메뉴 건너뛰기




Volumn 21, Issue 10, 2006, Pages 1544-1554

Urokinase plasminogen activator stimulates function of active forms of stromelysin and gelatinases (MMP-2 and MMP-9) in cirrhotic tissue

Author keywords

Carbon tetrachloride; Cirrhosis; Collagens; Hepatic stellate cells; Metalloproteinases; Urokinase plasminogen activator

Indexed keywords

ADENOVIRUS VECTOR; COLLAGEN TYPE 1; GELATINASE A; GELATINASE B; GREEN FLUORESCENT PROTEIN; MESSENGER RNA; PLASMINOGEN ACTIVATOR INHIBITOR 1; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TRANSFORMING GROWTH FACTOR BETA1; UROKINASE;

EID: 33747602999     PISSN: 08159319     EISSN: 14401746     Source Type: Journal    
DOI: 10.1111/j.1440-1746.2006.04398.x     Document Type: Article
Times cited : (16)

References (46)
  • 2
    • 0036116213 scopus 로고    scopus 로고
    • Non-alcoholic steatohepatitis (NASH): Where are we now and where are going?
    • Day CP. Non-alcoholic steatohepatitis (NASH): where are we now and where are going? Gut 2002; 50: 585-5.
    • (2002) Gut , vol.50 , pp. 585-585
    • Day, C.P.1
  • 3
    • 33746521801 scopus 로고
    • The cellular basis of hepatic fibrosis: Mechanisms and treatment strategies
    • Friedman SL. The cellular basis of hepatic fibrosis: mechanisms and treatment strategies. N. Engl. J. Med. 1993; 328: 1828-35.
    • (1993) N. Engl. J. Med. , vol.328 , pp. 1828-1835
    • Friedman, S.L.1
  • 4
    • 0023021612 scopus 로고
    • Measurement of urokinase-type plasminogen activator (u-PA) with an enzyme-linked immunosorbent assay (ELISA) based on three murine monoclonal antibodies
    • Darras V. Measurement of urokinase-type plasminogen activator (u-PA) with an enzyme-linked immunosorbent assay (ELISA) based on three murine monoclonal antibodies. Thromb. Haemost. 1986; 56: 411-14.
    • (1986) Thromb. Haemost. , vol.56 , pp. 411-414
    • Darras, V.1
  • 5
    • 0029998086 scopus 로고    scopus 로고
    • The plasminogen-activating system in hepatic stellate cells
    • Leyland H, Gentry J, Arthur M, Benyon R. The plasminogen-activating system in hepatic stellate cells. Hepatology 1996; 24: 1172-8.
    • (1996) Hepatology , vol.24 , pp. 1172-1178
    • Leyland, H.1    Gentry, J.2    Arthur, M.3    Benyon, R.4
  • 7
    • 0034567343 scopus 로고    scopus 로고
    • Cirrosis is reverted by urokinase-type plasminogen activator gene therapy
    • Salgado S, Garcia J, Vera J et al. Cirrosis is reverted by urokinase-type plasminogen activator gene therapy. Mol. Ther. 2000; 2: 545-51.
    • (2000) Mol. Ther. , vol.2 , pp. 545-551
    • Salgado, S.1    Garcia, J.2    Vera, J.3
  • 8
    • 1142275284 scopus 로고    scopus 로고
    • Improved effects of viral gene delivery of human uPA plus biliodigestive anastomosis induce recovery from experimental biliary cirrhosis
    • Miranda-Diaz A, Rincon AR, Salgado S et al. Improved effects of viral gene delivery of human uPA plus biliodigestive anastomosis induce recovery from experimental biliary cirrhosis. Mol. Ther. 2004; 9: 30-7.
    • (2004) Mol. Ther. , vol.9 , pp. 30-37
    • Miranda-Diaz, A.1    Rincon, A.R.2    Salgado, S.3
  • 10
    • 3242699717 scopus 로고    scopus 로고
    • uPA and uPAR in fibrinolysis, immunity and pathology
    • Mondino A, Blasi F. uPA and uPAR in fibrinolysis, immunity and pathology. Trends Immunol. 2004; 25: 450-6.
    • (2004) Trends Immunol. , vol.25 , pp. 450-456
    • Mondino, A.1    Blasi, F.2
  • 11
    • 0028295979 scopus 로고
    • Physiological consequences of loss of plasminogen activator gene function in mice
    • Carmeliet P, Schoonjans L, Kieckens L et al. Physiological consequences of loss of plasminogen activator gene function in mice. Nature 1994; 368: 419-24.
    • (1994) Nature , vol.368 , pp. 419-424
    • Carmeliet, P.1    Schoonjans, L.2    Kieckens, L.3
  • 12
    • 0028913699 scopus 로고
    • Biological effects of disruption of the tissue type plasminogen activator, urokinase-type plasminogen activator, and plasminogen activator inhibitor-1 genes in mice
    • Carmeliet P, Bouche A, De Clerq C et al. Biological effects of disruption of the tissue type plasminogen activator, urokinase-type plasminogen activator, and plasminogen activator inhibitor-1 genes in mice. Ann. N.Y. Acad. Sci. 1995; 748: 367-81.
    • (1995) Ann. N.Y. Acad. Sci. , vol.748 , pp. 367-381
    • Carmeliet, P.1    Bouche, A.2    De Clerq, C.3
  • 13
    • 0035101027 scopus 로고    scopus 로고
    • Plasminogen activators direct reorganization of the liver lobule after acute injure
    • Bezerra JA, Currier AR, Melin-Aldana H et al. Plasminogen activators direct reorganization of the liver lobule after acute injure. Am. J. Pathol. 2001; 158: 921-9.
    • (2001) Am. J. Pathol. , vol.158 , pp. 921-929
    • Bezerra, J.A.1    Currier, A.R.2    Melin-Aldana, H.3
  • 14
    • 10844237902 scopus 로고    scopus 로고
    • Modulation of urokinase-type plasminogen activator by transforming growth factor beta1 in acetaldehyde-activated hepatic stellate cells
    • Pérez-Liz G, Flores-Hernández J, Arias-Montaño JA, Reyes-Esparza JA, Rodríguez-Fragozo L. Modulation of urokinase-type plasminogen activator by transforming growth factor beta1 in acetaldehyde-activated hepatic stellate cells.. Pharmacology 2005; 73: 23-30.
    • (2005) Pharmacology , vol.73 , pp. 23-30
    • Pérez-Liz, G.1    Flores-Hernández, J.2    Arias-Montaño, J.A.3    Reyes-Esparza, J.A.4    Rodríguez-Fragozo, L.5
  • 15
    • 0025063948 scopus 로고
    • Regulation of TGFβ gene expression in rat liver intoxicated with carbon tetrachloride
    • Armendàriz-Borunda J, Seyer JM, Kang AH, Raghow R. Regulation of TGFβ gene expression in rat liver intoxicated with carbon tetrachloride. FASEB J. 1990; 4: 215-21.
    • (1990) FASEB J. , vol.4 , pp. 215-221
    • Armendàriz-Borunda, J.1    Seyer, J.M.2    Kang, A.H.3    Raghow, R.4
  • 17
    • 0004136246 scopus 로고
    • Sambrook J, Fritsch EF, Maniatis T, eds. New York: Cold Spring Harbor Laboratory Press
    • Sambrook J, Fritsch EF, Maniatis T, eds. Molecular Cloning: A Laboratory Manual, 2nd edn. New York: Cold Spring Harbor Laboratory Press, 1989.
    • (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn.
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of proteing utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of proteing utilizing the principle of protein-dye binding. Annal. Biochem. 1976; 72: 248-54.
    • (1976) Annal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0032996954 scopus 로고    scopus 로고
    • Direct evidence that hepatocyte growth factor-induced invasion of hepatocellular carcinoma cells is mediated by urokinase
    • Monvosin A, Neaud V, De Ledinghen V et al. Direct evidence that hepatocyte growth factor-induced invasion of hepatocellular carcinoma cells is mediated by urokinase. J. Hepatol. 1999; 30: 511-18.
    • (1999) J. Hepatol. , vol.30 , pp. 511-518
    • Monvosin, A.1    Neaud, V.2    De Ledinghen, V.3
  • 20
    • 0023725892 scopus 로고
    • In vitro inhibition of urokinase by penicicillins
    • Higazi A-R, Mayer M. In vitro inhibition of urokinase by penicicillins. Thromb. Haemost. 1988; 60: 305-7.
    • (1988) Thromb. Haemost. , vol.60 , pp. 305-307
    • Higazi, A.-R.1    Mayer, M.2
  • 21
    • 37349064728 scopus 로고
    • Nobel Lecture, March 20
    • Chain Ernest B. The Chemical Structure of the Penicillins. Nobel Lecture, March 20, 1946. Available from: http://nobelprize.org/medicine/laureates/1945/ chain-lecture.pdf [Accessed March 2000].
    • (1946) The Chemical Structure of the Penicillins
    • Chain Ernest, B.1
  • 22
    • 0029088057 scopus 로고
    • A modified urokinase plasminogen activator induces liver regeneration without bleeding
    • Lieber A, Vrancken PM-J, Gown A, Perkins J, Kay MA. A modified urokinase plasminogen activator induces liver regeneration without bleeding. Hum. Gene Ther. 1995; 6: 1029-37.
    • (1995) Hum. Gene Ther. , vol.6 , pp. 1029-1037
    • Lieber, A.1    Vrancken, P.M.-J.2    Gown, A.3    Perkins, J.4    Kay, M.A.5
  • 23
  • 24
    • 0028344129 scopus 로고
    • Heparin inhibits the induction of three matrix metalloproteinases (stromelysin, 92-kD gelatinase, and collagenase) in primate arterial smoth muscle cells
    • Kenagy RD, Nikkari ST, Welgus HG, Clowes AW. Heparin inhibits the induction of three matrix metalloproteinases (stromelysin, 92-kD gelatinase, and collagenase) in primate arterial smoth muscle cells. J. Clin. Invest. 1994; 93: 1987-93.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1987-1993
    • Kenagy, R.D.1    Nikkari, S.T.2    Welgus, H.G.3    Clowes, A.W.4
  • 25
    • 0020956387 scopus 로고
    • Comparative electrophoretic analysis of human and plasminogen activators in SDS polyacrylamide gels containing plasminogen and casein
    • Roche PC, Campeau JD, Shaw STJ. Comparative electrophoretic analysis of human and plasminogen activators in SDS polyacrylamide gels containing plasminogen and casein. Biochim. Biophys. Acta 1983; 745: 82-9.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 82-89
    • Roche, P.C.1    Campeau, J.D.2    Shaw, S.T.J.3
  • 26
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol cloroform extration
    • Chommczynsky P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol cloroform extration. Annal. Biochem. 1987; 162: 156-9.
    • (1987) Annal. Biochem. , vol.162 , pp. 156-159
    • Chommczynsky, P.1    Sacchi, N.2
  • 27
    • 0032561440 scopus 로고    scopus 로고
    • Treatment with anti-transforming growth factor b antibodies influences an altered pattern of cytokines expresion in injured rat liver
    • Delgado RV, Salazar A, Panduro A, Armendariz-Borunda J. Treatment with anti-transforming growth factor b antibodies influences an altered pattern of cytokines expresion in injured rat liver. Biochim. Biophys. Acta 1998; 1442: 20-7.
    • (1998) Biochim. Biophys. Acta , vol.1442 , pp. 20-27
    • Delgado, R.V.1    Salazar, A.2    Panduro, A.3    Armendariz-Borunda, J.4
  • 28
    • 0033652197 scopus 로고    scopus 로고
    • Cholestasis-induced fibrosis is reduced by interferon α-2a and is associated with elevated liver metalloprotease activity
    • Bueno MR, Daneri A, Armendariz-Borunda J. Cholestasis-induced fibrosis is reduced by interferon α-2a and is associated with elevated liver metalloprotease activity. J. Hepatol. 2000; 33: 915-25.
    • (2000) J. Hepatol. , vol.33 , pp. 915-925
    • Bueno, M.R.1    Daneri, A.2    Armendariz-Borunda, J.3
  • 29
    • 21844465158 scopus 로고    scopus 로고
    • Genomic and functional characterization of stellate cells isolated from human cirrhotic livers
    • Sancho-Bru P, Bataller R, Gasull X et al. Genomic and functional characterization of stellate cells isolated from human cirrhotic livers. J. Hepatol. 2005; 43: 272-82.
    • (2005) J. Hepatol. , vol.43 , pp. 272-282
    • Sancho-Bru, P.1    Bataller, R.2    Gasull, X.3
  • 30
    • 0037036387 scopus 로고    scopus 로고
    • Ets-1 is an effector of the transforming growth factor β (TGFβ) signaling pathway and an antagonist of the profibrotic effects of TGFβ
    • Czuwara J, Sementchenko V, Watson D, Trojanowska M. Ets-1 is an effector of the transforming growth factor β (TGFβ) signaling pathway and an antagonist of the profibrotic effects of TGFβ. J. Biol. Chem. 2002; 277: 20 399-498.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20399-20498
    • Czuwara, J.1    Sementchenko, V.2    Watson, D.3    Trojanowska, M.4
  • 31
    • 0033555244 scopus 로고    scopus 로고
    • Rel transcription factors contribute to elevated urokinase expression in human ovarian carcinoma cells
    • Reuninig U, Guerrini L, Nishiguchi T et al. Rel transcription factors contribute to elevated urokinase expression in human ovarian carcinoma cells. Eur. J. Biochem. 1999; 259: 143-8.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 143-148
    • Reuninig, U.1    Guerrini, L.2    Nishiguchi, T.3
  • 32
    • 0031740778 scopus 로고    scopus 로고
    • Altered balance between matrix metalloproteinases and their inhibitors in experimental biliary fibrosis
    • Kossakowska A, Lee S, Urbanski L et al. Altered balance between matrix metalloproteinases and their inhibitors in experimental biliary fibrosis. Am. J. Pathol. 1998; 153: 1895-902.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1895-1902
    • Kossakowska, A.1    Lee, S.2    Urbanski, L.3
  • 33
    • 2642537690 scopus 로고    scopus 로고
    • Engagement of a b integrin regulates proliferation and apoptosis of hepatic stellate cells
    • Zhou X, Murphy FR, Gehdu N, Zhang J, Iredale JP, Benyon C. Engagement of a b integrin regulates proliferation and apoptosis of hepatic stellate cells. J. Biol. Chem. 2004; 279: 23 996-4006.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23996-24006
    • Zhou, X.1    Murphy, F.R.2    Gehdu, N.3    Zhang, J.4    Iredale, J.P.5    Benyon, C.6
  • 34
    • 0032079433 scopus 로고    scopus 로고
    • Activation of gelatinase-tissue-inhibitors-of-metalloproteinase complexes by matrilysin
    • Von Bredow DC, Crees AE, Howard EW, Bowden GT, Nagle RB. Activation of gelatinase-tissue-inhibitors-of-metalloproteinase complexes by matrilysin. Biochem. J. 1998; 331: 965-72.
    • (1998) Biochem. J. , vol.331 , pp. 965-972
    • Von Bredow, D.C.1    Crees, A.E.2    Howard, E.W.3    Bowden, G.T.4    Nagle, R.B.5
  • 35
    • 0029310597 scopus 로고
    • Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease
    • Weiskirchen R, Kneifel J, Weiskirchen S et al. Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease. Biol. Chem. Hoppe Seyler 1995; 376: 345-55.
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 345-355
    • Weiskirchen, R.1    Kneifel, J.2    Weiskirchen, S.3
  • 36
    • 0030056244 scopus 로고    scopus 로고
    • Cell type specific expression of neural cell adhesion molecule (N-CAM) in ITO cells of rat liver: Upregulation during in vitro activation and in hepatic tissue repair
    • Knittel T, Aurisch S, Neubauer K, Eichhorst S, Ramadori G. Cell type specific expression of neural cell adhesion molecule (N-CAM) in ITO cells of rat liver: upregulation during in vitro activation and in hepatic tissue repair. Am. J. Pathol. 1996; 149: 449-62.
    • (1996) Am. J. Pathol. , vol.149 , pp. 449-462
    • Knittel, T.1    Aurisch, S.2    Neubauer, K.3    Eichhorst, S.4    Ramadori, G.5
  • 37
    • 0034680787 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors and hepatic stellate cell activation
    • Myahara T, Schrum L, Rippem R et al. Peroxisome proliferator-activated receptors and hepatic stellate cell activation. J. Biol. Chem. 1999; 275: 35 715-22.
    • (1999) J. Biol. Chem. , vol.275 , pp. 35715-35722
    • Myahara, T.1    Schrum, L.2    Rippem, R.3
  • 38
    • 0034532055 scopus 로고    scopus 로고
    • Inactivation of plasminogen activator inhibitor-1 by specific proteolysis with stromelysin-1 (MMP-3)
    • Lijnen HR, Arza B, Van Hoef B, Collen D, Declerck P. Inactivation of plasminogen activator inhibitor-1 by specific proteolysis with stromelysin-1 (MMP-3). J. Biol. Chem. 2000; 276: 37645-50.
    • (2000) J. Biol. Chem. , vol.276 , pp. 37645-37650
    • Lijnen, H.R.1    Arza, B.2    Van Hoef, B.3    Collen, D.4    Declerck, P.5
  • 39
    • 11144357753 scopus 로고    scopus 로고
    • Treatment with human metalloproteinase-8 gene delivery ameliorates experimental rat liver cirrhosis
    • Siller-Lopez F, Sandoval A, Salgado S et al. Treatment with human metalloproteinase-8 gene delivery ameliorates experimental rat liver cirrhosis. Gastroenterology 2004; 126: 1122-33.
    • (2004) Gastroenterology , vol.126 , pp. 1122-1133
    • Siller-Lopez, F.1    Sandoval, A.2    Salgado, S.3
  • 41
    • 0024322010 scopus 로고
    • Regulation of type 1 plasminogen activator inhibitor gene expression in cultured bovine aortic endothelial cells
    • Sawdey M, Podor JT, Loskutoff DJ. Regulation of type 1 plasminogen activator inhibitor gene expression in cultured bovine aortic endothelial cells. J. Biol. Chem. 1989; 264: 10 396-401.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10396-10401
    • Sawdey, M.1    Podor, J.T.2    Loskutoff, D.J.3
  • 42
    • 0034743778 scopus 로고    scopus 로고
    • Characterization of TGFbeta-responsive human trophoblast derived cell line
    • Smith AN, Carter QL, Kniss DA, Brown TL. Characterization of TGFbeta-responsive human trophoblast derived cell line. Placenta 2001; 22: 425-31.
    • (2001) Placenta , vol.22 , pp. 425-431
    • Smith, A.N.1    Carter, Q.L.2    Kniss, D.A.3    Brown, T.L.4
  • 43
    • 4644231399 scopus 로고    scopus 로고
    • Nuclear factor inducing kinase plays a crucial role in osteopontin-induced MAPK/I kinase-dependent nuclear factor kB-mediated promatrix metalloproteinase-9 activation
    • Rangaswami H, Bulbule A, Kundu G. Nuclear factor inducing kinase plays a crucial role in osteopontin-induced MAPK/I kinase-dependent nuclear factor kB-mediated promatrix metalloproteinase-9 activation. J. Biol. Chem. 2004; 279: 38 921-35.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38921-38935
    • Rangaswami, H.1    Bulbule, A.2    Kundu, G.3
  • 44
    • 0033405694 scopus 로고    scopus 로고
    • Resistance of young gelatinase B-deficent mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions
    • Dubois B, Massure S, Hurtenbach U et al. Resistance of young gelatinase B-deficent mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions. J. Clin. Invest. 1999; 104: 1507-15.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1507-1515
    • Dubois, B.1    Massure, S.2    Hurtenbach, U.3
  • 45
    • 0027462903 scopus 로고
    • Differential regulation of gelatinase B and tissue-type plasmin activator expression in human bowes melanoma cells
    • Houde M, de Bruyne G, Bracke M et al. Differential regulation of gelatinase B and tissue-type plasmin activator expression in human bowes melanoma cells. Int. J. Cancer 1993; 1: 395-400.
    • (1993) Int. J. Cancer , vol.1 , pp. 395-400
    • Houde, M.1    De Bruyne, G.2    Bracke, M.3
  • 46
    • 0033532205 scopus 로고    scopus 로고
    • Activation of metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion
    • Ramos-DeSimone N, Hahn-Dantona E, Sipley J, Nagase H, French DL, Quigley James P. Activation of metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J. Biol. Chem. 1999; 274: 13 066-76.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13066-13076
    • Ramos-DeSimone, N.1    Hahn-Dantona, E.2    Sipley, J.3    Nagase, H.4    French, D.L.5    Quigley James, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.