    • 0018376872 scopus 로고
    • Secretion of plasminogen activator by bone marrow-derived mononuclear phagocytes and its enhancement by colony-stimulating factors
    • Lin, H.-S., and Gordon, S. Secretion of plasminogen activator by bone marrow-derived mononuclear phagocytes and its enhancement by colony-stimulating factors. J. Exp. Med., 150: 231-245, 1979.
    • (1979) J. Exp. Med , vol.150 , pp. 231-245
    • Lin, H.-S.1    Gordon, S.2
  • 199
    • 0021321676 scopus 로고
    • The correlation between plasminogen activator activity and thymidine incorporation in mouse bone marrow-derived macrophages
    • Hume, D. A., and Gordon, S. The correlation between plasminogen activator activity and thymidine incorporation in mouse bone marrow-derived macrophages. Exp. Cell Res., 150: 347-355, 1984.
    • (1984) Exp. Cell Res , vol.150 , pp. 347-355
    • Hume, D.A.1    Gordon, S.2
  • 200
    • 0019440949 scopus 로고
    • Increased secretion of plasminogen activator by human macrophages after exposure to leucocyte interferon
    • Hovi, T., Saksela, O., and Vaheri, A. Increased secretion of plasminogen activator by human macrophages after exposure to leucocyte interferon. FEBS Lett., 129: 233-236, 1981.
    • (1981) FEBS Lett , vol.129 , pp. 233-236
    • Hovi, T.1    Saksela, O.2    Vaheri, A.3
  • 201
    • 0022982147 scopus 로고
    • γ-Interferon enhances macrophage transcription of the tumor necrosis fac-tor/cachectin, interleukin-1 and urokinase genes, which are controlled by short-lived repressors
    • Collart, M. A., Belin, D., Vassalli, J.-D., De Kossodo, S., and Vassalli, P. γ-Interferon enhances macrophage transcription of the tumor necrosis fac-tor/cachectin, interleukin-1 and urokinase genes, which are controlled by short-lived repressors. J. Exp. Med., 164: 2113-2118, 1986.
    • (1986) J. Exp. Med , vol.164 , pp. 2113-2118
    • Collart, M.A.1    Belin, D.2    Vassalli, J.-D.3    De Kossodo, S.4    Vassalli, P.5
  • 202
    • 0023875704 scopus 로고
    • Cytokine activation of vascular endothelium. Effects on tissue-type plasminogen activator and type 1 plasminogen activator inhibitor
    • Schleef, R. R., Bevilacqua, M. P., Sawdey, M., Gimbrone, M. A., and Loskutoff, D. J. Cytokine activation of vascular endothelium. Effects on tissue-type plasminogen activator and type 1 plasminogen activator inhibitor. J. Biol. Chem., 263: 5797-5803, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 5797-5803
    • Schleef, R.R.1    Bevilacqua, M.P.2    Sawdey, M.3    Gimbrone, M.A.4    Loskutoff, D.J.5
  • 203
    • 0022517446 scopus 로고
    • Interleukin 1 induces endothelial cell synthesis of plasminogen activator inhibitor
    • Nachman, R. L., Hajjar, K. A., Silverstein, R. L., and Dinarello, C. A. Interleukin 1 induces endothelial cell synthesis of plasminogen activator inhibitor. J. Exp. Med., 163: 1595-1600, 1986.
    • (1986) J. Exp. Med , vol.163 , pp. 1595-1600
    • Nachman, R.L.1    Hajjar, K.A.2    Silverstein, R.L.3    Dinarello, C.A.4
  • 205
    • 0022550086 scopus 로고
    • Type β transforming growth factor in human platelets: release during platelet degranulation and action on vascular smooth muscle cells
    • Assoian, R. K., and Sporn, M. B. Type β transforming growth factor in human platelets: release during platelet degranulation and action on vascular smooth muscle cells. J. Cell Biol., 102: 1217-1223, 1986.
    • (1986) J. Cell Biol , vol.102 , pp. 1217-1223
    • Assoian, R.K.1    Sporn, M.B.2
  • 207
    • 0023597604 scopus 로고
    • Some recent advances in the chemistry and biology of transforming growth factor-β
    • Sporn, M. B., Roberts, A. B., Wakefield, L. M., and de Combrugghe, B. Some recent advances in the chemistry and biology of transforming growth factor-β. J. Cell Biol., 105: 1039-1045, 1987.
    • (1987) J. Cell Biol , vol.105 , pp. 1039-1045
    • Sporn, M.B.1    Roberts, A.B.2    Wakefield, L.M.3    de Combrugghe, B.4
  • 209
    • 0020576560 scopus 로고
    • Transforming growth factor-β in human platelets. Identification of a major storage site, purification, and characterization
    • Assoian, R. K., Komoriya, A., Meyers, C. A., Miller, D. M., and Sporn, M. B. Transforming growth factor-β in human platelets. Identification of a major storage site, purification, and characterization. J. Biol. Chem., 258: 7155-7160,1983.
    • (1983) J. Biol. Chem , vol.258 , pp. 7155-7160
    • Assoian, R.K.1    Komoriya, A.2    Meyers, C.A.3    Miller, D.M.4    Sporn, M.B.5
  • 210
    • 2542488254 scopus 로고
    • Purification and characterization of two cartilage-inducing factors from bovine demineralized bone
    • Seyedin, S. M., Thomas, T. C., Thompson, A. Y., Rosen, D. M., and Piez, K. A. Purification and characterization of two cartilage-inducing factors from bovine demineralized bone. Proc. Natl. Acad. Sci. USA, 82: 2267-2271,1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2267-2271
    • Seyedin, S.M.1    Thomas, T.C.2    Thompson, A.Y.3    Rosen, D.M.4    Piez, K.A.5
  • 214
    • 0023218031 scopus 로고
    • Cloning and sequence analysis of simian transforming growth factor cDNA
    • Sharpies, K., Plowman, G. D., Rose, T. M., Twardzik, D. R., and Purchio, A. F. Cloning and sequence analysis of simian transforming growth factor cDNA. DNA, 6: 239-244, 1987.
    • (1987) DNA , vol.6 , pp. 239-244
    • Sharpies, K.1    Plowman, G.D.2    Rose, T.M.3    Twardzik, D.R.4    Purchio, A.F.5
  • 215
    • 0023026253 scopus 로고
    • The murine transforming growth factor-β precursor
    • Derynck, R., Jarrett, J. A., Chen, E. Y., and Goeddel, D. V. The murine transforming growth factor-β precursor. J. Biol. Chem., 261: 4377–4379, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 4377-4379
    • Derynck, R.1    Jarrett, J.A.2    Chen, E.Y.3    Goeddel, D.V.4
  • 216
  • 217
    • 0022335318 scopus 로고
    • Conversion of a high molecular weight latent β-TGF from chicken embryo fibroblasts into a low molecular weight active β-TGF under acidic conditions
    • Lawrence, D. A., Pircher, R., and Jullien, P. Conversion of a high molecular weight latent β-TGF from chicken embryo fibroblasts into a low molecular weight active β-TGF under acidic conditions. Biochem. Biophys. Res. Commun., 133: 1026-1034, 1985.
    • (1985) Biochem. Biophys. Res. Commun , vol.133 , pp. 1026-1034
    • Lawrence, D.A.1    Pircher, R.2    Jullien, P.3
  • 218
    • 0022477623 scopus 로고
    • β-transforming growth factor is Biophys. stored in human blood platelets as a latent high molecular weight complex
    • Pircher, R., Jullien, P., and Lawrence, D. A. β-transforming growth factor is Biophys. stored in human blood platelets as a latent high molecular weight complex. Biochem. Res. Commun., 136: 30-37, 1986.
    • (1986) Biochem. Res. Commun , vol.136 , pp. 30-37
    • Pircher, R.1    Jullien, P.2    Lawrence, D.A.3
  • 219
    • 0023604578 scopus 로고
    • Distribution and modulation of the cellular receptor for transforming growth factor-β
    • Wakefield, L. M., Smith, D. M., Masui, T., Harris, C. C., and Sporn, M. B. Distribution and modulation of the cellular receptor for transforming growth factor-β. J. Cell Biol., 105: 965-975, 1987.
    • (1987) J. Cell Biol , vol.105 , pp. 965-975
    • Wakefield, L.M.1    Smith, D.M.2    Masui, T.3    Harris, C.C.4    Sporn, M.B.5
  • 220
    • 0023193194 scopus 로고
    • Latent transforming growth factor-β in serum: a specific complex with α2-macroglobulin
    • O’Connor-McCourt, M. D., and Wakefield, L. M. Latent transforming growth factor-β in serum: a specific complex with α2-macroglobulin. J. Biol. Chem., 262: 14090-14099, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 14090-14099
    • O’Connor-McCourt, M.D.1    Wakefield, L.M.2
  • 221
    • 0023840611 scopus 로고
    • 2-macroglobulin complex is a latent form of transforming growth factor-β
    • 2-macroglobulin complex is a latent form of transforming growth factor-β. J. Biol. Chem., 263: 1535-1541, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 1535-1541
    • Huang, S.S.1    O’Grady, P.2    Huang, J.S.3
  • 222
    • 0023473081 scopus 로고
    • Hepatic processing of transforming growth factor β in the rat. Uptake, metabolism, and biliary excretion
    • Coffey, R. J., Jr., Kost, L. J., Lyons, R. M., Moses, H. L., and LaRusso, N. F. Hepatic processing of transforming growth factor β in the rat. Uptake, metabolism, and biliary excretion. J. Clin. Invest., 80: 750-757, 1987.
    • (1987) J. Clin. Invest , vol.80 , pp. 750-757
    • Coffey, R.J.1    Kost, L.J.2    Lyons, R.M.3    Moses, H.L.4    LaRusso, N.F.5
  • 223
    • 0023652332 scopus 로고
    • The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors
    • Cheifetz, S., Weatherbee, J. A., Tsang, M. L.-S., Anderson, J. K., Mole, J. E., Lucas, R., and Massague, J. The transforming growth factor-β system, a complex pattern of cross-reactive ligands and receptors. Cell, 48: 409-415.1987.
    • (1987) Cell , vol.48 , pp. 409-415
    • Cheifetz, S.1    Weatherbee, J.A.2    Tsang, M.L.-S.3    Anderson, J.K.4    Mole, J.E.5    Lucas, R.6    Massague, J.7
  • 224
    • 0023014155 scopus 로고
    • Cellular distribution of type I and type II receptors for transforming growth factor-β
    • Cheifetz, S., Like, B., and Massague, J. Cellular distribution of type I and type II receptors for transforming growth factor-β. J. Biol. Chem., 261: 9972-9978, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 9972-9978
    • Cheifetz, S.1    Like, B.2    Massague, J.3
  • 225
    • 0023763397 scopus 로고
    • The TGFβ receptor type is a membrane proteoglycan. Domain structure of the receptor
    • Cheifetz, S., Andres, J. L., and Massague, J. The TGFβ receptor type is a membrane proteoglycan. Domain structure of the receptor. J. Biol. Chem., 263: 16984-16991, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 16984-16991
    • Cheifetz, S.1    Andres, J.L.2    Massague, J.3
  • 226
    • 0023948067 scopus 로고
    • The high molecular weight receptor to transforming growth factor-β contains glycosaminoglycan chains
    • Segarini, P. R., and Seyedin, S. M. The high molecular weight receptor to transforming growth factor-β contains glycosaminoglycan chains. J. Biol. Chem., 263: 8366-8370, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 8366-8370
    • Segarini, P.R.1    Seyedin, S.M.2
  • 227
    • 0024538265 scopus 로고
    • Transforming growth factor-β inhibition of epithelial cell proliferation linked to the expression of a 53 kDa membrane receptor
    • Boyd, F. T., and Massague, J. Transforming growth factor-β inhibition of epithelial cell proliferation linked to the expression of a 53 kDa membrane receptor. J. Biol. Chem., 264: 2272-2278, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 2272-2278
    • Boyd, F.T.1    Massague, J.2
  • 228
    • 0023187604 scopus 로고
    • Complete amino acid sequence of human transforming growth factor type β2
    • Marquardt, H., Lioubin, M. N., and Ikeda, T. Complete amino acid sequence of human transforming growth factor type β2. J. Biol. Chem., 262: 12127-12131, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 12127-12131
    • Marquardt, H.1    Lioubin, M.N.2    Ikeda, T.3
  • 229
    • 0023162479 scopus 로고
    • Two forms of transforming growth factor-β distinguished by multipotential haematopoietic progenitor cells
    • Ohta, M., Greenberg, J. S., Anklesaria, P., Bassols, A., and Massague, J. Two forms of transforming growth factor-β distinguished by multipotential haematopoietic progenitor cells. Nature (Lond.), 329: 539-541, 1987.
    • (1987) Nature (Lond.) , vol.329 , pp. 539-541
    • Ohta, M.1    Greenberg, J.S.2    Anklesaria, P.3    Bassols, A.4    Massague, J.5
  • 230
    • 0005862522 scopus 로고
    • Identification of another member of the transforming growth factor type β gene family
    • ten Dijke, P., Hansen, P., Iwata, K. K., Pieler, C., and Foulkes, J. G. Identification of another member of the transforming growth factor type β gene family. Proc. Natl. Acad. Sci. USA, 85: 4717-4719, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4717-4719
    • ten Dijke, P.1    Hansen, P.2    Iwata, K.K.3    Pieler, C.4    Foulkes, J.G.5
  • 232
    • 0023662289 scopus 로고
    • The TGF-β family of growth and differentiation factors
    • Massague, J. The TGF-β family of growth and differentiation factors. Cell, 49:437-438, 1987.
    • (1987) Cell , vol.49 , pp. 437-438
    • Massague, J.1
  • 233
    • 0023654060 scopus 로고
    • Cartilage-inducing factor-β is a unique protein structurally and functionally related to transforming growth factor-β
    • Seyedin, S. M., Segarini, P. R., Rosen, D. M., Thompson, A. Y., Bentz, H., and Graycar, J. Cartilage-inducing factor-β is a unique protein structurally and functionally related to transforming growth factor-β. J. Biol. Chem., 262: 1946-1949, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 1946-1949
    • Seyedin, S.M.1    Segarini, P.R.2    Rosen, D.M.3    Thompson, A.Y.4    Bentz, H.5    Graycar, J.6
  • 234
    • 0022914649 scopus 로고
    • Transforming growth factor-β: a very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells
    • Florini, J. R., Roberts, A. B., Ewton, D. Z., Falen, S. L., Flanders, K. C., and Sporn, M. B. Transforming growth factor-β: a very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells. J. Biol. Chem., 261: 16509-16513, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 16509-16513
    • Florini, J.R.1    Roberts, A.B.2    Ewton, D.Z.3    Falen, S.L.4    Flanders, K.C.5    Sporn, M.B.6
  • 235
    • 0018143340 scopus 로고
    • Density-dependent regulation of growth of BSC-1 cells in cell culture: growth inhibitors formed by the cells
    • Holley, R. W., Armour, R., and Baldwin, J. H. Density-dependent regulation of growth of BSC-1 cells in cell culture: growth inhibitors formed by the cells. Proc. Natl. Acad. Sci. USA, 75: 1864-1866, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1864-1866
    • Holley, R.W.1    Armour, R.2    Baldwin, J.H.3
  • 237
    • 0021720359 scopus 로고
    • Growth inhibitor from BSC-1 cells is closely related to the platelet type β transforming growth factor
    • Tucker, R. F., Shipley, G. D., Moses, H. L., and Holley, R. W. Growth inhibitor from BSC-1 cells is closely related to the platelet type β transforming growth factor. Science (Wash. DC), 226: 705-707, 1984.
    • (1984) Science (Wash. DC) , vol.226 , pp. 705-707
    • Tucker, R.F.1    Shipley, G.D.2    Moses, H.L.3    Holley, R.W.4
  • 238
    • 0023704384 scopus 로고
    • Amino acid sequence of the BSC-1 cell growth inhibitor (polyergin) deduced from the nucleotide sequence of the cDNA
    • Hanks, S. K., Armour, R., Baldwin, J. H., Maldonado, F., Spiess, J., and Holley, R. W. Amino acid sequence of the BSC-1 cell growth inhibitor (polyergin) deduced from the nucleotide sequence of the cDNA. Proc. Natl. Acad. Sci. USA, 85: 79-82, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 79-82
    • Hanks, S.K.1    Armour, R.2    Baldwin, J.H.3    Maldonado, F.4    Spiess, J.5    Holley, R.W.6
  • 239
    • 0023354032 scopus 로고
    • T-cell suppressor factor from human glioblastoma cells is a 12.5-kd protein closely related to transforming growth factor-β
    • Wrann, M., Bodmer, S., de Martin, R., Siepl, C., Hofer-Warbinek, R., Frei, K., Hofer, E., and Fontana, A. T-cell suppressor factor from human glioblastoma cells is a 12.5-kd protein closely related to transforming growth factor-β. EMBO J., 6: 1633-1636, 1987.
    • (1987) EMBO J , vol.6 , pp. 1633-1636
    • Wrann, M.1    Bodmer, S.2    de Martin, R.3    Siepl, C.4    Hofer-Warbinek, R.5    Frei, K.6    Hofer, E.7    Fontana, A.8
  • 240
    • 0023477137 scopus 로고
    • Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-β gene family
    • de Martin, R., Haendler, B., Hofer-Warbinek, R., Gaugitsch, H., Schluse-ner, H., Seifert, J. M., Bodmer, S., Fontana, A., and Hofer, E. Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-β gene family. EMBO J., 6: 3676-3677, 1987.
    • (1987) EMBO J , vol.6 , pp. 3676-3677
    • de Martin, R.1    Haendler, B.2    Hofer-Warbinek, R.3    Gaugitsch, H.4    Schluse-ner, H.5    Seifert, J.M.6    Bodmer, S.7    Fontana, A.8    Hofer, E.9
  • 241
    • 0022380618 scopus 로고
    • Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-β
    • Mason, A. J., Hayflick, J. S., Ling, N., Esch, F., Ueno, N., Ying, S.-Y., Guillemin, R., Niall, H., and Seeburg, P. H. Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-β. Nature (Lond.), 318: 659-663,1985.
    • (1985) Nature (Lond.) , vol.318 , pp. 659-663
    • Mason, A.J.1    Hayflick, J.S.2    Ling, N.3    Esch, F.4    Ueno, N.5    Ying, S.-Y.6    Guillemin, R.7    Niall, H.8    Seeburg, P.H.9
  • 243
    • 0023233755 scopus 로고
    • A transcript from a Drosophila pattern gene predicts a protein homologous to the transforming growth factor-β family
    • Padgett, R. W. St. Johnston, R. D., and Gelbart, W. M. A transcript from a Drosophila pattern gene predicts a protein homologous to the transforming growth factor-β family. Nature (Lond.), 325: 81-84, 1987.
    • (1987) Nature (Lond.) , vol.325 , pp. 81-84
    • Padgett, R.W.S.1    Johnston, R.D.2    Gelbart, W.M.3
  • 244
    • 0023644206 scopus 로고
    • A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGFβ
    • Weeks, D. L., and Melton, D. A. A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGFβ. Cell, 51: 861-867, 1987.
    • (1987) Cell , vol.51 , pp. 861-867
    • Weeks, D.L.1    Melton, D.A.2
  • 245
    • 0346254671 scopus 로고
    • New class of transforming growth factors potentiated by epidermal growth factor: isolation from nonneoplastic tissues
    • Roberts, A. B., Anzano, M. A., Lamb, L. C., Smith, J. M., and Sporn, M. B. New class of transforming growth factors potentiated by epidermal growth factor: isolation from nonneoplastic tissues. Proc. Natl. Acad. Sci. USA, 78: 5339-5343, 1981.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5339-5343
    • Roberts, A.B.1    Anzano, M.A.2    Lamb, L.C.3    Smith, J.M.4    Sporn, M.B.5
  • 246
    • 0023664056 scopus 로고
    • Transforming growth factorβ is a bifunctional regulator of replication and collagen synthesis in osteoblast-enriched cell cultures from fetal rat bone
    • Centrella, M., McCarthy, T. L., and Canalis, E. Transforming growth factorβ is a bifunctional regulator of replication and collagen synthesis in osteoblast-enriched cell cultures from fetal rat bone. J. Biol. Chem., 262: 2869-2874.1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 2869-2874
    • Centrella, M.1    McCarthy, T.L.2    Canalis, E.3
  • 248
    • 0343216494 scopus 로고
    • Type β-transforming growth factor/growth inhibitor stimulates entry of monolayer cultures of AKR-2B cells into S phase after a prolonged prereplicative interval
    • Shipley, G. D., Tucker, R. F., and Moses, H. L. Type β-transforming growth factor/growth inhibitor stimulates entry of monolayer cultures of AKR-2B cells into S phase after a prolonged prereplicative interval. Proc. Natl. Acad. Sci. USA, 82: 4147-4151, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4147-4151
    • Shipley, G.D.1    Tucker, R.F.2    Moses, H.L.3
  • 249
    • 0038641688 scopus 로고
    • Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor-β: a proposed model for indirect mitogenesis involving autocrine activity
    • Leof, E. B., Proper, J. A., Goustin, A. S., Shipley, G. D., DiCorleto, P. E., and Moses, H. L. Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor-β: a proposed model for indirect mitogenesis involving autocrine activity. Proc. Natl. Acad. Sci. USA, 83: 2453-2457, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2453-2457
    • Leof, E.B.1    Proper, J.A.2    Goustin, A.S.3    Shipley, G.D.4    DiCorleto, P.E.5    Moses, H.L.6
  • 250
    • 0024515459 scopus 로고
    • Enhanced jun gene expression is an early genomic response to transforming growth factor-β
    • Pertovaara, L., Sistonen, L., Bos, T. J., Vogt, P. K., Keski-Oja, J., and Alitalo, K. Enhanced jun gene expression is an early genomic response to transforming growth factor-β. Mol. Cell. Biol., 9:1255-1262, 1989.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 1255-1262
    • Pertovaara, L.1    Sistonen, L.2    Bos, T.J.3    Vogt, P.K.4    Keski-Oja, J.5    Alitalo, K.6
  • 251
    • 0024150264 scopus 로고
    • Transforming growth factors in the regulation of malignant cell growth and invasion
    • Keski-Oja, J., Postlethwaite, A. E., and Moses, H. L. Transforming growth factors in the regulation of malignant cell growth and invasion. Cancer Invest., 6: 37-56, 1988.
    • (1988) Cancer Invest , vol.6 , pp. 37-56
    • Keski-Oja, J.1    Postlethwaite, A.E.2    Moses, H.L.3
  • 252
    • 84965834276 scopus 로고
    • Type β transforming growth factor is a growth stimulator and a growth inhibitor
    • J. Feramisco, B. Ozanne, and C. Stiles (eds.) Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Moses, H. L., Tucker, R. F., Leof, E. B., Coffey, R. J. J., Halper, J., and Shipley, G. D. Type β transforming growth factor is a growth stimulator and a growth inhibitor. In: J. Feramisco, B. Ozanne, and C. Stiles (eds.), Cancer Cells, Vol. 3, pp. 65–75. Cold Spring Harbor, NY: Cold Spring Harbor Press, 1985.
    • (1985) Cancer Cells , vol.3 , pp. 65-75
    • Moses, H.L.1    Tucker, R.F.2    Leof, E.B.3    Coffey, R.J.J.4    Halper, J.5    Shipley, G.D.6
  • 254
    • 0022550508 scopus 로고
    • Type β transforming growth factor is the primary differentiation-inducing serum factor for normal human bronchial epithelial cells
    • Masui, T., Wakefield, L. M., Lechner, J. F., LaVeck, M. A., Sporn, M. B., and Harris, C. C. Type β transforming growth factor is the primary differentiation-inducing serum factor for normal human bronchial epithelial cells. Proc. Natl. Acad. Sci. USA, 83: 2438-2442, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2438-2442
    • Masui, T.1    Wakefield, L.M.2    Lechner, J.F.3    LaVeck, M.A.4    Sporn, M.B.5    Harris, C.C.6
  • 255
    • 0011899697 scopus 로고
    • Type β transforming growth factor is an inhibitor of myogenic differentiation
    • Massague, J., Cheifetz, S., Endo, T., and Nadal-Ginard, B. Type β transforming growth factor is an inhibitor of myogenic differentiation. Proc. Natl. Acad. Sci. USA, 83: 8206-8210, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8206-8210
    • Massague, J.1    Cheifetz, S.2    Endo, T.3    Nadal-Ginard, B.4
  • 256
    • 0342542810 scopus 로고
    • Type β transforming growth factor controls the adipogenic differentiation of 3T3 fibroblasts
    • Ignotz, R. A., and Massague, J. Type β transforming growth factor controls the adipogenic differentiation of 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA, 82: 8530-8534, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8530-8534
    • Ignotz, R.A.1    Massague, J.2
  • 258
    • 0023639110 scopus 로고
    • Synergistic induction of mesoderm by FGF and TGFβ and the identification of an mRNA coding for FGF in the early Xenopus embryo
    • Kimelman, D., and Kirschner, M. Synergistic induction of mesoderm by FGF and TGFβ and the identification of an mRNA coding for FGF in the early Xenopus embryo. Cell, 51: 869-877, 1987.
    • (1987) Cell , vol.51 , pp. 869-877
    • Kimelman, D.1    Kirschner, M.2
  • 260
    • 37049184914 scopus 로고
    • Polypeptide transforming growth factors isolated from bovine sources and used for wound healing in vivo
    • Sporn, M. B., Roberts, A. B., Shull, J. H., Smith, J. M., Ward, J. M., and Sodek, J. Polypeptide transforming growth factors isolated from bovine sources and used for wound healing in vivo. Science (Wash. DC), 219: 1329-1331, 1983.
    • (1983) Science (Wash. DC) , vol.219 , pp. 1329-1331
    • Sporn, M.B.1    Roberts, A.B.2    Shull, J.H.3    Smith, J.M.4    Ward, J.M.5    Sodek, J.6
  • 262
    • 0023262932 scopus 로고
    • Accelerated healing of incisional wounds in rats induced by transforming growth factor-β
    • Mustoe, T. A., Pierce, G. F., Thomason, A., Gramates, P., Sporn, M. B., and Deuel, T. F. Accelerated healing of incisional wounds in rats induced by transforming growth factor-β. Science (Wash. DC), 237: 1333–1336, 1987.
    • (1987) Science (Wash. DC) , vol.237 , pp. 1333-1336
    • Mustoe, T.A.1    Pierce, G.F.2    Thomason, A.3    Gramates, P.4    Sporn, M.B.5    Deuel, T.F.6
  • 263
    • 0022998254 scopus 로고
    • Antibodies to the N-terminal portion of cartilage-inducing factor A and transforming growth factor β. Immunohistochemical localization and association with differentiating cells
    • Ellingsworth, L. R., Brennan, J. E., Fok, K., Rosen, D. M., Bentz, H., Piez, K. A., and Seyedin, S. M. Antibodies to the N-terminal portion of cartilage-inducing factor A and transforming growth factor β. Immunohistochemical localization and association with differentiating cells. J. Biol. Chem., 261: 12362-12367, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 12362-12367
    • Ellingsworth, L.R.1    Brennan, J.E.2    Fok, K.3    Rosen, D.M.4    Bentz, H.5    Piez, K.A.6    Seyedin, S.M.7
  • 265
    • 0023025366 scopus 로고
    • Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix
    • Ignotz, R. A., and Massague, J. Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix. J. Biol. Chem., 261: 4337-4345, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 4337-4345
    • Ignotz, R.A.1    Massague, J.2
  • 266
    • 0023654923 scopus 로고
    • Regulation of fibronectin and type I collagen mRNA levels by transforming growth factor-β
    • Ignotz, R. A., Endo, T., and Massague, J. Regulation of fibronectin and type I collagen mRNA levels by transforming growth factor-β. J. Biol. Chem., 262: 6443-6446, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 6443-6446
    • Ignotz, R.A.1    Endo, T.2    Massague, J.3
  • 267
    • 0023251136 scopus 로고
    • Transforming growth factor-β increases steady-state levels of type I procollagen and fibronectin messenger RNAs posttranscriptionally in cultured human dermal fibroblasts
    • Raghow, R., Postlethwaite, A. E., Keski-Oja, J., Moses, H. L., and Kang, H. Transforming growth factor-β increases steady-state levels of type I procollagen and fibronectin messenger RNAs posttranscriptionally in cultured human dermal fibroblasts. J. Clin. Invest., 79: 1285-1288, 1987.
    • (1987) J. Clin. Invest , vol.79 , pp. 1285-1288
    • Raghow, R.1    Postlethwaite, A.E.2    Keski-Oja, J.3    Moses, H.L.4    Kang, H.5
  • 268
    • 0023864574 scopus 로고
    • Regulation of mRNAs for type-1 plasminogen activator inhibitor, fibronectin, and type-1 procollagen by transforming growth factor-β: divergent responses in lung fibroblasts and carcinoma cells
    • Keski-Oja, J., Raghow, R., Sawdey, M., Loskutoff, D. J., Postlethwaite, A. E., Kang, A. H., and Moses, H. L. Regulation of mRNAs for type-1 plasminogen activator inhibitor, fibronectin, and type-1 procollagen by transforming growth factor-β: divergent responses in lung fibroblasts and carcinoma cells. J. Biol. Chem., 263: 3111-3115, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 3111-3115
    • Keski-Oja, J.1    Raghow, R.2    Sawdey, M.3    Loskutoff, D.J.4    Postlethwaite, A.E.5    Kang, A.H.6    Moses, H.L.7
  • 270
    • 0023221985 scopus 로고
    • The effect of transforming growth factor-β on cell proliferation and collagen formation by lung fibroblasts
    • Fine, A., and Goldstein, R. H. The effect of transforming growth factor-β on cell proliferation and collagen formation by lung fibroblasts. J. Biol. Chem., 262: 3897-3902, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 3897-3902
    • Fine, A.1    Goldstein, R.H.2
  • 271
    • 0023834148 scopus 로고
    • Transforming growth factor β regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans
    • Bassols, A., and Massague, J. Transforming growth factor β regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans. J. Biol. Chem., 263: 3039-3045, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 3039-3045
    • Bassols, A.1    Massague, J.2
  • 272
    • 0343292988 scopus 로고
    • Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability
    • Penttinen, R. P., Kobayashi, S., and Bornstein, P. Transforming growth factor β increases mRNA for matrix proteins both in the presence and in the absence of changes in mRNA stability. Proc. Natl. Acad. Sci. USA, 85: 1105-1108,1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1105-1108
    • Penttinen, R.P.1    Kobayashi, S.2    Bornstein, P.3
  • 273
    • 0023633741 scopus 로고
    • Cell adhesion protein receptors as targets for transforming growth factor-β action
    • Ignotz, R. A., and Massague, J. Cell adhesion protein receptors as targets for transforming growth factor-β action. Cell, 51: 189-197,1987.
    • (1987) Cell , vol.51 , pp. 189-197
    • Ignotz, R.A.1    Massague, J.2
  • 274
    • 0024534130 scopus 로고
    • Regulation of cell adhesion receptors by transforming growth factor-β
    • Heino, J., Ignotz, R. A., Hemler, M. E., Crouse, C., and Massague, J. Regulation of cell adhesion receptors by transforming growth factor-β. J. Biol. Chem., 264: 380-388, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 380-388
    • Heino, J.1    Ignotz, R.A.2    Hemler, M.E.3    Crouse, C.4    Massague, J.5
  • 275
    • 0023666065 scopus 로고
    • Integrins: a family of cell surface receptors
    • Hynes, R. O. Integrins: a family of cell surface receptors. Cell, 48: 549–554, 1987.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 276
    • 0021827185 scopus 로고
    • Regulation of plasminogen activator activity in human fibroblastic cells by fibrosarcoma cell-derived factors
    • Saksela, O., Laiho, M., and Keski-Oja, J. Regulation of plasminogen activator activity in human fibroblastic cells by fibrosarcoma cell-derived factors. Cancer Res., 45: 2314-2319, 1985.
    • (1985) Cancer Res , vol.45 , pp. 2314-2319
    • Saksela, O.1    Laiho, M.2    Keski-Oja, J.3
  • 277
    • 0023919547 scopus 로고
    • Modulation of extracellular proteolytic activity and anchorage-independent growth of cultured cells by sarcoma cell-derived factors. Relationships to transforming growth factor-β
    • Laiho, M. Modulation of extracellular proteolytic activity and anchorage-independent growth of cultured cells by sarcoma cell-derived factors. Relationships to transforming growth factor-β. Exp. Cell Res., 176: 297–308, 1988.
    • (1988) Exp. Cell Res , vol.176 , pp. 297-308
    • Laiho, M.1
  • 278
    • 0022530451 scopus 로고
    • Transforming growth factor-β alters plasminogen activator activity in human skin fibroblasts
    • Laiho, M., Saksela, O., and Keski-Oja, J. Transforming growth factor-β alters plasminogen activator activity in human skin fibroblasts. Exp. Cell Res., 164: 399-407, 1986.
    • (1986) Exp. Cell Res , vol.164 , pp. 399-407
    • Laiho, M.1    Saksela, O.2    Keski-Oja, J.3
  • 279
    • 0023881278 scopus 로고
    • Regulation of the synthesis and activity of urokinase plasminogen activator in A549 human lung carcinoma cells by transforming growth factor-β
    • Keski-Oja, J., Blasi, F., Leof, E. B., and Moses, H. L. Regulation of the synthesis and activity of urokinase plasminogen activator in A549 human lung carcinoma cells by transforming growth factor-β. J. Cell Biol., 106: 451-459,1988.
    • (1988) J. Cell Biol , vol.106 , pp. 451-459
    • Keski-Oja, J.1    Blasi, F.2    Leof, E.B.3    Moses, H.L.4
  • 280
    • 0021064318 scopus 로고
    • 35S]methionine into proteins secreted by African green monkey (BSC-1) cells
    • 35S]methionine into proteins secreted by African green monkey (BSC-1) cells. Proc. Natl. Acad. Sci. USA, 80: 5636-5640, 1983.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5636-5640
    • Nilsen-Hamilton, M.1    Holley, R.W.2
  • 281
    • 0023654083 scopus 로고
    • Specific induction of secreted proteins by transforming growth factor-β and 12-O-tetradecanoylphorbol-13-acetate
    • Thalacker, F. W., and Nilsen-Hamilton, M. Specific induction of secreted proteins by transforming growth factor-β and 12-O-tetradecanoylphorbol-13-acetate. J. Biol. Chem., 262: 2283-2290, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 2283-2290
    • Thalacker, F.W.1    Nilsen-Hamilton, M.2
  • 282
    • 0022969191 scopus 로고
    • Opposite and selective effects of epidermal growth factor and human platelet transforming growth factor-β on the production of secreted proteins by murine 3T3 cells and human fibroblasts
    • Chiang, C.-P., and Nilsen-Hamilton, M. Opposite and selective effects of epidermal growth factor and human platelet transforming growth factor-β on the production of secreted proteins by murine 3T3 cells and human fibroblasts. J. Biol. Chem., 261: 10478-10481, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 10478-10481
    • Chiang, C.-P.1    Nilsen-Hamilton, M.2
  • 283
    • 0023296095 scopus 로고
    • Mesosecrin: a secreted glycoprotein produced in abundance by human mesothelial, endothelial, and kidney epithelial cells in culture
    • Rheinwald, J. G., Jorgensen, J. L., Hahn, W. C., Terpstra, A. J., O’Connell, T. M., and Plummer, K. K. Mesosecrin: a secreted glycoprotein produced in abundance by human mesothelial, endothelial, and kidney epithelial cells in culture. J. Cell Biol., 104: 263-275, 1987.
    • (1987) J. Cell Biol , vol.104 , pp. 263-275
    • Rheinwald, J.G.1    Jorgensen, J.L.2    Hahn, W.C.3    Terpstra, A.J.4    O’Connell, T.M.5    Plummer, K.K.6
  • 284
    • 0023337921 scopus 로고
    • Transforming growth factor-β is a strong and fast acting positive regulator of the level of type-1 plasminogen activator inhibitor mRNA in WI-38 human lung fibroblasts
    • Lund, L. R., Riccio, A., Andreasen, P. A., Nielsen, L. S., Kristensen, P., Laiho, M., Saksela, O., Blasi, F., and Dano, K. Transforming growth factor-β is a strong and fast acting positive regulator of the level of type-1 plasminogen activator inhibitor mRNA in WI-38 human lung fibroblasts. EMBO J., 6: 1281-1286, 1987.
    • (1987) EMBO J , vol.6 , pp. 1281-1286
    • Lund, L.R.1    Riccio, A.2    Andreasen, P.A.3    Nielsen, L.S.4    Kristensen, P.5    Laiho, M.6    Saksela, O.7    Blasi, F.8    Dano, K.9
  • 285
    • 0023256210 scopus 로고
    • Plasminogen activator inhibitor type 1 biosynthesis and human mRNA level are increased by dexamethasone in human fibrosarcoma cells
    • Andreasen, P. A., Pyke, C., Riccio, A., Kristensen, P., Nielsen, L. S., Lund, L. R., Blasi, F., and Dano, K. Plasminogen activator inhibitor type 1 biosynthesis and human mRNA level are increased by dexamethasone in human fibrosarcoma cells. Mol. Cell. Biol., 7: 3021-3025,1987.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 3021-3025
    • Andreasen, P.A.1    Pyke, C.2    Riccio, A.3    Kristensen, P.4    Nielsen, L.S.5    Lund, L.R.6    Blasi, F.7    Dano, K.8
  • 286
    • 0023888941 scopus 로고
    • The regulatory region of the human plasminogen activator inhibitor type-1 (PA1-1) gene
    • Riccio, A., Lund, L. R., Sartorio, R., Lania, A., Andreasen, P. A., Dano, K., and Blasi, F. The regulatory region of the human plasminogen activator inhibitor type-1 (PA1-1) gene. Nucl. Acids Res., 16: 2805-2824, 1988.
    • (1988) Nucl. Acids Res , vol.16 , pp. 2805-2824
    • Riccio, A.1    Lund, L.R.2    Sartorio, R.3    Lania, A.4    Andreasen, P.A.5    Dano, K.6    Blasi, F.7
  • 287
    • 0023856558 scopus 로고
    • A nuclear factor 1 binding site mediates the transcriptional activation of a type I collagen promoter by transforming growth factor-β
    • Rossi, P., Karsenty, G., Roberts, A. B., Roche, N. S., Sporn, M. B., and de Crombrugghe, B. A nuclear factor 1 binding site mediates the transcriptional activation of a type I collagen promoter by transforming growth factor-β. Cell, 52: 405-414, 1988.
    • (1988) Cell , vol.52 , pp. 405-414
    • Rossi, P.1    Karsenty, G.2    Roberts, A.B.3    Roche, N.S.4    Sporn, M.B.5    de Crombrugghe, B.6
  • 288
    • 0020567533 scopus 로고
    • A polypeptide secreted by transformed cells that modulates human plasminogen activator production
    • Davies, R. L., Rifkin, D. B., Tepper, R., Miller, A., and Kucherlapati, R. A polypeptide secreted by transformed cells that modulates human plasminogen activator production. Science (Wash. DC), 221: 171-173, 1983.
    • (1983) Science (Wash. DC) , vol.221 , pp. 171-173
    • Davies, R.L.1    Rifkin, D.B.2    Tepper, R.3    Miller, A.4    Kucherlapati, R.5
  • 290
    • 0019492908 scopus 로고
    • Role of collagenous matrices in the adhesion and growth of cells
    • Kleinman, H. K., Klebe, R. J., and Martin, G. R. Role of collagenous matrices in the adhesion and growth of cells. J. Cell Biol., 88: 473–485, 1981.
    • (1981) J. Cell Biol , vol.88 , pp. 473-485
    • Kleinman, H.K.1    Klebe, R.J.2    Martin, G.R.3
  • 291
    • 0020437446 scopus 로고
    • Pericellular matrix and malignant transformation
    • Alitalo, K., and Vaheri, A. Pericellular matrix and malignant transformation. Adv. Cancer Res., 37: 111–158, 1982.
    • (1982) Adv. Cancer Res , vol.37 , pp. 111-158
    • Alitalo, K.1    Vaheri, A.2
  • 292
    • 0022656975 scopus 로고
    • Tumor invasion and metastases-role of the extracellular matrix
    • Liotta, L. A. Tumor invasion and metastases-role of the extracellular matrix. Cancer Res., 46: 1-7, 1986.
    • (1986) Cancer Res , vol.46 , pp. 1-7
    • Liotta, L.A.1
  • 293
    • 0017145632 scopus 로고
    • Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells
    • Quigley, J. P. Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells. J. Cell Biol., 71: 472-486, 1976.
    • (1976) J. Cell Biol , vol.71 , pp. 472-486
    • Quigley, J.P.1
  • 294
    • 0021248709 scopus 로고
    • Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites
    • Chen, W.-T., Olden, K., Bernard, B. A., and Chu, F.-F. Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J. Cell Biol., 98: 1546-1555, 1984.
    • (1984) J. Cell Biol , vol.98 , pp. 1546-1555
    • Chen, W.-T.1    Olden, K.2    Bernard, B.A.3    Chu, F.-F.4
  • 295
    • 0023506166 scopus 로고
    • Proteolytic degradation of extracellular matrix in tumor invasion
    • Tryggvason, K., Hoyhtya, M., and Salo, T. Proteolytic degradation of extracellular matrix in tumor invasion. Biochim. Biophys. Acta, 907: 191-217,1987.
    • (1987) Biochim. Biophys. Acta , vol.907 , pp. 191-217
    • Tryggvason, K.1    Hoyhtya, M.2    Salo, T.3
  • 296
    • 0023667821 scopus 로고
    • Fibronectin-degrading proteases from the membranes of transformed cells
    • Chen, J.-M., and Chen, W.-T. Fibronectin-degrading proteases from the membranes of transformed cells. Cell, 48: 193-203, 1987.
    • (1987) Cell , vol.48 , pp. 193-203
    • Chen, J.-M.1    Chen, W.-T.2
  • 297
    • 0017367477 scopus 로고
    • Endogenous activation of latent collagenase by rheumatoid synovial cells
    • Werb, Z., Mainardi, C. L., Vater, C. A., and Harris, E. D. Endogenous activation of latent collagenase by rheumatoid synovial cells. N. Engl. J. Med., 296: 1017-1023, 1977.
    • (1977) N. Engl. J. Med , vol.296 , pp. 1017-1023
    • Werb, Z.1    Mainardi, C.L.2    Vater, C.A.3    Harris, E.D.4
  • 298
    • 0019481008 scopus 로고
    • Rat mammary carcinoma cells secrete active collagenase and activate latent enzyme in the stroma via plasminogen activator
    • O’Grady, R. L., Upfold, L. I., and Stephens, R. W. Rat mammary carcinoma cells secrete active collagenase and activate latent enzyme in the stroma via plasminogen activator. Int. J. Cancer, 28: 509-515, 1981.
    • (1981) Int. J. Cancer , vol.28 , pp. 509-515
    • O’Grady, R.L.1    Upfold, L.I.2    Stephens, R.W.3
  • 299
    • 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
  • 300
    • 0023597328 scopus 로고
    • Extracellular matrix of cultured bovine aortic endothelial cells contains functionally active type 1 plasminogen activator inhibitor
    • Mimuro, J., Schleef, R. R., and Loskutoff, D. J. Extracellular matrix of cultured bovine aortic endothelial cells contains functionally active type 1 plasminogen activator inhibitor. Blood, 70: 721-728, 1987.
    • (1987) Blood , vol.70 , pp. 721-728
    • Mimuro, J.1    Schleef, R.R.2    Loskutoff, D.J.3
  • 301
    • 0023572111 scopus 로고
    • Plasminogen activator inhibitor is associated with the extracellular matrix of cultured bovine smooth muscle cells
    • Knudsen, B. S., Harpel, P. C., and Nachman, R. L. Plasminogen activator inhibitor is associated with the extracellular matrix of cultured bovine smooth muscle cells. J. Clin. Invest., 80: 1082-1089, 1987.
    • (1987) J. Clin. Invest , vol.80 , pp. 1082-1089
    • Knudsen, B.S.1    Harpel, P.C.2    Nachman, R.L.3
  • 302
    • 0023553695 scopus 로고
    • Association of a plasminogen activator inhibitor (PAI-1)with the growth substratum and membrane of human endothelial cells
    • Levin, E. G., and Santell, L. Association of a plasminogen activator inhibitor (PAI-1)with the growth substratum and membrane of human endothelial cells. J. Cell Biol., 105: 2543-2549, 1987.
    • (1987) J. Cell Biol , vol.105 , pp. 2543-2549
    • Levin, E.G.1    Santell, L.2
  • 303
    • 0023906370 scopus 로고
    • Interaction of tissue-type plasminogen activator and plasminogen activator inhibitor 1 on the surface of endothelial cells
    • Sakata, Y., Okada, M., Noro, A., and Matsuda, M. Interaction of tissue-type plasminogen activator and plasminogen activator inhibitor 1 on the surface of endothelial cells. J. Biol. Chem., 263: 1960-1969, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 1960-1969
    • Sakata, Y.1    Okada, M.2    Noro, A.3    Matsuda, M.4
  • 304
    • 0019124422 scopus 로고
    • Specific effects of fibronectin-releasing peptides on the extracellular matrices of cultured human fibroblasts
    • Keski-Oja, J., and Todaro, G. J. Specific effects of fibronectin-releasing peptides on the extracellular matrices of cultured human fibroblasts. Cancer Res., 40: 4722-4727, 1980.
    • (1980) Cancer Res , vol.40 , pp. 4722-4727
    • Keski-Oja, J.1    Todaro, G.J.2
  • 305
    • 0020078563 scopus 로고
    • The cellular target for the plasminogen activator, urokinase, in human fibroblasts—66.000 dalton protein
    • Keski-Oja, J., and Vaheri, A. The cellular target for the plasminogen activator, urokinase, in human fibroblasts—66.000 dalton protein. Biochim. Biophys. Acta, 720: 141-146, 1982.
    • (1982) Biochim. Biophys. Acta , vol.720 , pp. 141-146
    • Keski-Oja, J.1    Vaheri, A.2
  • 306
    • 0010469194 scopus 로고
    • Limited cleavage of cellular fibronectin by plasminogen activator purified from transformed cells
    • Quigley, J. P., Gold, L. I., Schwimmer, R., and Sullivan, L. Limited cleavage of cellular fibronectin by plasminogen activator purified from transformed cells. Proc. Natl. Acad. Sci. USA, 84: 2776-2780, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2776-2780
    • Quigley, J.P.1    Gold, L.I.2    Schwimmer, R.3    Sullivan, L.4
  • 307
    • 0021059131 scopus 로고
    • Inhibition by bovine endothelial cells of degradation by HT-1080 fibrosarcoma cells of extracellular matrix proteins
    • Heisel, M., Laug, W. E., and Jones, P. A. Inhibition by bovine endothelial cells of degradation by HT-1080 fibrosarcoma cells of extracellular matrix proteins. J. Natl. Cancer Inst., 71: 1183-1187, 1983.
    • (1983) J. Natl. Cancer Inst , vol.71 , pp. 1183-1187
    • Heisel, M.1    Laug, W.E.2    Jones, P.A.3
  • 308
    • 0023944278 scopus 로고
    • Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: colocalization of cell surface urokinase with vinculin
    • Hebert, C. A., and Baker, J. B. Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: colocalization of cell surface urokinase with vinculin. J. Cell Biol., 106: 1241-1247, 1988.
    • (1988) J. Cell Biol , vol.106 , pp. 1241-1247
    • Hebert, C.A.1    Baker, J.B.2
  • 309
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta, L. A., Tryggvason, K., Garbisa, S., Hart, I., Foltz, C. M., and Shafie, S. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature (Lond.), 284: 67-68, 1980.
    • (1980) Nature (Lond.) , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 310
    • 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
  • 311
    • 0022085068 scopus 로고
    • Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts
    • Matrisian, L. M., Glaichenhaus, N., Gesnel, M.-C., and Breathnach, R. Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts. EMBO J., 4: 1435-1440, 1985.
    • (1985) EMBO J , vol.4 , pp. 1435-1440
    • Matrisian, L.M.1    Glaichenhaus, N.2    Gesnel, M.-C.3    Breathnach, R.4
  • 312
    • 0022982416 scopus 로고
    • Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts
    • Matrisian, L. M., Leroy, P., Ruhlmann, C., Gesnel, M.-C., and Breathnach, R. Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts. Mol. Cell. Biol., 6: 1679–1686, 1986.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 1679-1686
    • Matrisian, L.M.1    Leroy, P.2    Ruhlmann, C.3    Gesnel, M.-C.4    Breathnach, R.5
  • 313
    • 2442724379 scopus 로고
    • Transforming growth factor-β modulates the expression of collagenase and metalloproteinase inhibitor
    • Edwards, D. R., Murphy, G., Reynolds, J. J., Whitham, S. E., Docherty, A. J. P., Angel, P., and Heath, J. K. Transforming growth factor-β modulates the expression of collagenase and metalloproteinase inhibitor. EMBO J., 6: 1899-1904,1987.
    • (1987) EMBO J , vol.6 , pp. 1899-1904
    • Edwards, D.R.1    Murphy, G.2    Reynolds, J.J.3    Whitham, S.E.4    Docherty, A.J.P.5    Angel, P.6    Heath, J.K.7
  • 315
    • 0023947728 scopus 로고
    • Transcriptional modulation of transin gene expression by epidermal growth factor and transforming growth factor beta
    • Machida, C. M., Muldoon, L. L., Rodland, K. D., and Magun, B. E. Transcriptional modulation of transin gene expression by epidermal growth factor and transforming growth factor beta. Mol. Cell. Biol., 8: 2479-2483, 1988.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 2479-2483
    • Machida, C.M.1    Muldoon, L.L.2    Rodland, K.D.3    Magun, B.E.4
  • 316
    • 0021865197 scopus 로고
    • Induction of collagenase secretion in human fibroblast cultures by growth promoting factors
    • Chua, C. C., Geiman, D. E., Keller, G. H., and Ladda, R. L. Induction of collagenase secretion in human fibroblast cultures by growth promoting factors. J. Biol. Chem., 260: 5213-5216, 1985.
    • (1985) J. Biol. Chem , vol.260 , pp. 5213-5216
    • Chua, C.C.1    Geiman, D.E.2    Keller, G.H.3    Ladda, R.L.4
  • 317
    • 0017884232 scopus 로고
    • Transformation-dependent secretion of a low molecular weight protein by murine fibroblasts
    • Gottesman, M. M. Transformation-dependent secretion of a low molecular weight protein by murine fibroblasts. Proc. Natl. Acad. Sci. USA, 75: 2767-2771, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2767-2771
    • Gottesman, M.M.1
  • 319
    • 0024534977 scopus 로고
    • Independent regulation of collagenase, 72-kDA progelatinase, and metalloendoproteinase inhibitor expression in human fibroblasts by transforming growth factor β
    • Overall, C. M., Wrana, J. L., and Sodek, J. Independent regulation of collagenase, 72-kDA progelatinase, and metalloendoproteinase inhibitor expression in human fibroblasts by transforming growth factor β. J. Biol. Chem. 264: 1860-1869, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 1860-1869
    • Overall, C.M.1    Wrana, J.L.2    Sodek, J.3
  • 320
    • 0005911475 scopus 로고
    • Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix
    • Vlodavsky, I., Folkman, J., Sullivan, R., Fridman, R., Ishai-Michael, R., Sasse, J., and Klagsbrun, M. Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix. Proc. Natl. Acad. Sci. USA, 84: 2292-2296, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2292-2296
    • Vlodavsky, I.1    Folkman, J.2    Sullivan, R.3    Fridman, R.4    Ishai-Michael, R.5    Sasse, J.6    Klagsbrun, M.7
  • 321
    • 0023095122 scopus 로고
    • Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: implications for a role of heparinase-like enzymes in the neovascular response
    • Baird, A., and Ling, N. Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: implications for a role of heparinase-like enzymes in the neovascular response. Biochem. Biophys. Res. Commun., 142: 428-435, 1987.
    • (1987) Biochem. Biophys. Res. Commun , vol.142 , pp. 428-435
    • Baird, A.1    Ling, N.2
  • 322
    • 0023687871 scopus 로고
    • Endothelial cell-derived heparan sulfate binds basic fibroblast and protects it from proteolytic degradation
    • Saksela, O., Moscatelli, D., Sommer, A., and Rifkin, D. B. Endothelial cell-derived heparan sulfate binds basic fibroblast and protects it from proteolytic degradation. J. Cell Biol., 107: 743-751, 1988.
    • (1988) J. Cell Biol , vol.107 , pp. 743-751
    • Saksela, O.1    Moscatelli, D.2    Sommer, A.3    Rifkin, D.B.4
  • 323
  • 324
    • 0023104031 scopus 로고
    • Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor β
    • Postlethwaite, A. E., Keski-Oja, J., Moses, H. L., and Kang, A. H. Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor β. J. Exp. Med., 165: 251-256, 1987.
    • (1987) J. Exp. Med , vol.165 , pp. 251-256
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Moses, H.L.3    Kang, A.H.4
  • 326
    • 0024278715 scopus 로고
    • Transforming growth factor β1 positively regulates its own expression in normal and transformed cells
    • Van Obberghen-Schilling, E., Roche, N. S., Flanders, K. C., Sporn, M. B., and Roberts, A. B. Transforming growth factor β1 positively regulates its own expression in normal and transformed cells. J. Biol. Chem., 263: 7741-7746, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 7741-7746
    • Van Obberghen-Schilling, E.1    Roche, N.S.2    Flanders, K.C.3    Sporn, M.B.4    Roberts, A.B.5
  • 327
    • 0022538577 scopus 로고
    • Inhibition of endothelial cell proliferation by type β-transforming growth factor: interactions with acidic and basic fibroblast growth factors
    • Baird, A., and Durkin, T. Inhibition of endothelial cell proliferation by type β-transforming growth factor: interactions with acidic and basic fibroblast growth factors. Biochem. Biophys. Res. Commun., 138: 476-482, 1986.
    • (1986) Biochem. Biophys. Res. Commun , vol.138 , pp. 476-482
    • Baird, A.1    Durkin, T.2
  • 329
    • 0022492518 scopus 로고
    • Inhibition of endothelial regeneration by type-β transforming growth factor from platelets
    • Heimark, R. L., Twardzik, D. R., and Schwartz, S. M. Inhibition of endothelial regeneration by type-β transforming growth factor from platelets. Science (Wash. DC), 233: 1078-1080, 1986.
    • (1986) Science (Wash. DC) , vol.233 , pp. 1078-1080
    • Heimark, R.L.1    Twardzik, D.R.2    Schwartz, S.M.3
  • 330
    • 0023623241 scopus 로고
    • TGFβ-induction of endothelial cell proliferation: alteration of EGF binding and EGF-induced growth-regulatory (competence) gene expression
    • Takehara, K., LeRoy, E. C., and Grotendorst, G. R. TGFβ-induction of endothelial cell proliferation: alteration of EGF binding and EGF-induced growth-regulatory (competence) gene expression. Cell, 49: 415-422, 1987.
    • (1987) Cell , vol.49 , pp. 415-422
    • Takehara, K.1    LeRoy, E.C.2    Grotendorst, G.R.3
  • 332
    • 4243418379 scopus 로고
    • Transforming growth factor-β as an immunoregulatory molecule
    • McCartney-Francis, N., Mizel, D., Wongh, H., Wahl, L., and Wahl, S. Transforming growth factor-β as an immunoregulatory molecule. FASEB J., 2: A875, 1988.
    • (1988) FASEB J , vol.2 , pp. A875
    • McCartney-Francis, N.1    Mizel, D.2    Wongh, H.3    Wahl, L.4    Wahl, S.5
  • 333
    • 0023940794 scopus 로고
    • Latent high molecular weight complex of transforming growth factor 01. Purification from human platelets and structural characterization
    • Miyazono, K., Heilman, U., Wernstedt, C., and Heldin, C.-H. Latent high molecular weight complex of transforming growth factor 01. Purification from human platelets and structural characterization. J. Biol. Chem., 263: 6407-6415, 1988.
    • (1988) J. Biol. Chem , vol.263 , pp. 6407-6415
    • Miyazono, K.1    Heilman, U.2    Wernstedt, C.3    Heldin, C.-H.4
  • 334
    • 0023429489 scopus 로고
    • Type 1 transforming growth factor-β: amplified expression and secretion of mature and precursor polypeptide in Chinese hamster ovary cells
    • Gentry, L. E., Webb, N. R., Lim, G. J., Brunner, A. M., Ranchalis, J. E., Twardzik, D. R., Lioubin, M. N., Marquardt, H., and Purchio, A. F. Type 1 transforming growth factor-β: amplified expression and secretion of mature and precursor polypeptide in Chinese hamster ovary cells. Mol. Cell. Biol., 7: 4318-4327, 1987.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 4318-4327
    • Gentry, L.E.1    Webb, N.R.2    Lim, G.J.3    Brunner, A.M.4    Ranchalis, J.E.5    Twardzik, D.R.6    Lioubin, M.N.7    Marquardt, H.8    Purchio, A.F.9
  • 335
    • 0023628526 scopus 로고
    • Alterations in the synthesis of a fibroblast surface associated 35 Kd protein modulates the binding of somatomedin-C/insulin-like growth factor I
    • Clemmons, D. R., Han, V. K. M., Elgin, R. G., and D’Ercole, A. J. Alterations in the synthesis of a fibroblast surface associated 35 Kd protein modulates the binding of somatomedin-C/insulin-like growth factor I. Mol. Endocrinol., 1: 339-347, 1987.
    • (1987) Mol. Endocrinol , vol.1 , pp. 339-347
    • Clemmons, D.R.1    Han, V.K.M.2    Elgin, R.G.3    D’Ercole, A.J.4
  • 336
    • 0342476502 scopus 로고
    • An insulin-like growth factor (IGF) binding protein enhances the biologic response to IGF-I
    • Elgin, R. G., Busby, W. H., Jr., and Clemmons, D. R. An insulin-like growth factor (IGF) binding protein enhances the biologic response to IGF-I. Proc. Natl. Acad. Sci. USA, 84: 3254-3258, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3254-3258
    • Elgin, R.G.1    Busby, W.H.2    Clemmons, D.R.3
  • 337
    • 0024504371 scopus 로고
    • In vitro angiogenesis of the human amniotic membrane: requirement for basic fibroblast growth factor-induced proteinases
    • Mignotti, P., Tsubai, R. Robbins, E., and Rifkin, D. B. In vitro angiogenesis of the human amniotic membrane: requirement for basic fibroblast growth factor-induced proteinases. J. Cell. Biol., 108: 671-682, 1989.
    • (1989) J. Cell. Biol , vol.108 , pp. 671-682
    • Mignotti, P.1    Tsubai, R.2    Robbins, E.3    Rifkin, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.