메뉴 건너뛰기




Volumn 246, Issue 1, 1999, Pages 233-242

Exposure to lysosomotropic amines and protease inhibitors retard corneal endothelial cell migration along the natural basement membrane during wound repair

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; ANTIPAIN; CHLOROQUINE; LEUPEPTIN; LYSOSOMOTROPIC AMINE DERIVATIVE; METALLOPROTEINASE INHIBITOR; METHYLAMINE; PHOSPHORAMIDON; PROPYLAMINE; PROTEINASE INHIBITOR; SOYBEAN TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0033540265     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4298     Document Type: Article
Times cited : (8)

References (81)
  • 1
    • 0018095218 scopus 로고
    • Studies on corneal endothelial growth and repair. I. Microfluorometric and autoradiographic analyses of DNA synthesis, mitosis and amitosis following freeze injury
    • Gordon S. R., Rothstein H. Studies on corneal endothelial growth and repair. I. Microfluorometric and autoradiographic analyses of DNA synthesis, mitosis and amitosis following freeze injury. Metab. Ophthamol. 2:1978;57-63.
    • (1978) Metab. Ophthamol. , vol.2 , pp. 57-63
    • Gordon, S.R.1    Rothstein, H.2
  • 2
    • 0029764582 scopus 로고    scopus 로고
    • Expression of cell cycle-associated proteins in human and rabbit corneal endotheliumin situ
    • Joyce N. C., Navon S. E., Roy S., Zieske J. D. Expression of cell cycle-associated proteins in human and rabbit corneal endotheliumin situ. Invest. Ophthalmol. Vis. Sci. 37:1996;1566-1575.
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 1566-1575
    • Joyce, N.C.1    Navon, S.E.2    Roy, S.3    Zieske, J.D.4
  • 5
    • 0020061870 scopus 로고
    • Studies on corneal endothelial growth and repair. III. Effects of DNA and RNA synthesis inhibitors upon restoration of transparency following injury
    • Gordon S. R., Rothstein H. Studies on corneal endothelial growth and repair. III. Effects of DNA and RNA synthesis inhibitors upon restoration of transparency following injury. Ophthal. Res. 14:1982;195-209.
    • (1982) Ophthal. Res. , vol.14 , pp. 195-209
    • Gordon, S.R.1    Rothstein, H.2
  • 6
    • 0020793271 scopus 로고
    • Studies on corneal endothelial growth and repair. IV. Changes in the surface during cell division as revealed by scanning electron microscopy
    • Gordon S. R., Rothstein H., Harding C. V. Studies on corneal endothelial growth and repair. IV. Changes in the surface during cell division as revealed by scanning electron microscopy. Eur. J. Cell Biol. 31:1983;26-33.
    • (1983) Eur. J. Cell Biol. , vol.31 , pp. 26-33
    • Gordon, S.R.1    Rothstein, H.2    Harding, C.V.3
  • 8
    • 0023912642 scopus 로고
    • Changes in the distribution of extracellular matrix proteins during wound repair in corneal endothelium
    • Gordon S. R. Changes in the distribution of extracellular matrix proteins during wound repair in corneal endothelium. J. Histochem. Cytochem. 36:1988;409-416.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 409-416
    • Gordon, S.R.1
  • 9
    • 0024536715 scopus 로고
    • Ultrastructural immunocytochemical localization of fibronectin deposition during corneal endothelial wound repair: Evidence for cytoskeletal involvement
    • Sabet M. D., Gordon S. R. Ultrastructural immunocytochemical localization of fibronectin deposition during corneal endothelial wound repair: Evidence for cytoskeletal involvement. Biol. Cell. 65:1989;171-179.
    • (1989) Biol. Cell , vol.65 , pp. 171-179
    • Sabet, M.D.1    Gordon, S.R.2
  • 10
    • 0025066916 scopus 로고
    • Role of the cytoskeleton during injury-induced cell migration in corneal endothelium
    • Gordon S. R., Staley C. A. Role of the cytoskeleton during injury-induced cell migration in corneal endothelium. Cell Motil. Cytoskel. 16:1990;47-57.
    • (1990) Cell Motil. Cytoskel. , vol.16 , pp. 47-57
    • Gordon, S.R.1    Staley, C.A.2
  • 11
    • 0027328929 scopus 로고
    • Actin filament organization during endothelial wound healing in the rabbit cornea: Comparison between transcorneal freeze and mechanical scrape injuries
    • Ichijima H., Petroll W. M., Barry P. A., Andrews P. M., Dai M., Cavanagh H. D., Jester J. V. Actin filament organization during endothelial wound healing in the rabbit cornea: Comparison between transcorneal freeze and mechanical scrape injuries. Invest. Ophthalmol. Vis. Sci. 34:1993;2803-2812.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 2803-2812
    • Ichijima, H.1    Petroll, W.M.2    Barry, P.A.3    Andrews, P.M.4    Dai, M.5    Cavanagh, H.D.6    Jester, J.V.7
  • 12
    • 0030670046 scopus 로고    scopus 로고
    • Inhibition of cytoskeletal reorganization stimulates actin and tubulin syntheses during injury-induced cell migration in the corneal endothelium
    • Gordon S. R., Buxar R. B. Inhibition of cytoskeletal reorganization stimulates actin and tubulin syntheses during injury-induced cell migration in the corneal endothelium. J. Cell. Biochem. 67:1997;409-421.
    • (1997) J. Cell. Biochem. , vol.67 , pp. 409-421
    • Gordon, S.R.1    Buxar, R.B.2
  • 13
    • 0020631281 scopus 로고
    • Basement membrane collagen: Degradation by migrating endothelial cells
    • Kalebic T., Garbisa S., Glaser B., Liotta L. A. Basement membrane collagen: Degradation by migrating endothelial cells. Science. 221:1983;281-283.
    • (1983) Science , vol.221 , pp. 281-283
    • Kalebic, T.1    Garbisa, S.2    Glaser, B.3    Liotta, L.A.4
  • 14
    • 0023946446 scopus 로고
    • Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialization in vivo
    • Grøndahl-Hansen J., Lund L. R., Ralfkiær E., Ottevanger V., Danø K. Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialization in vivo. J. Invest. Dermatol. 90:1988;790-795.
    • (1988) J. Invest. Dermatol. , vol.90 , pp. 790-795
    • Grøndahl-Hansen, J.1    Lund, L.R.2    Ralfkiær, E.3    Ottevanger, V.4    Danø, K.5
  • 15
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J. F. Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:1991;2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner J.F., Jr.1
  • 16
    • 0027308877 scopus 로고
    • Stromal fibroblasts synthesize collagenase and stromelysin during long-term tissue remodeling
    • Girad M. T., Matsubara M., Kublin C., Tessier M. J., Cintron C., Fini M. E. Stromal fibroblasts synthesize collagenase and stromelysin during long-term tissue remodeling. J. Cell Sci. 104:1993;1001-1011.
    • (1993) J. Cell Sci. , vol.104 , pp. 1001-1011
    • Girad, M.T.1    Matsubara, M.2    Kublin, C.3    Tessier, M.J.4    Cintron, C.5    Fini, M.E.6
  • 18
    • 0029911386 scopus 로고    scopus 로고
    • The role of plasminogen, plasminogen activators, and matrix metalloproteinases in primate arterial smooth muscle cell migration
    • Kenagy R. D., Vergel S., Mattsson E., Bendeck M., Reidy M. A., Clowes A. W. The role of plasminogen, plasminogen activators, and matrix metalloproteinases in primate arterial smooth muscle cell migration. Arterioscler. Thromb. Vasc. Biol. 16:1996;1373-1382.
    • (1996) Arterioscler. Thromb. Vasc. Biol. , vol.16 , pp. 1373-1382
    • Kenagy, R.D.1    Vergel, S.2    Mattsson, E.3    Bendeck, M.4    Reidy, M.A.5    Clowes, A.W.6
  • 19
    • 0029965936 scopus 로고    scopus 로고
    • Temporal study of the activity of matrix metalloproteinases and their endogenous inhibitors during wound repair
    • Moses M. A., Marikovsky M., Harper J. W., Vogt P., Eriksson E., Klagsbrun M., Langer R. Temporal study of the activity of matrix metalloproteinases and their endogenous inhibitors during wound repair. J. Cell. Biochem. 60:1996;379-386.
    • (1996) J. Cell. Biochem. , vol.60 , pp. 379-386
    • Moses, M.A.1    Marikovsky, M.2    Harper, J.W.3    Vogt, P.4    Eriksson, E.5    Klagsbrun, M.6    Langer, R.7
  • 20
    • 0022608745 scopus 로고
    • Release of plasminogen activator by cultured corneal epithelial cells during differentiation and wound closure
    • Chan K. Y. Release of plasminogen activator by cultured corneal epithelial cells during differentiation and wound closure. Exp. Eye Res. 42:1986;417-431.
    • (1986) Exp. Eye Res. , vol.42 , pp. 417-431
    • Chan, K.Y.1
  • 21
    • 0023576670 scopus 로고
    • Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells
    • Pepper M. S., Vassalli J.-D., Montesano R., Orci L. Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells. J. Cell Biol. 105:1987;2535-2541.
    • (1987) J. Cell Biol. , vol.105 , pp. 2535-2541
    • Pepper, M.S.1    Vassalli, J.-D.2    Montesano, R.3    Orci, L.4
  • 22
    • 0024469171 scopus 로고
    • Plasminogen activator activity is associated with neural crest cell motility in tissue culture
    • Erickson C. A., Isseroff R. R. Plasminogen activator activity is associated with neural crest cell motility in tissue culture. J. Exp. Zool. 251:1989;123-133.
    • (1989) J. Exp. Zool. , vol.251 , pp. 123-133
    • Erickson, C.A.1    Isseroff, R.R.2
  • 23
    • 0028225445 scopus 로고
    • Plasminogen activators are involved in keratinocyte and fibroblast migration in wounded cultures in vitro
    • Quax P. H. A., Boxman I. L. A., van Kesteren C. A. M., Verheijen J. H., Ponec M. Plasminogen activators are involved in keratinocyte and fibroblast migration in wounded cultures in vitro. Fibrinolysis. 8:1994;221-228.
    • (1994) Fibrinolysis , vol.8 , pp. 221-228
    • Quax, P.H.A.1    Boxman, I.L.A.2    Van Kesteren, C.A.M.3    Verheijen, J.H.4    Ponec, M.5
  • 24
    • 0029965504 scopus 로고    scopus 로고
    • Wound repair-induced expression of stromelysins is associated with the acquisition of a mesenchymal phenotype in human respiratory epithelial cells
    • Buisson A.-C., Gilles C., Polette M., Zahm J.-M., Birembaut P., Tournier J.-M. Wound repair-induced expression of stromelysins is associated with the acquisition of a mesenchymal phenotype in human respiratory epithelial cells. Lab. Invest. 74:1996;658-669.
    • (1996) Lab. Invest. , vol.74 , pp. 658-669
    • Buisson, A.-C.1    Gilles, C.2    Polette, M.3    Zahm, J.-M.4    Birembaut, P.5    Tournier, J.-M.6
  • 25
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potenial
    • Sloane B. F., Dunn J. R., Honn K. V. Lysosomal cathepsin B: Correlation with metastatic potenial. Science. 212:1981;1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 27
    • 0027650966 scopus 로고
    • Proteases of cell adhesion proteins in cancer
    • Monsky W. L., Chen W.-T. Proteases of cell adhesion proteins in cancer. Cancer Biol. 4:1993;251-258.
    • (1993) Cancer Biol. , vol.4 , pp. 251-258
    • Monsky, W.L.1    Chen, W.-T.2
  • 28
    • 0028152543 scopus 로고
    • A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells
    • Monsky W. L., Lin C.-Y., Aoyama A., Kelly T., Akiyama S. K., Mueller S. C., Chen W.-T. A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells. Cancer Res. 54:1994;5702-5710.
    • (1994) Cancer Res. , vol.54 , pp. 5702-5710
    • Monsky, W.L.1    Lin, C.-Y.2    Aoyama, A.3    Kelly, T.4    Akiyama, S.K.5    Mueller, S.C.6    Chen, W.-T.7
  • 30
    • 0029999333 scopus 로고    scopus 로고
    • Proteases associated with invadopodia, and their role in degradation of extracellular matrix
    • Chen W.-T. Proteases associated with invadopodia, and their role in degradation of extracellular matrix. Enzyme Protein. 49:1996;59-71.
    • (1996) Enzyme Protein , vol.49 , pp. 59-71
    • Chen, W.-T.1
  • 31
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • Andreasen P. A., Kjøller L., Christensen L., Duffy M. J. The urokinase-type plasminogen activator system in cancer metastasis: A review. Int. J. Cancer. 72:1997;1-22.
    • (1997) Int. J. Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjøller, L.2    Christensen, L.3    Duffy, M.J.4
  • 32
    • 0023192953 scopus 로고
    • Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells
    • Pöllänen J., Saksela O., Salonen E.-M., Andreasen P., Nielsen L., Danø K., Vaheri A. Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells. J. Cell Biol. 104:1987;1085-1096.
    • (1987) J. Cell Biol. , vol.104 , pp. 1085-1096
    • Pöllänen, J.1    Saksela, O.2    Salonen, E.-M.3    Andreasen, P.4    Nielsen, L.5    Danø, K.6    Vaheri, A.7
  • 33
    • 0023819126 scopus 로고
    • Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contacts
    • Pöllänen J., Hedman K., Nielsen L. S., Danø K., Vaheri A. Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contacts. J. Cell Biol. 106:1988;87-95.
    • (1988) J. Cell Biol. , vol.106 , pp. 87-95
    • Pöllänen, J.1    Hedman, K.2    Nielsen, L.S.3    Danø, K.4    Vaheri, A.5
  • 34
    • 0023944278 scopus 로고
    • Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: Colocalization of cell surface urokinase with vinculin
    • Hébert C. A., Baker J. B. Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: Colocalization of cell surface urokinase with vinculin. J. Cell Biol. 106:1988;1241-1247.
    • (1988) J. Cell Biol. , vol.106 , pp. 1241-1247
    • Hébert, C.A.1    Baker, J.B.2
  • 35
    • 0020570408 scopus 로고
    • Heparan sulfate degradation: Relation to tumor invasive and metastatic properties of mouse B16 melanoma sublines
    • Nakajima M., Irimura T., Di Ferrante D., Di Ferrante N., Nicolson G. L. Heparan sulfate degradation: Relation to tumor invasive and metastatic properties of mouse B16 melanoma sublines. Science. 220:1983;611-613.
    • (1983) Science , vol.220 , pp. 611-613
    • Nakajima, M.1    Irimura, T.2    Di Ferrante, D.3    Di Ferrante, N.4    Nicolson, G.L.5
  • 36
    • 0021248709 scopus 로고
    • Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites
    • Chen W.-T., Olden K., Bernard B. A., Chu F.-F. Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J. Cell Biol. 98:1984;1546-1555.
    • (1984) J. Cell Biol. , vol.98 , pp. 1546-1555
    • Chen, W.-T.1    Olden, K.2    Bernard, B.A.3    Chu, F.-F.4
  • 37
    • 0023667821 scopus 로고
    • Fibronectin-degrading proteases from the membranes of transformed cells
    • Chen J.-M., Chen W.-T. Fibronectin-degrading proteases from the membranes of transformed cells. Cell. 48:1987;193-203.
    • (1987) Cell , vol.48 , pp. 193-203
    • Chen, J.-M.1    Chen, W.-T.2
  • 39
    • 0025314849 scopus 로고
    • Degradation of basement membrane laminin by human neutrophil elastase and cathepsin G
    • Heck L. W., Blackburn W. D., Irwin M. H., Abrahamson D. R. Degradation of basement membrane laminin by human neutrophil elastase and cathepsin G. Am. J. Pathol. 136:1990;1267-1274.
    • (1990) Am. J. Pathol. , vol.136 , pp. 1267-1274
    • Heck, L.W.1    Blackburn, W.D.2    Irwin, M.H.3    Abrahamson, D.R.4
  • 40
    • 0026500165 scopus 로고
    • Plasminogen dependent laminin degradation and matrigel invasion by cultured colon cancer is directed by receptor-bound urokinase
    • Boyd D. Plasminogen dependent laminin degradation and matrigel invasion by cultured colon cancer is directed by receptor-bound urokinase. Fibrinolysis. 6:1992;17-21.
    • (1992) Fibrinolysis , vol.6 , pp. 17-21
    • Boyd, D.1
  • 41
    • 0027469284 scopus 로고
    • Interaction of tissue-type plasminogen activator with fibronectin and fibronectin fragments
    • Marchina E., De Petro G., Barlati S. Interaction of tissue-type plasminogen activator with fibronectin and fibronectin fragments. Fibrinolysis. 7:1993;51-57.
    • (1993) Fibrinolysis , vol.7 , pp. 51-57
    • Marchina, E.1    De Petro, G.2    Barlati, S.3
  • 42
    • 0028866283 scopus 로고
    • Degradation of fibronectin fibrils by matrilysin and characterization of the degradation products
    • von Bredow D. C., Nagle R. B., Bowden G. T., Cress A. E. Degradation of fibronectin fibrils by matrilysin and characterization of the degradation products. Exp. Cell Res. 221:1995;83-91.
    • (1995) Exp. Cell Res. , vol.221 , pp. 83-91
    • Von Bredow, D.C.1    Nagle, R.B.2    Bowden, G.T.3    Cress, A.E.4
  • 43
    • 0029443042 scopus 로고
    • Neutrophil proteinases and matrix degradation: The cell biology of pericellular proteolysis
    • Owen C. A., Campbell E. J. Neutrophil proteinases and matrix degradation: The cell biology of pericellular proteolysis. Semin. Cell Biol. 6:1995;367-376.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 367-376
    • Owen, C.A.1    Campbell, E.J.2
  • 44
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 7:1995;728-735.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 45
    • 0021045628 scopus 로고
    • Antibodies to plasminogen activator inhibit human tumor metastasis
    • Ossowski L., Reich E. Antibodies to plasminogen activator inhibit human tumor metastasis. Cell. 35:1983;611-619.
    • (1983) Cell , vol.35 , pp. 611-619
    • Ossowski, L.1    Reich, E.2
  • 46
    • 0023211971 scopus 로고
    • Role of protease inhibition in cellular migration and neuritic outgrowth
    • Monard D. Role of protease inhibition in cellular migration and neuritic outgrowth. Biochem. Pharmacol. 36:1987;1389-1392.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 1389-1392
    • Monard, D.1
  • 48
    • 0028904704 scopus 로고
    • Suppression of in vitro invasion of human fibrosarcoma cells by a leupeptin analogue inhibiting the urokinase-plasmin system
    • Kawada M., Umezawa K. Suppression of in vitro invasion of human fibrosarcoma cells by a leupeptin analogue inhibiting the urokinase-plasmin system. Biochem. Biophys. Res. Commun. 209:1995;25-30.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 25-30
    • Kawada, M.1    Umezawa, K.2
  • 49
    • 0028202550 scopus 로고
    • Inhibition of metastasis of Lewis lung carcinoma by antibody against urokinase-type plasminogen activator in the experimental and spontaneous metastasis model
    • Kobayashi H., Gotoh J., Shinohara H., Moniwa N., Terao T. Inhibition of metastasis of Lewis lung carcinoma by antibody against urokinase-type plasminogen activator in the experimental and spontaneous metastasis model. Thromb. Haemostas. 71:1994;474-480.
    • (1994) Thromb. Haemostas. , vol.71 , pp. 474-480
    • Kobayashi, H.1    Gotoh, J.2    Shinohara, H.3    Moniwa, N.4    Terao, T.5
  • 50
    • 0029165411 scopus 로고
    • Inhibition of organ invasion by the matrix metalloproteinase inhibitor batimastat (BB-94) in two human colon carcinoma metastasis models
    • Watson S. A., Morris T. M., Robinson G., Crimmin M. J., Brown P. D., Hardcastle J. D. Inhibition of organ invasion by the matrix metalloproteinase inhibitor batimastat (BB-94) in two human colon carcinoma metastasis models. Cancer Res. 55:1995;3629-3633.
    • (1995) Cancer Res. , vol.55 , pp. 3629-3633
    • Watson, S.A.1    Morris, T.M.2    Robinson, G.3    Crimmin, M.J.4    Brown, P.D.5    Hardcastle, J.D.6
  • 52
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Wei Y., Waltz D. A., Rao N., Drummond R. J., Rosenberg S., Chapman H. A. Identification of the urokinase receptor as an adhesion receptor for vitronectin. J. Biol. Chem. 269:1994;32380-32388.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 53
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin-binding protein on endothelial cells
    • Kanse S. M., Kost C., Wilhelm O. G., Andreasen P. A., Preissner K. T. The urokinase receptor is a major vitronectin-binding protein on endothelial cells. Exp. Cell Res. 224:1996;344-353.
    • (1996) Exp. Cell Res. , vol.224 , pp. 344-353
    • Kanse, S.M.1    Kost, C.2    Wilhelm, O.G.3    Andreasen, P.A.4    Preissner, K.T.5
  • 54
    • 0029847191 scopus 로고    scopus 로고
    • Requirement of receptor-bound urokinase-type plasminogen activator for integrin αvβ5-directed cell migration
    • Yebra M., Parry G. C. N., Strömblad S., Mackman N., Rosenberg S., Mueller B. M., Cheresh D. A. Requirement of receptor-bound urokinase-type plasminogen activator for integrin αvβ5-directed cell migration. J. Biol. Chem. 271:1996;29393-29399.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29393-29399
    • Yebra, M.1    Parry, G.C.N.2    Strömblad, S.3    Mackman, N.4    Rosenberg, S.5    Mueller, B.M.6    Cheresh, D.A.7
  • 56
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjøller L., Kanse S. M., Kirkegaard T., Rodenburg K. W., Rønne E., Goodman S. L., Preissner K. T., Ossowski L., Andreasen P. A. Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation. Exp. Cell Res. 232:1997;420-429.
    • (1997) Exp. Cell Res. , vol.232 , pp. 420-429
    • Kjøller, L.1    Kanse, S.M.2    Kirkegaard, T.3    Rodenburg, K.W.4    Rønne, E.5    Goodman, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 57
    • 0028250278 scopus 로고
    • Cytological and immunocytochemical approaches to the study of corneal endothelial wound repair
    • Gordon S. R. Cytological and immunocytochemical approaches to the study of corneal endothelial wound repair. Prog. Histochem. Cytochem. 28:1994;1-66.
    • (1994) Prog. Histochem. Cytochem. , vol.28 , pp. 1-66
    • Gordon, S.R.1
  • 58
    • 0000478919 scopus 로고
    • Ion distribution and membrane permeability in lysosomal suspensions
    • Amsterdam: North Holland
    • Goldman R. Ion distribution and membrane permeability in lysosomal suspensions. Lysosomes in Biology and Pathology. 1976;North Holland, Amsterdam.
    • (1976) Lysosomes in Biology and Pathology
    • Goldman, R.1
  • 59
    • 0001528654 scopus 로고
    • Histochemical methods for acid phosphatase
    • Gomori G. Histochemical methods for acid phosphatase. J. Histochem. Cytochem. 4:1956;453-461.
    • (1956) J. Histochem. Cytochem. , vol.4 , pp. 453-461
    • Gomori, G.1
  • 60
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • Basbaum C. B., Werb Z. Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr. Opin. Cell Biol. 8:1996;731-738.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 731-738
    • Basbaum, C.B.1    Werb, Z.2
  • 61
    • 0027133427 scopus 로고
    • Cell-matrix interactions modulate interstitial collagenase expression by human keratinocytes actively involved in wound healing
    • Saarialho-Kere U. K., Kovacs S. O., Pentland A. P., Olerud J. E., Welgus H. G., Parks W. C. Cell-matrix interactions modulate interstitial collagenase expression by human keratinocytes actively involved in wound healing. J. Clin. Invest. 92:1993;2858-2866.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2858-2866
    • Saarialho-Kere, U.K.1    Kovacs, S.O.2    Pentland, A.P.3    Olerud, J.E.4    Welgus, H.G.5    Parks, W.C.6
  • 62
    • 0028262145 scopus 로고
    • Expression of matrix metalloproteinase-2 and -9 during early human wound healing
    • Salo T., Mäkela M., Kylmäniemi M., Autio-Harmainen H., Larjava H. Expression of matrix metalloproteinase-2 and -9 during early human wound healing. Lab. Invest. 70:1994;176-182.
    • (1994) Lab. Invest. , vol.70 , pp. 176-182
    • Salo, T.1    Mäkela, M.2    Kylmäniemi, M.3    Autio-Harmainen, H.4    Larjava, H.5
  • 63
    • 0344636435 scopus 로고
    • Lysosomes: A survey
    • M. Alfert, W. Beermann, G. Rudkin, W. Sandritter, & P. Sitte. Vienna: Springer-Verlag
    • Holtzman E. Lysosomes: A survey. Alfert M., Beermann W., Rudkin G., Sandritter W., Sitte P. Cell Biology Monographs. 1976;Springer-Verlag, Vienna.
    • (1976) Cell Biology Monographs
    • Holtzman, E.1
  • 64
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman I., Fuchs R., Helenius A. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55:1986;663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 65
    • 0019783571 scopus 로고
    • Histochemical localization of cathepsin B at the invasion front of the rabbit V2 carcinoma
    • Graf M., Baici A., Sträuli P. Histochemical localization of cathepsin B at the invasion front of the rabbit V2 carcinoma. Lab. Invest. 45:1981;587-596.
    • (1981) Lab. Invest. , vol.45 , pp. 587-596
    • Graf, M.1    Baici, A.2    Sträuli, P.3
  • 66
    • 0026530280 scopus 로고
    • Cathepsin D in the malignant progression of neoplastic diseases (Review)
    • Leto G., Gebbia N., Rausa L., Tumminello F. M. Cathepsin D in the malignant progression of neoplastic diseases (Review). Anticancer Res. 12:1992;235-240.
    • (1992) Anticancer Res. , vol.12 , pp. 235-240
    • Leto, G.1    Gebbia, N.2    Rausa, L.3    Tumminello, F.M.4
  • 68
    • 0025133381 scopus 로고
    • Localization of urokinase-type plasminogen activator in human eyes: An immunocytochemical study
    • Tripathi R. C., Tripathi B. J., Park J. K. Localization of urokinase-type plasminogen activator in human eyes: An immunocytochemical study. Exp. Eye Res. 51:1990;545-552.
    • (1990) Exp. Eye Res. , vol.51 , pp. 545-552
    • Tripathi, R.C.1    Tripathi, B.J.2    Park, J.K.3
  • 69
    • 0005465184 scopus 로고
    • Plasminogen, a necessary factor for cell migration in vitro
    • E. Reich, D. B. Rifkin, & E. Shaw. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Ossowski L., Quigley J. P., Reich E. Plasminogen, a necessary factor for cell migration in vitro. Reich E., Rifkin D. B., Shaw E. Proteases and Biological Control. 1975;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1975) Proteases and Biological Control
    • Ossowski, L.1    Quigley, J.P.2    Reich, E.3
  • 70
    • 0029905641 scopus 로고    scopus 로고
    • Urokinase and tissue-type plasminogen activator stimulate human vascular smooth muscle cell migration
    • Wijnberg M. J., Nieuwenbroek N. M. E., Slomp J., Quax P. H. A., Verheijen J. H. Urokinase and tissue-type plasminogen activator stimulate human vascular smooth muscle cell migration. Fibrinolysis. 10:1996;75-78.
    • (1996) Fibrinolysis , vol.10 , pp. 75-78
    • Wijnberg, M.J.1    Nieuwenbroek, N.M.E.2    Slomp, J.3    Quax, P.H.A.4    Verheijen, J.H.5
  • 71
    • 0028293357 scopus 로고
    • Confocal fluorescence microscopy of urokinase plasminogen activator receptor and cathepsin D in human MDA-MB-231 breast cancer cells migrating in reconstituted basement membrane
    • Bastholm L., Nielsen M. H., DeMay J., Danø K., Brünner N., Høyer-Hansen G., Rønne E., Elling F. Confocal fluorescence microscopy of urokinase plasminogen activator receptor and cathepsin D in human MDA-MB-231 breast cancer cells migrating in reconstituted basement membrane. Biotechnol. Histochem. 69:1994;61-67.
    • (1994) Biotechnol. Histochem. , vol.69 , pp. 61-67
    • Bastholm, L.1    Nielsen, M.H.2    Demay, J.3    Danø, K.4    Brünner, N.5    Høyer-Hansen, G.6    Rønne, E.7    Elling, F.8
  • 72
    • 0025504570 scopus 로고
    • A high affinity receptor for urokinase plasminogen activator on human keratinocytes: Characterization and potential modulation during migration
    • McNeill H., Jensen P. J. A high affinity receptor for urokinase plasminogen activator on human keratinocytes: Characterization and potential modulation during migration. Cell Regul. 1:1990;843-852.
    • (1990) Cell Regul. , vol.1 , pp. 843-852
    • McNeill, H.1    Jensen, P.J.2
  • 73
    • 0028905522 scopus 로고
    • Migrating vascular smooth muscle cells polarize cell surface urokinase receptors after injury in vitro
    • Okada S. S., Tomaszewski J. E., Barnathan E. S. Migrating vascular smooth muscle cells polarize cell surface urokinase receptors after injury in vitro. Exp. Cell Res. 217:1995;180-187.
    • (1995) Exp. Cell Res. , vol.217 , pp. 180-187
    • Okada, S.S.1    Tomaszewski, J.E.2    Barnathan, E.S.3
  • 74
    • 0028868384 scopus 로고
    • Expression of the human gene encoding urokinase plasminogen activator is activated by disruption of the cytoskeleton
    • Bayraktutan U., Jones P. Expression of the human gene encoding urokinase plasminogen activator is activated by disruption of the cytoskeleton. Exp. Cell Res. 221:1995;486-495.
    • (1995) Exp. Cell Res. , vol.221 , pp. 486-495
    • Bayraktutan, U.1    Jones, P.2
  • 75
    • 0020360018 scopus 로고
    • In situ demonstration of actin in normal and injured ocular tissues using 7-nitrobenz-2-oxa-1,3-diazole phallacidin
    • Gordon S. R., Essner E., Rothstein H. In situ demonstration of actin in normal and injured ocular tissues using 7-nitrobenz-2-oxa-1,3-diazole phallacidin. Cell Motil. 2:1982;343-354.
    • (1982) Cell Motil. , vol.2 , pp. 343-354
    • Gordon, S.R.1    Essner, E.2    Rothstein, H.3
  • 76
    • 0024439185 scopus 로고
    • Colocalization of fibroblast growth factor binding sites with extracellular matrix components in normal and keratoconus corneas
    • Morton K., Hutchinson C., Jeanny J. C., Karpouzas I., Pouliquen Y., Courtois Y. Colocalization of fibroblast growth factor binding sites with extracellular matrix components in normal and keratoconus corneas. Curr. Eye Res. 8:1989;975-987.
    • (1989) Curr. Eye Res. , vol.8 , pp. 975-987
    • Morton, K.1    Hutchinson, C.2    Jeanny, J.C.3    Karpouzas, I.4    Pouliquen, Y.5    Courtois, Y.6
  • 77
    • 0023831047 scopus 로고
    • A heparin-binding angiogenic protein - Basic fibroblast growth factor - Is stored within basement membrane
    • Folkman J., Klagsbrun M., Sasse J., Wadzinski M., Ingber D., Vlodavsky I. A heparin-binding angiogenic protein - basic fibroblast growth factor - is stored within basement membrane. Am. J. Pathol. 130:1988;393-400.
    • (1988) Am. J. Pathol. , vol.130 , pp. 393-400
    • Folkman, J.1    Klagsbrun, M.2    Sasse, J.3    Wadzinski, M.4    Ingber, D.5    Vlodavsky, I.6
  • 78
    • 0024410420 scopus 로고
    • Basic fibroblast growth factor is released from endothelial extracellular matrix in a biologically active form
    • Presta M., Maier J. A. M., Rusnati M., Ragnotti G. Basic fibroblast growth factor is released from endothelial extracellular matrix in a biologically active form. J. Cell. Physiol. 140:1989;68-74.
    • (1989) J. Cell. Physiol. , vol.140 , pp. 68-74
    • Presta, M.1    Maier, J.A.M.2    Rusnati, M.3    Ragnotti, G.4
  • 79
    • 0025753774 scopus 로고
    • MCF7 mammary cancer cells respond to bFGF and internalize it following its release from extracellular matrix: A permissive role for cathepsin D
    • Briozzo P., Badet J., Capony F., Pieri I., Montcourrier P., Barritault D., Rochefort H. MCF7 mammary cancer cells respond to bFGF and internalize it following its release from extracellular matrix: A permissive role for cathepsin D. Exp. Cell Res. 194:1991;252-259.
    • (1991) Exp. Cell Res. , vol.194 , pp. 252-259
    • Briozzo, P.1    Badet, J.2    Capony, F.3    Pieri, I.4    Montcourrier, P.5    Barritault, D.6    Rochefort, H.7
  • 80
    • 0027173065 scopus 로고
    • Transforming growth factor-β1 stimulates macrophage urokinase expression and release of matrix-bound basic fibroblast growth factor
    • Falcone D. J., McCaffrey T. A., Haimovitz-Friedman A., Garcia M. Transforming growth factor-β1 stimulates macrophage urokinase expression and release of matrix-bound basic fibroblast growth factor. J. Cell. Physiol. 155:1993;595-605.
    • (1993) J. Cell. Physiol. , vol.155 , pp. 595-605
    • Falcone, D.J.1    McCaffrey, T.A.2    Haimovitz-Friedman, A.3    Garcia, M.4
  • 81
    • 0026651507 scopus 로고
    • Biological and clinical significance of cathepsin D in breast cancer
    • Rochefort H. Biological and clinical significance of cathepsin D in breast cancer. Acta Oncol. 31:1992;125-130.
    • (1992) Acta Oncol. , vol.31 , pp. 125-130
    • Rochefort, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.