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Volumn 103, Issue 5, 2012, Pages 1060-1068

Plasmin triggers a switch-like decrease in thrombospondin-dependent activation of TGF-β1

Author keywords

[No Author keywords available]

Indexed keywords

PLASMIN; THROMBOSPONDIN 1; TRANSFORMING GROWTH FACTOR BETA1;

EID: 84865774133     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.06.050     Document Type: Article
Times cited : (22)

References (67)
  • 2
    • 0034608937 scopus 로고    scopus 로고
    • Transforming growth factor β contributes to progressive diabetic nephropathy
    • W.B. Reeves, and T.E. Andreoli Transforming growth factor β contributes to progressive diabetic nephropathy Proc. Natl. Acad. Sci. USA 97 2000 7667 7669
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7667-7669
    • Reeves, W.B.1    Andreoli, T.E.2
  • 3
    • 58149236744 scopus 로고    scopus 로고
    • Roles of TGFβ in metastasis
    • D. Padua, and J. Massagué Roles of TGFβ in metastasis Cell Res. 19 2009 89 102
    • (2009) Cell Res. , vol.19 , pp. 89-102
    • Padua, D.1    Massagué, J.2
  • 4
    • 0034604110 scopus 로고    scopus 로고
    • Role of transforming growth factor β in human disease
    • G.C. Blobe, W.P. Schiemann, and H.F. Lodish Role of transforming growth factor β in human disease N. Engl. J. Med. 342 2000 1350 1358
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1350-1358
    • Blobe, G.C.1    Schiemann, W.P.2    Lodish, H.F.3
  • 5
    • 55649123317 scopus 로고    scopus 로고
    • Smad signaling dynamics: Insights from a parsimonious model
    • H. Shankaran, and H.S. Wiley Smad signaling dynamics: insights from a parsimonious model Sci. Signal. 1 2008 pe41
    • (2008) Sci. Signal. , vol.1 , pp. 41
    • Shankaran, H.1    Wiley, H.S.2
  • 6
    • 44349125602 scopus 로고    scopus 로고
    • Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system
    • B. Schmierer, and A.L. Tournier C.S. Hill Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system Proc. Natl. Acad. Sci. USA 105 2008 6608 6613
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6608-6613
    • Schmierer, B.1    Tournier, A.L.2    Hill, C.S.3
  • 7
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFβ activation
    • J.P. Annes, J.S. Munger, and D.B. Rifkin Making sense of latent TGFβ activation J. Cell Sci. 116 2003 217 224
    • (2003) J. Cell Sci. , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 8
    • 61849099472 scopus 로고    scopus 로고
    • TGF-β bioavailability: Latency, targeting and activation
    • R. Derynck, K. Miyazono, Cold Spring Harbor Laboratory Press Long Island, NY
    • B. Dabovic, and D.B. Rifkin TGF-β bioavailability: latency, targeting and activation R. Derynck, K. Miyazono, The TGF-β Family 2008 Cold Spring Harbor Laboratory Press Long Island, NY 1114
    • (2008) The TGF-β Family , pp. 1114
    • Dabovic, B.1    Rifkin, D.B.2
  • 9
    • 0035049231 scopus 로고    scopus 로고
    • Thrombospondins as matricellular modulators of cell function
    • P. Bornstein Thrombospondins as matricellular modulators of cell function J. Clin. Invest. 107 2001 929 934
    • (2001) J. Clin. Invest. , vol.107 , pp. 929-934
    • Bornstein, P.1
  • 10
    • 12344320716 scopus 로고    scopus 로고
    • Thrombospondin-1 is a major activator of TGF-β1 in vivo
    • S.E. Crawford, and V. Stellmach N. Bouck Thrombospondin-1 is a major activator of TGF-β1 in vivo Cell 93 1998 1159 1170
    • (1998) Cell , vol.93 , pp. 1159-1170
    • Crawford, S.E.1    Stellmach, V.2    Bouck, N.3
  • 11
    • 0037677200 scopus 로고    scopus 로고
    • The thrombospondin 1-TGF-β axis in fibrotic renal disease
    • C. Hugo The thrombospondin 1-TGF-β axis in fibrotic renal disease Nephrol. Dial. Transplant. 18 2003 1241 1245
    • (2003) Nephrol. Dial. Transplant. , vol.18 , pp. 1241-1245
    • Hugo, C.1
  • 12
    • 0242490951 scopus 로고    scopus 로고
    • A blocking peptide for transforming growth factor-β1 activation prevents hepatic fibrosis in vivo
    • H. Kondou, and S. Mushiake K. Ozono A blocking peptide for transforming growth factor-β1 activation prevents hepatic fibrosis in vivo J. Hepatol. 39 2003 742 748
    • (2003) J. Hepatol. , vol.39 , pp. 742-748
    • Kondou, H.1    Mushiake, S.2    Ozono, K.3
  • 13
    • 0033662588 scopus 로고    scopus 로고
    • Autocrine thrombospondin partially mediates TGF-β1-induced proliferation of vascular smooth muscle cells
    • M. Sajid, M. Lele, and G.A. Stouffer Autocrine thrombospondin partially mediates TGF-β1-induced proliferation of vascular smooth muscle cells Am. J. Physiol. Heart Circ. Physiol. 279 2000 H2159 H2165
    • (2000) Am. J. Physiol. Heart Circ. Physiol. , vol.279
    • Sajid, M.1    Lele, M.2    Stouffer, G.A.3
  • 14
    • 17844395977 scopus 로고    scopus 로고
    • Constitutive thrombospondin-1 overexpression contributes to autocrine transforming growth factor-β signaling in cultured scleroderma fibroblasts
    • Y. Mimura, and H. Ihn K. Tamaki Constitutive thrombospondin-1 overexpression contributes to autocrine transforming growth factor-β signaling in cultured scleroderma fibroblasts Am. J. Pathol. 166 2005 1451 1463
    • (2005) Am. J. Pathol. , vol.166 , pp. 1451-1463
    • Mimura, Y.1    Ihn, H.2    Tamaki, K.3
  • 15
    • 0025215307 scopus 로고
    • Mechanism of activation of latent recombinant transforming growth factor β1 by plasmin
    • R.M. Lyons, and L.E. Gentry H.L. Moses Mechanism of activation of latent recombinant transforming growth factor β1 by plasmin J. Cell Biol. 110 1990 1361 1367
    • (1990) J. Cell Biol. , vol.110 , pp. 1361-1367
    • Lyons, R.M.1    Gentry, L.E.2    Moses, H.L.3
  • 16
    • 0019230430 scopus 로고
    • Plaminogen is synthesized by primary cultures of rat hepatocytes
    • J.F. Bohmfalk, and G.M. Fuller Plaminogen is synthesized by primary cultures of rat hepatocytes Science 209 1980 408 410
    • (1980) Science , vol.209 , pp. 408-410
    • Bohmfalk, J.F.1    Fuller, G.M.2
  • 17
    • 0242469081 scopus 로고    scopus 로고
    • Plasminogen mediates liver regeneration and angiogenesis after experimental partial hepatectomy
    • T.A. Drixler, and J.M. Vogten I.H. Borel Rinkes Plasminogen mediates liver regeneration and angiogenesis after experimental partial hepatectomy Br. J. Surg. 90 2003 1384 1390
    • (2003) Br. J. Surg. , vol.90 , pp. 1384-1390
    • Drixler, T.A.1    Vogten, J.M.2    Borel Rinkes, I.H.3
  • 19
    • 18844375381 scopus 로고    scopus 로고
    • Pleiotropic functions of plasminogen activator inhibitor-1
    • H.R. Lijnen Pleiotropic functions of plasminogen activator inhibitor-1 J. Thromb. Haemost. 3 2005 35 45
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 35-45
    • Lijnen, H.R.1
  • 20
    • 77950623414 scopus 로고    scopus 로고
    • Plasmin plays a key role in the regulation of profibrogenic molecules in hepatic stellate cells
    • A. Martínez-Rizo, and M. Bueno-Topete J. Armendáriz-Borunda Plasmin plays a key role in the regulation of profibrogenic molecules in hepatic stellate cells Liver Int. 30 2010 298 310
    • (2010) Liver Int. , vol.30 , pp. 298-310
    • Martínez-Rizo, A.1    Bueno-Topete, M.2    Armendáriz-Borunda, J.3
  • 21
    • 0042388115 scopus 로고    scopus 로고
    • A mutant, noninhibitory plasminogen activator inhibitor type 1 decreases matrix accumulation in experimental glomerulonephritis
    • Y. Huang, and M. Haraguchi N.A. Noble A mutant, noninhibitory plasminogen activator inhibitor type 1 decreases matrix accumulation in experimental glomerulonephritis J. Clin. Invest. 112 2003 379 388
    • (2003) J. Clin. Invest. , vol.112 , pp. 379-388
    • Huang, Y.1    Haraguchi, M.2    Noble, N.A.3
  • 22
    • 0034657657 scopus 로고    scopus 로고
    • Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase
    • A. Bonnefoy, and C. Legrand Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase Thromb. Res. 98 2000 323 332
    • (2000) Thromb. Res. , vol.98 , pp. 323-332
    • Bonnefoy, A.1    Legrand, C.2
  • 23
    • 0026583974 scopus 로고
    • Thrombospondin is a slow tight-binding inhibitor of plasmin
    • P.J. Hogg, J. Stenflo, and D.F. Mosher Thrombospondin is a slow tight-binding inhibitor of plasmin Biochemistry 31 1992 265 269
    • (1992) Biochemistry , vol.31 , pp. 265-269
    • Hogg, P.J.1    Stenflo, J.2    Mosher, D.F.3
  • 24
    • 33645754505 scopus 로고    scopus 로고
    • Signal processing in the TGF-β superfamily ligand-receptor network
    • J.M. Vilar, R. Jansen, and C. Sander Signal processing in the TGF-β superfamily ligand-receptor network PLOS Comput. Biol. 2 2006 e3
    • (2006) PLOS Comput. Biol. , vol.2 , pp. 3
    • Vilar, J.M.1    Jansen, R.2    Sander, C.3
  • 25
    • 33750533388 scopus 로고    scopus 로고
    • Physicochemical modelling of cell signalling pathways
    • B.B. Aldridge, and J.M. Burke P.K. Sorger Physicochemical modelling of cell signalling pathways Nat. Cell Biol. 8 2006 1195 1203
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1195-1203
    • Aldridge, B.B.1    Burke, J.M.2    Sorger, P.K.3
  • 26
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • U.S. Bhalla, and R. Iyengar Emergent properties of networks of biological signaling pathways Science 283 1999 381 387
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 27
    • 43149108161 scopus 로고    scopus 로고
    • A bistable Rb-E2F switch underlies the restriction point
    • G. Yao, and T.J. Lee L. You A bistable Rb-E2F switch underlies the restriction point Nat. Cell Biol. 10 2008 476 482
    • (2008) Nat. Cell Biol. , vol.10 , pp. 476-482
    • Yao, G.1    Lee, T.J.2    You, L.3
  • 28
    • 34347381069 scopus 로고    scopus 로고
    • Irreversible cell-cycle transitions are due to systems-level feedback
    • B. Novak, and J.J. Tyson A. Csikasz-Nagy Irreversible cell-cycle transitions are due to systems-level feedback Nat. Cell Biol. 9 2007 724 728
    • (2007) Nat. Cell Biol. , vol.9 , pp. 724-728
    • Novak, B.1    Tyson, J.J.2    Csikasz-Nagy, A.3
  • 29
    • 80054713184 scopus 로고    scopus 로고
    • Steady states and dynamics of urokinase-mediated plasmin activation in silico and in vitro
    • L. Venkatraman, and H. Li L. Tucker-Kellogg Steady states and dynamics of urokinase-mediated plasmin activation in silico and in vitro Biophys. J. 101 2011 1825 1834
    • (2011) Biophys. J. , vol.101 , pp. 1825-1834
    • Venkatraman, L.1    Li, H.2    Tucker-Kellogg, L.3
  • 30
    • 0023199478 scopus 로고
    • Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study
    • V. Ellis, M.F. Scully, and V.V. Kakkar Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study J. Biol. Chem. 262 1987 14998 15003
    • (1987) J. Biol. Chem. , vol.262 , pp. 14998-15003
    • Ellis, V.1    Scully, M.F.2    Kakkar, V.V.3
  • 31
    • 0021082363 scopus 로고
    • The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity
    • M.A. Lucas, and D.L. Straight P.A. McKee The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity J. Biol. Chem. 258 1983 12171 12177
    • (1983) J. Biol. Chem. , vol.258 , pp. 12171-12177
    • Lucas, M.A.1    Straight, D.L.2    McKee, P.A.3
  • 32
    • 0024368891 scopus 로고
    • The mechanism of plasminogen activation and fibrin dissolution by single chain urokinase-type plasminogen activator in a plasma milieu in vitro
    • H.R. Lijnen, and B. Van Hoef D. Collen The mechanism of plasminogen activation and fibrin dissolution by single chain urokinase-type plasminogen activator in a plasma milieu in vitro Blood 73 1989 1864 1872
    • (1989) Blood , vol.73 , pp. 1864-1872
    • Lijnen, H.R.1    Van Hoef, B.2    Collen, D.3
  • 33
    • 34250350056 scopus 로고    scopus 로고
    • Modeling of the role of a Bax-activation switch in the mitochondrial apoptosis decision
    • C. Chen, and J. Cui P. Shen Modeling of the role of a Bax-activation switch in the mitochondrial apoptosis decision Biophys. J. 92 2007 4304 4315
    • (2007) Biophys. J. , vol.92 , pp. 4304-4315
    • Chen, C.1    Cui, J.2    Shen, P.3
  • 34
    • 44849128902 scopus 로고    scopus 로고
    • Two independent positive feedbacks and bistability in the Bcl-2 apoptotic switch
    • J. Cui, and C. Chen P. Shen Two independent positive feedbacks and bistability in the Bcl-2 apoptotic switch PLoS ONE 3 2008 e1469
    • (2008) PLoS ONE , vol.3 , pp. 1469
    • Cui, J.1    Chen, C.2    Shen, P.3
  • 35
    • 84874191665 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 36
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-β by thrombospondin-1: Mechanisms and physiology
    • J.E. Murphy-Ullrich, and M. Poczatek Activation of latent TGF-β by thrombospondin-1: mechanisms and physiology Cytokine Growth Factor Rev. 11 2000 59 69
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 37
    • 0034747099 scopus 로고    scopus 로고
    • TGF-β1-induced PAI-1 gene expression requires MEK activity and cell-to-substrate adhesion
    • S.M. Kutz, and J. Hordines P.J. Higgins TGF-β1-induced PAI-1 gene expression requires MEK activity and cell-to-substrate adhesion J. Cell Sci. 114 2001 3905 3914
    • (2001) J. Cell Sci. , vol.114 , pp. 3905-3914
    • Kutz, S.M.1    Hordines, J.2    Higgins, P.J.3
  • 38
    • 0025273735 scopus 로고
    • Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1
    • M.V. Cubellis, T.C. Wun, and F. Blasi Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1 EMBO J. 9 1990 1079 1085
    • (1990) EMBO J. , vol.9 , pp. 1079-1085
    • Cubellis, M.V.1    Wun, T.C.2    Blasi, F.3
  • 39
    • 0023711754 scopus 로고
    • Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator by plasminogen-activator inhibitor type 1 and type 2
    • S. Thorsen, and M. Philips B. Astedt Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator by plasminogen-activator inhibitor type 1 and type 2 Eur. J. Biochem. 175 1988 33 39
    • (1988) Eur. J. Biochem. , vol.175 , pp. 33-39
    • Thorsen, S.1    Philips, M.2    Astedt, B.3
  • 40
    • 0024508318 scopus 로고
    • Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes
    • V. Ellis, M.F. Scully, and V.V. Kakkar Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes J. Biol. Chem. 264 1989 2185 2188
    • (1989) J. Biol. Chem. , vol.264 , pp. 2185-2188
    • Ellis, V.1    Scully, M.F.2    Kakkar, V.V.3
  • 41
    • 0021741452 scopus 로고
    • Mechanism of α2-macroglobulin-proteinase interactions. Studies with trypsin and plasmin
    • U. Christensen, and L. Sottrup-Jensen Mechanism of α2- macroglobulin-proteinase interactions. Studies with trypsin and plasmin Biochemistry 23 1984 6619 6626
    • (1984) Biochemistry , vol.23 , pp. 6619-6626
    • Christensen, U.1    Sottrup-Jensen, L.2
  • 42
    • 0027459352 scopus 로고
    • Characterization of the antiplasmin activity of human thrombospondin-1 in solution
    • P.K. Anonick, and J.K. Yoo S.L. Gonias Characterization of the antiplasmin activity of human thrombospondin-1 in solution Biochem. J. 289 1993 903 909
    • (1993) Biochem. J. , vol.289 , pp. 903-909
    • Anonick, P.K.1    Yoo, J.K.2    Gonias, S.L.3
  • 43
    • 35348866243 scopus 로고    scopus 로고
    • Robustness analysis identifies the plausible model of the Bcl-2 apoptotic switch
    • C. Chen, and J. Cui P. Shen Robustness analysis identifies the plausible model of the Bcl-2 apoptotic switch FEBS Lett. 581 2007 5143 5150
    • (2007) FEBS Lett. , vol.581 , pp. 5143-5150
    • Chen, C.1    Cui, J.2    Shen, P.3
  • 44
    • 52449129045 scopus 로고    scopus 로고
    • Development of dual-compartment perfusion bioreactor for serial coculture of hepatocytes and stellate cells in poly(lactic-co-glycolic acid)-collagen scaffolds
    • F. Wen, and S. Chang H. Yu Development of dual-compartment perfusion bioreactor for serial coculture of hepatocytes and stellate cells in poly(lactic-co-glycolic acid)-collagen scaffolds J. Biomed. Mater. Res. B Appl. Biomater. 87 2008 154 162
    • (2008) J. Biomed. Mater. Res. B Appl. Biomater. , vol.87 , pp. 154-162
    • Wen, F.1    Chang, S.2    Yu, H.3
  • 45
    • 17644370659 scopus 로고    scopus 로고
    • Three-dimensional co-culture of hepatocytes and stellate cells
    • S.F. Abu-Absi, L.K. Hansen, and W.S. Hu Three-dimensional co-culture of hepatocytes and stellate cells Cytotechnology 45 2004 125 140
    • (2004) Cytotechnology , vol.45 , pp. 125-140
    • Abu-Absi, S.F.1    Hansen, L.K.2    Hu, W.S.3
  • 46
    • 0345700833 scopus 로고    scopus 로고
    • Building a cell cycle oscillator: Hysteresis and bistability in the activation of Cdc2
    • J.R. Pomerening, E.D. Sontag, and J.E. Ferrell Jr. Building a cell cycle oscillator: hysteresis and bistability in the activation of Cdc2 Nat. Cell Biol. 5 2003 346 351
    • (2003) Nat. Cell Biol. , vol.5 , pp. 346-351
    • Pomerening, J.R.1    Sontag, E.D.2    Ferrell Jr., J.E.3
  • 47
    • 41549132691 scopus 로고    scopus 로고
    • Quantitative analysis of pathways controlling extrinsic apoptosis in single cells
    • J.G. Albeck, and J.M. Burke P.K. Sorger Quantitative analysis of pathways controlling extrinsic apoptosis in single cells Mol. Cell 30 2008 11 25
    • (2008) Mol. Cell , vol.30 , pp. 11-25
    • Albeck, J.G.1    Burke, J.M.2    Sorger, P.K.3
  • 48
    • 0015351412 scopus 로고
    • Metabolism of plasminogen in healthy subjects: Effect of tranexamic acid
    • D. Collen, and G. Tytgat P. Wallén Metabolism of plasminogen in healthy subjects: effect of tranexamic acid J. Clin. Invest. 51 1972 1310 1318
    • (1972) J. Clin. Invest. , vol.51 , pp. 1310-1318
    • Collen, D.1    Tytgat, G.2    Wallén, P.3
  • 49
    • 1642296148 scopus 로고    scopus 로고
    • Type 1 plasminogen activator inhibitor deficiency aggravates the course of experimental glomerulonephritis through overactivation of transforming growth factor β
    • A. Hertig, and J. Berrou E. Rondeau Type 1 plasminogen activator inhibitor deficiency aggravates the course of experimental glomerulonephritis through overactivation of transforming growth factor β FASEB J. 17 2003 1904 1906
    • (2003) FASEB J. , vol.17 , pp. 1904-1906
    • Hertig, A.1    Berrou, J.2    Rondeau, E.3
  • 50
    • 77953685065 scopus 로고    scopus 로고
    • Cell-delivery therapeutics for liver regeneration
    • W. Zhang, and L. Tucker-Kellogg H. Yu Cell-delivery therapeutics for liver regeneration Adv. Drug Deliv. Rev. 62 2010 814 826
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 814-826
    • Zhang, W.1    Tucker-Kellogg, L.2    Yu, H.3
  • 51
    • 20144386753 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 deficiency retards diabetic nephropathy
    • S.B. Nicholas, and E. Aguiniga W.A. Hsueh Plasminogen activator inhibitor-1 deficiency retards diabetic nephropathy Kidney Int. 67 2005 1297 1307
    • (2005) Kidney Int. , vol.67 , pp. 1297-1307
    • Nicholas, S.B.1    Aguiniga, E.2    Hsueh, W.A.3
  • 52
    • 0034767501 scopus 로고    scopus 로고
    • Transforming growth factor β and the liver
    • D.M. Bissell, D. Roulot, and J. George Transforming growth factor β and the liver Hepatology 34 2001 859 867
    • (2001) Hepatology , vol.34 , pp. 859-867
    • Bissell, D.M.1    Roulot, D.2    George, J.3
  • 53
    • 0028289518 scopus 로고
    • Modulation of transforming growth factor β receptors of rat lipocytes during the hepatic wound healing response. Enhanced binding and reduced gene expression accompany cellular activation in culture and in vivo
    • S.L. Friedman, G. Yamasaki, and L. Wong Modulation of transforming growth factor β receptors of rat lipocytes during the hepatic wound healing response. Enhanced binding and reduced gene expression accompany cellular activation in culture and in vivo J. Biol. Chem. 269 1994 10551 10558
    • (1994) J. Biol. Chem. , vol.269 , pp. 10551-10558
    • Friedman, S.L.1    Yamasaki, G.2    Wong, L.3
  • 54
    • 0033036099 scopus 로고    scopus 로고
    • Role of transforming growth factor β type II receptor in hepatic fibrosis: Studies of human chronic hepatitis C and experimental fibrosis in rats
    • D. Roulot, and A.M. Sevcsik S. Marullo Role of transforming growth factor β type II receptor in hepatic fibrosis: studies of human chronic hepatitis C and experimental fibrosis in rats Hepatology 29 1999 1730 1738
    • (1999) Hepatology , vol.29 , pp. 1730-1738
    • Roulot, D.1    Sevcsik, A.M.2    Marullo, S.3
  • 55
    • 0025089051 scopus 로고
    • Regulation of plasmin, miniplasmin, and streptokinase-plasmin complex by α2-antiplasmin, α2-macroglobulin, and antithrombin III in the presence of heparin
    • P.K. Anonick, B. Wolf, and S.L. Gonias Regulation of plasmin, miniplasmin, and streptokinase-plasmin complex by α2-antiplasmin, α2-macroglobulin, and antithrombin III in the presence of heparin Thromb. Res. 59 1990 449 462
    • (1990) Thromb. Res. , vol.59 , pp. 449-462
    • Anonick, P.K.1    Wolf, B.2    Gonias, S.L.3
  • 56
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • J. Travis, and G.S. Salvesen Human plasma proteinase inhibitors Annu. Rev. Biochem. 52 1983 655 709
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 57
    • 4344674786 scopus 로고    scopus 로고
    • Bistability analyses of a caspase activation model for receptor-induced apoptosis
    • T. Eissing, and H. Conzelmann P. Scheurich Bistability analyses of a caspase activation model for receptor-induced apoptosis J. Biol. Chem. 279 2004 36892 36897
    • (2004) J. Biol. Chem. , vol.279 , pp. 36892-36897
    • Eissing, T.1    Conzelmann, H.2    Scheurich, P.3
  • 58
    • 33646124974 scopus 로고    scopus 로고
    • Bistability in apoptosis: Roles of bax, bcl-2, and mitochondrial permeability transition pores
    • E.Z. Bagci, and Y. Vodovotz I. Bahar Bistability in apoptosis: roles of bax, bcl-2, and mitochondrial permeability transition pores Biophys. J. 90 2006 1546 1559
    • (2006) Biophys. J. , vol.90 , pp. 1546-1559
    • Bagci, E.Z.1    Vodovotz, Y.2    Bahar, I.3
  • 59
    • 0025810460 scopus 로고
    • Half-life of single-chain urokinase-type plasminogen activator (scu-PA) and two-chain urokinase-type plasminogen activator (tcu-PA) in patients with acute myocardial infarction
    • M. Köhler, S. Sen, C. Miyashita, R. Hermes, G. Pindur, M. Heiden, G. Berg, S. Mörsdorf, G. Leipnitz, and M. Zeppezauer Half-life of single-chain urokinase-type plasminogen activator (scu-PA) and two-chain urokinase-type plasminogen activator (tcu-PA) in patients with acute myocardial infarction Thromb. Res. 62 1991 75 81
    • (1991) Thromb. Res. , vol.62 , pp. 75-81
    • Köhler, M.1    Sen, S.2    Miyashita, C.3    Hermes, R.4    Pindur, G.5    Heiden, M.6    Berg, G.7    Mörsdorf, S.8    Leipnitz, G.9    Zeppezauer, M.10
  • 60
    • 33749370199 scopus 로고    scopus 로고
    • Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability
    • S. Legewie, N. Blüthgen, and H. Herzel Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability PLOS Comput. Biol. 2 2006 e120
    • (2006) PLOS Comput. Biol. , vol.2 , pp. 120
    • Legewie, S.1    Blüthgen, N.2    Herzel, H.3
  • 61
  • 62
    • 0025255847 scopus 로고
    • The concentration of tissue plasminogen activator and urokinase in plasma and tissues of patients with ovarian and uterine tumors
    • K. Saito, and M. Nagashima A. Takada The concentration of tissue plasminogen activator and urokinase in plasma and tissues of patients with ovarian and uterine tumors Thromb. Res. 58 1990 355 366
    • (1990) Thromb. Res. , vol.58 , pp. 355-366
    • Saito, K.1    Nagashima, M.2    Takada, A.3
  • 63
    • 0038303500 scopus 로고    scopus 로고
    • A simple method for the simultaneous isolation of stellate cells and hepatocytes from rat liver tissue
    • L. Riccalton-Banks, and R. Bhandari K.M. Shakesheff A simple method for the simultaneous isolation of stellate cells and hepatocytes from rat liver tissue Mol. Cell. Biochem. 248 2003 97 102
    • (2003) Mol. Cell. Biochem. , vol.248 , pp. 97-102
    • Riccalton-Banks, L.1    Bhandari, R.2    Shakesheff, K.M.3
  • 64
    • 0033921113 scopus 로고    scopus 로고
    • An immortalized rat liver stellate cell line (HSC-T6): A new cell model for the study of retinoid metabolism in vitro
    • S. Vogel, and R. Piantedosi W.S. Blaner An immortalized rat liver stellate cell line (HSC-T6): a new cell model for the study of retinoid metabolism in vitro J. Lipid Res. 41 2000 882 893
    • (2000) J. Lipid Res. , vol.41 , pp. 882-893
    • Vogel, S.1    Piantedosi, R.2    Blaner, W.S.3
  • 65
    • 11844252576 scopus 로고    scopus 로고
    • Analysis of five streptokinase formulations using the euglobulin lysis test and the plasminogen activation assay
    • L.T. Couto, J.L. Donato, and G. de Nucci Analysis of five streptokinase formulations using the euglobulin lysis test and the plasminogen activation assay Braz. J. Med. Biol. Res. 37 2004 1889 1894
    • (2004) Braz. J. Med. Biol. Res. , vol.37 , pp. 1889-1894
    • Couto, L.T.1    Donato, J.L.2    De Nucci, G.3
  • 66
    • 39849102966 scopus 로고    scopus 로고
    • Direct effects of alcohol on hepatic fibrinolytic balance: Implications for alcoholic liver disease
    • D. Seth, and P.J. Hogg P.S. Haber Direct effects of alcohol on hepatic fibrinolytic balance: implications for alcoholic liver disease J. Hepatol. 48 2008 614 627
    • (2008) J. Hepatol. , vol.48 , pp. 614-627
    • Seth, D.1    Hogg, P.J.2    Haber, P.S.3
  • 67
    • 0024544506 scopus 로고
    • Activation of pro-urokinase and plasminogen on human sarcoma cells: A proteolytic system with surface-bound reactants
    • R.W. Stephens, and J. Pöllänen A. Vaheri Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic system with surface-bound reactants J. Cell Biol. 108 1989 1987 1995
    • (1989) J. Cell Biol. , vol.108 , pp. 1987-1995
    • Stephens, R.W.1    Pöllänen, J.2    Vaheri, A.3


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