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Volumn 6, Issue , 2015, Pages 565-577

Reciprocal regulation of TGF-β and reactive oxygen species: A perverse cycle for fibrosis

Author keywords

Fibrosis; NADPH oxidases; Oxidative stress; PAI 1; TGF

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TRANSFORMING GROWTH FACTOR BETA;

EID: 84944906108     PISSN: 22132317     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.redox.2015.09.009     Document Type: Review
Times cited : (502)

References (264)
  • 2
    • 0030024139 scopus 로고    scopus 로고
    • Oxidized BAL fluid proteins in patients with interstitial lung diseases
    • Lenz A.G., Costabel U., Maier K.L. Oxidized BAL fluid proteins in patients with interstitial lung diseases. Eur. Respir. J. 1996, 9:307-312.
    • (1996) Eur. Respir. J. , vol.9 , pp. 307-312
    • Lenz, A.G.1    Costabel, U.2    Maier, K.L.3
  • 3
    • 22044435952 scopus 로고    scopus 로고
    • Carbonylated proteins in bronchoalveolar lavage of patients with sarcoidosis, pulmonary fibrosis associated with systemic sclerosis and idiopathic pulmonary fibrosis
    • Rottoli P., Magi B., Cianti R., Bargagli E., Vagaggini C., Nikiforakis N., Pallini V., Bini L. Carbonylated proteins in bronchoalveolar lavage of patients with sarcoidosis, pulmonary fibrosis associated with systemic sclerosis and idiopathic pulmonary fibrosis. Proteomics 2005, 5:2612-2618.
    • (2005) Proteomics , vol.5 , pp. 2612-2618
    • Rottoli, P.1    Magi, B.2    Cianti, R.3    Bargagli, E.4    Vagaggini, C.5    Nikiforakis, N.6    Pallini, V.7    Bini, L.8
  • 5
    • 74149085153 scopus 로고    scopus 로고
    • Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis
    • Liu R.M., Gaston Pravia K.A. Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis. Free. Radic. Biol. Med. 2010, 48:1-15.
    • (2010) Free. Radic. Biol. Med. , vol.48 , pp. 1-15
    • Liu, R.M.1    Gaston Pravia, K.A.2
  • 6
    • 0026010305 scopus 로고
    • Transforming growth factor beta 1 is present at sites of extracellular matrix gene expression in human pulmonary fibrosis
    • Broekelmann T.J., Limper A.H., Colby T.V., McDonald J.A. Transforming growth factor beta 1 is present at sites of extracellular matrix gene expression in human pulmonary fibrosis. Proc. Natl. Acad. Sci. USA 1991, 88:6642-6646.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6642-6646
    • Broekelmann, T.J.1    Limper, A.H.2    Colby, T.V.3    McDonald, J.A.4
  • 10
    • 54949158787 scopus 로고    scopus 로고
    • New insights into the mechanisms of fibrosis and sclerosis in diabetic nephropathy
    • Brosius F. New insights into the mechanisms of fibrosis and sclerosis in diabetic nephropathy. Rev. Endocr. Metab. Disord. 2008, 9:245-254.
    • (2008) Rev. Endocr. Metab. Disord. , vol.9 , pp. 245-254
    • Brosius, F.1
  • 12
    • 0027768803 scopus 로고
    • Immunohistochemical localization of transforming growth factor-beta 1 in rats with experimental silicosis, alveolar type II hyperplasia, and lung cancer
    • Williams A.O., Flanders K.C., Saffiotti U. Immunohistochemical localization of transforming growth factor-beta 1 in rats with experimental silicosis, alveolar type II hyperplasia, and lung cancer. Am. J. Pathol. 1993, 142:1831-1840.
    • (1993) Am. J. Pathol. , vol.142 , pp. 1831-1840
    • Williams, A.O.1    Flanders, K.C.2    Saffiotti, U.3
  • 13
    • 0031059572 scopus 로고    scopus 로고
    • Transforming growth factors-beta 1, -beta 2, and -beta 3 stimulate fibroblast procollagen production in vitro but are differentially expressed during bleomycin-induced lung fibrosis
    • Coker R.K., Laurent G.J., Shahzeidi S., Lympany P.A., du Bois R.M., Jeffery P.K., McAnulty R.J. Transforming growth factors-beta 1, -beta 2, and -beta 3 stimulate fibroblast procollagen production in vitro but are differentially expressed during bleomycin-induced lung fibrosis. Am. J. Pathol. 1997, 150:981-991.
    • (1997) Am. J. Pathol. , vol.150 , pp. 981-991
    • Coker, R.K.1    Laurent, G.J.2    Shahzeidi, S.3    Lympany, P.A.4    du Bois, R.M.5    Jeffery, P.K.6    McAnulty, R.J.7
  • 14
    • 0342264524 scopus 로고    scopus 로고
    • Dose-dependent induction of transforming growth factor beta (TGF-beta) in the lung tissue of fibrosis-prone mice after thoracic irradiation
    • Rube C.E., Uthe D., Schmid K.W., Richter K.D., Wessel J., Schuck A., Willich N., Rube C. Dose-dependent induction of transforming growth factor beta (TGF-beta) in the lung tissue of fibrosis-prone mice after thoracic irradiation. Int. J. Radiat. Oncol. Biol. Phys. 2000, 47:1033-1042.
    • (2000) Int. J. Radiat. Oncol. Biol. Phys. , vol.47 , pp. 1033-1042
    • Rube, C.E.1    Uthe, D.2    Schmid, K.W.3    Richter, K.D.4    Wessel, J.5    Schuck, A.6    Willich, N.7    Rube, C.8
  • 15
    • 2042512329 scopus 로고    scopus 로고
    • Expression of growth factors by airway epithelial cells in a model of chronic asthma: regulation and relationship to subepithelial fibrosis
    • Kumar R.K., Herbert C., Foster P.S. Expression of growth factors by airway epithelial cells in a model of chronic asthma: regulation and relationship to subepithelial fibrosis. Clin. Exp. Allergy 2004, 34:567-575.
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 567-575
    • Kumar, R.K.1    Herbert, C.2    Foster, P.S.3
  • 17
  • 18
    • 48449106999 scopus 로고    scopus 로고
    • Pentoxifylline inhibits transforming growth factor-beta signaling and renal fibrosis in experimental crescentic glomerulonephritis in rats
    • Ng Y.Y., Chen Y.M., Tsai T.J., Lan X.R., Yang W.C., Lan H.Y. Pentoxifylline inhibits transforming growth factor-beta signaling and renal fibrosis in experimental crescentic glomerulonephritis in rats. Am. J. Nephrol. 2009, 29:43-53.
    • (2009) Am. J. Nephrol. , vol.29 , pp. 43-53
    • Ng, Y.Y.1    Chen, Y.M.2    Tsai, T.J.3    Lan, X.R.4    Yang, W.C.5    Lan, H.Y.6
  • 21
    • 9744257028 scopus 로고    scopus 로고
    • Conditional overexpression of bioactive transforming growth factor-beta1 in neonatal mouse lung: a new model for bronchopulmonary dysplasia?
    • Vicencio A.G., Lee C.G., Cho S.J., Eickelberg O., Chuu Y., Haddad G.G., Elias J.A. Conditional overexpression of bioactive transforming growth factor-beta1 in neonatal mouse lung: a new model for bronchopulmonary dysplasia?. Am. J. Respir. Cell Mol. Biol. 2004, 31:650-656.
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , pp. 650-656
    • Vicencio, A.G.1    Lee, C.G.2    Cho, S.J.3    Eickelberg, O.4    Chuu, Y.5    Haddad, G.G.6    Elias, J.A.7
  • 22
    • 0030800795 scopus 로고    scopus 로고
    • Adenovector-mediated gene transfer of active transforming growth factor-beta1 induces prolonged severe fibrosis in rat lung
    • Sime P.J., Xing Z., Graham F.L., Csaky K.G., Gauldie J. Adenovector-mediated gene transfer of active transforming growth factor-beta1 induces prolonged severe fibrosis in rat lung. J. Clin. Investig. 1997, 100:768-776.
    • (1997) J. Clin. Investig. , vol.100 , pp. 768-776
    • Sime, P.J.1    Xing, Z.2    Graham, F.L.3    Csaky, K.G.4    Gauldie, J.5
  • 23
    • 0035984567 scopus 로고    scopus 로고
    • Differences in the fibrogenic response after transfer of active transforming growth factor-beta1 gene to lungs of "fibrosis-prone" and "fibrosis-resistant" mouse strains
    • Kolb M., Bonniaud P., Galt T., Sime P.J., Kelly M.M., Margetts P.J., Gauldie J. Differences in the fibrogenic response after transfer of active transforming growth factor-beta1 gene to lungs of "fibrosis-prone" and "fibrosis-resistant" mouse strains. Am. J. Respir. Cell Mol. Biol. 2002, 27:141-150.
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.27 , pp. 141-150
    • Kolb, M.1    Bonniaud, P.2    Galt, T.3    Sime, P.J.4    Kelly, M.M.5    Margetts, P.J.6    Gauldie, J.7
  • 26
    • 84855397962 scopus 로고    scopus 로고
    • Therapeutic value of small molecule inhibitor to plasminogen activator inhibitor-1 for lung fibrosis
    • Huang W.T., Vayalil P.K., Miyata T., Hagood J., Liu R.M. Therapeutic value of small molecule inhibitor to plasminogen activator inhibitor-1 for lung fibrosis. Am. J. Respir. Cell Mol. Biol. 2012, 46:87-95.
    • (2012) Am. J. Respir. Cell Mol. Biol. , vol.46 , pp. 87-95
    • Huang, W.T.1    Vayalil, P.K.2    Miyata, T.3    Hagood, J.4    Liu, R.M.5
  • 30
    • 0027425864 scopus 로고
    • Effect of antibody to transforming growth factor beta on bleomycin induced accumulation of lung collagen in mice
    • Giri S.N., Hyde D.M., Hollinger M.A. Effect of antibody to transforming growth factor beta on bleomycin induced accumulation of lung collagen in mice. Thorax 1993, 48:959-966.
    • (1993) Thorax , vol.48 , pp. 959-966
    • Giri, S.N.1    Hyde, D.M.2    Hollinger, M.A.3
  • 32
    • 0032771311 scopus 로고    scopus 로고
    • Reduction of bleomycin induced lung fibrosis by transforming growth factor beta soluble receptor in hamsters
    • Wang Q., Wang Y., Hyde D.M., Gotwals P.J., Koteliansky V.E., Ryan S.T., Giri S.N. Reduction of bleomycin induced lung fibrosis by transforming growth factor beta soluble receptor in hamsters. Thorax 1999, 54:805-812.
    • (1999) Thorax , vol.54 , pp. 805-812
    • Wang, Q.1    Wang, Y.2    Hyde, D.M.3    Gotwals, P.J.4    Koteliansky, V.E.5    Ryan, S.T.6    Giri, S.N.7
  • 37
    • 35048875855 scopus 로고    scopus 로고
    • TGF-beta signaling: a tale of two responses
    • Rahimi R.A., Leof E.B. TGF-beta signaling: a tale of two responses. J. Cell. Biochem. 2007, 102:593-608.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 593-608
    • Rahimi, R.A.1    Leof, E.B.2
  • 38
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • Derynck R., Zhang Y.E. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 2003, 425:577-584.
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 39
    • 42649120148 scopus 로고    scopus 로고
    • Smad7 as a therapeutic agent for chronic kidney diseases
    • Lan H.Y. Smad7 as a therapeutic agent for chronic kidney diseases. Front. Biosci. 2008, 13:4984-4992.
    • (2008) Front. Biosci. , vol.13 , pp. 4984-4992
    • Lan, H.Y.1
  • 41
    • 0035958625 scopus 로고    scopus 로고
    • Transforming growth factor beta signal transduction in hepatic stellate cells via Smad2/3 phosphorylation, a pathway that is abrogated during in vitro progression to myofibroblasts. TGFbeta signal transduction during transdifferentiation of hepatic stellate cells
    • Dooley S., Delvoux B., Streckert M., Bonzel L., Stopa M., ten Dijke P., Gressner A.M. Transforming growth factor beta signal transduction in hepatic stellate cells via Smad2/3 phosphorylation, a pathway that is abrogated during in vitro progression to myofibroblasts. TGFbeta signal transduction during transdifferentiation of hepatic stellate cells. FEBS Lett. 2001, 502:4-10.
    • (2001) FEBS Lett. , vol.502 , pp. 4-10
    • Dooley, S.1    Delvoux, B.2    Streckert, M.3    Bonzel, L.4    Stopa, M.5    ten Dijke, P.6    Gressner, A.M.7
  • 44
    • 84863392473 scopus 로고    scopus 로고
    • Oxymatrine inhibits collagen synthesis in keloid fibroblasts via inhibition of transforming growth factor-beta1/Smad signaling pathway
    • Fan D.L., Zhao W.J., Wang Y.X., Han S.Y., Guo S. Oxymatrine inhibits collagen synthesis in keloid fibroblasts via inhibition of transforming growth factor-beta1/Smad signaling pathway. Int. J. Dermatol. 2012, 51:463-472.
    • (2012) Int. J. Dermatol. , vol.51 , pp. 463-472
    • Fan, D.L.1    Zhao, W.J.2    Wang, Y.X.3    Han, S.Y.4    Guo, S.5
  • 45
    • 0037377993 scopus 로고    scopus 로고
    • N-Acetyl-seryl-aspartyl-lysyl-proline inhibits TGF-beta-mediated plasminogen activator inhibitor-1 expression via inhibition of Smad pathway in human mesangial cells
    • Kanasaki K., Koya D., Sugimoto T., Isono M., Kashiwagi A., Haneda M. N-Acetyl-seryl-aspartyl-lysyl-proline inhibits TGF-beta-mediated plasminogen activator inhibitor-1 expression via inhibition of Smad pathway in human mesangial cells. J. Am. Soc. Nephrol. 2003, 14:863-872.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 863-872
    • Kanasaki, K.1    Koya, D.2    Sugimoto, T.3    Isono, M.4    Kashiwagi, A.5    Haneda, M.6
  • 46
    • 84906043420 scopus 로고    scopus 로고
    • Hierarchy of molecules in TGF-beta1 signaling relevant to myofibroblast activation and renal fibrosis
    • Zhan M., Kanwar Y.S. Hierarchy of molecules in TGF-beta1 signaling relevant to myofibroblast activation and renal fibrosis. Am. J. Physiol. Ren. Physiol. 2014, 307:F385-F387.
    • (2014) Am. J. Physiol. Ren. Physiol. , vol.307 , pp. F385-F387
    • Zhan, M.1    Kanwar, Y.S.2
  • 47
    • 84865808428 scopus 로고    scopus 로고
    • The impact of TGF-beta on lung fibrosis: from targeting to biomarkers
    • Fernandez I.E., Eickelberg O. The impact of TGF-beta on lung fibrosis: from targeting to biomarkers. Proc. Am. Thorac. Soc. 2012, 9:111-116.
    • (2012) Proc. Am. Thorac. Soc. , vol.9 , pp. 111-116
    • Fernandez, I.E.1    Eickelberg, O.2
  • 51
    • 0037099745 scopus 로고    scopus 로고
    • TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses
    • Yu L., Hebert M.C., Zhang Y.E. TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses. EMBO J. 2002, 21:3749-3759.
    • (2002) EMBO J. , vol.21 , pp. 3749-3759
    • Yu, L.1    Hebert, M.C.2    Zhang, Y.E.3
  • 52
  • 53
    • 36349007768 scopus 로고    scopus 로고
    • Glutathione suppresses TGF-beta-induced PAI-1 expression by inhibiting p38 and JNK MAPK and the binding of AP-1, SP-1, and Smad to the PAI-1 promoter
    • Vayalil P.K., Iles K.E., Choi J., Yi A.K., Postlethwait E.M., Liu R.M. Glutathione suppresses TGF-beta-induced PAI-1 expression by inhibiting p38 and JNK MAPK and the binding of AP-1, SP-1, and Smad to the PAI-1 promoter. Am. J. Physiol. Lung Cell. Mol. Physiol. 2007, 293:L1281-L1292.
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.293 , pp. L1281-L1292
    • Vayalil, P.K.1    Iles, K.E.2    Choi, J.3    Yi, A.K.4    Postlethwait, E.M.5    Liu, R.M.6
  • 54
    • 27944495712 scopus 로고    scopus 로고
    • Glutathione restores collagen degradation in TGF-beta-treated fibroblasts by blocking plasminogen activator inhibitor-1 expression and activating plasminogen
    • Vayalil P.K., Olman M., Murphy-Ullrich J.E., Postlethwait E.M., Liu R.M. Glutathione restores collagen degradation in TGF-beta-treated fibroblasts by blocking plasminogen activator inhibitor-1 expression and activating plasminogen. Am. J. Physiol. Lung Cell. Mol. Physiol. 2005, 289:L937-L945.
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.289 , pp. L937-L945
    • Vayalil, P.K.1    Olman, M.2    Murphy-Ullrich, J.E.3    Postlethwait, E.M.4    Liu, R.M.5
  • 55
    • 34249845879 scopus 로고    scopus 로고
    • Transforming growth factor-beta receptor type I-dependent fibrogenic gene program is mediated via activation of Smad1 and ERK1/2 pathways
    • Pannu J., Nakerakanti S., Smith E., ten Dijke P., Trojanowska M. Transforming growth factor-beta receptor type I-dependent fibrogenic gene program is mediated via activation of Smad1 and ERK1/2 pathways. J. Biol. Chem. 2007, 282:10405-10413.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10405-10413
    • Pannu, J.1    Nakerakanti, S.2    Smith, E.3    ten Dijke, P.4    Trojanowska, M.5
  • 58
    • 84868305344 scopus 로고    scopus 로고
    • TGF-beta signaling in tissue fibrosis: redox controls, target genes and therapeutic opportunities
    • Samarakoon R., Overstreet J.M., Higgins P.J. TGF-beta signaling in tissue fibrosis: redox controls, target genes and therapeutic opportunities. Cell. Signal. 2013, 25:264-268.
    • (2013) Cell. Signal. , vol.25 , pp. 264-268
    • Samarakoon, R.1    Overstreet, J.M.2    Higgins, P.J.3
  • 59
    • 84893415235 scopus 로고    scopus 로고
    • NADPH oxidase-dependent redox signaling in TGF-beta-mediated fibrotic responses
    • Jiang F., Liu G.S., Dusting G.J., Chan E.C. NADPH oxidase-dependent redox signaling in TGF-beta-mediated fibrotic responses. Redox Biol. 2014, 2:267-272.
    • (2014) Redox Biol. , vol.2 , pp. 267-272
    • Jiang, F.1    Liu, G.S.2    Dusting, G.J.3    Chan, E.C.4
  • 60
    • 84896133689 scopus 로고    scopus 로고
    • Redox signaling as a therapeutic target to inhibit myofibroblast activation in degenerative fibrotic disease
    • Sampson N., Berger P., Zenzmaier C. Redox signaling as a therapeutic target to inhibit myofibroblast activation in degenerative fibrotic disease. Biomed. Res. Int. 2014, 2014:131737.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 131737
    • Sampson, N.1    Berger, P.2    Zenzmaier, C.3
  • 61
    • 84904357131 scopus 로고    scopus 로고
    • RhoA/Rho kinase mediates TGF-beta1-induced kidney myofibroblast activation through Poldip2/Nox4-derived reactive oxygen species
    • Manickam N., Patel M., Griendling K.K., Gorin Y., Barnes J.L. RhoA/Rho kinase mediates TGF-beta1-induced kidney myofibroblast activation through Poldip2/Nox4-derived reactive oxygen species. Am. J. Physiol. Ren. Physiol. 2014, 307:F159-F171.
    • (2014) Am. J. Physiol. Ren. Physiol. , vol.307 , pp. F159-F171
    • Manickam, N.1    Patel, M.2    Griendling, K.K.3    Gorin, Y.4    Barnes, J.L.5
  • 62
    • 34147209859 scopus 로고    scopus 로고
    • Diverse signaling pathways regulate fibroblast differentiation and transformation through Rho kinase activation
    • Harvey K.A., Paranavitana C.N., Zaloga G.P., Siddiqui R.A. Diverse signaling pathways regulate fibroblast differentiation and transformation through Rho kinase activation. J. Cell. Physiol. 2007, 211:353-363.
    • (2007) J. Cell. Physiol. , vol.211 , pp. 353-363
    • Harvey, K.A.1    Paranavitana, C.N.2    Zaloga, G.P.3    Siddiqui, R.A.4
  • 63
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman S.J., Ridley A.J. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 2008, 9:690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 64
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: coordinating cell responses
    • Ridley A.J. Rho family proteins: coordinating cell responses. Trends Cell. Biol. 2001, 11:471-477.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 65
    • 84903648153 scopus 로고    scopus 로고
    • Cellular mechanisms of tissue fibrosis. 8. Current and future drug targets in fibrosis: focus on Rho GTPase-regulated gene transcription
    • Tsou P.S., Haak A.J., Khanna D., Neubig R.R. Cellular mechanisms of tissue fibrosis. 8. Current and future drug targets in fibrosis: focus on Rho GTPase-regulated gene transcription. Am. J. Physiol. Cell Physiol. 2014, 307:C2-13.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.307 , pp. C2-13
    • Tsou, P.S.1    Haak, A.J.2    Khanna, D.3    Neubig, R.R.4
  • 67
    • 84893643399 scopus 로고    scopus 로고
    • Novel Rho/MRTF/SRF inhibitors block matrix-stiffness and TGF-beta-induced fibrogenesis in human colonic myofibroblasts
    • Johnson L.A., Rodansky E.S., Haak A.J., Larsen S.D., Neubig R.R., Higgins P.D. Novel Rho/MRTF/SRF inhibitors block matrix-stiffness and TGF-beta-induced fibrogenesis in human colonic myofibroblasts. Inflamm. Bowel Dis. 2014, 20:154-165.
    • (2014) Inflamm. Bowel Dis. , vol.20 , pp. 154-165
    • Johnson, L.A.1    Rodansky, E.S.2    Haak, A.J.3    Larsen, S.D.4    Neubig, R.R.5    Higgins, P.D.6
  • 68
    • 4744347777 scopus 로고    scopus 로고
    • Activation of Rho/Rho kinase signaling pathway by reactive oxygen species in rat aorta
    • Jin L., Ying Z., Webb R.C. Activation of Rho/Rho kinase signaling pathway by reactive oxygen species in rat aorta. Am. J. Physiol. Heart Circ. Physiol. 2004, 287:H1495-H1500.
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.287 , pp. H1495-H1500
    • Jin, L.1    Ying, Z.2    Webb, R.C.3
  • 69
    • 21644490277 scopus 로고    scopus 로고
    • Reactive oxygen species from smooth muscle mitochondria initiate cold-induced constriction of cutaneous arteries
    • Bailey S.R., Mitra S., Flavahan S., Flavahan N.A. Reactive oxygen species from smooth muscle mitochondria initiate cold-induced constriction of cutaneous arteries. Am. J. Physiol. Heart Circ. Physiol. 2005, 289:H243-H250.
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289 , pp. H243-H250
    • Bailey, S.R.1    Mitra, S.2    Flavahan, S.3    Flavahan, N.A.4
  • 70
    • 24744433531 scopus 로고    scopus 로고
    • Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases
    • Heo J., Campbell S.L. Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases. J. Biol. Chem. 2005, 280:31003-31010.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31003-31010
    • Heo, J.1    Campbell, S.L.2
  • 72
    • 77951209408 scopus 로고    scopus 로고
    • Direct activation of RhoA by reactive oxygen species requires a redox-sensitive motif
    • Aghajanian A., Wittchen E.S., Campbell S.L., Burridge K. Direct activation of RhoA by reactive oxygen species requires a redox-sensitive motif. PloS One 2009, 4:e8045.
    • (2009) PloS One , vol.4 , pp. e8045
    • Aghajanian, A.1    Wittchen, E.S.2    Campbell, S.L.3    Burridge, K.4
  • 73
    • 84867696986 scopus 로고    scopus 로고
    • Diabetes-induced increased oxidative stress in cardiomyocytes is sustained by a positive feedback loop involving Rho kinase and PKCbeta2
    • Soliman H., Gador A., Lu Y.H., Lin G., Bankar G., MacLeod K.M. Diabetes-induced increased oxidative stress in cardiomyocytes is sustained by a positive feedback loop involving Rho kinase and PKCbeta2. Am. J. Physiol. Heart Circ. Physiol. 2012, 303:H989-H1000.
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.303 , pp. H989-H1000
    • Soliman, H.1    Gador, A.2    Lu, Y.H.3    Lin, G.4    Bankar, G.5    MacLeod, K.M.6
  • 75
    • 85012056742 scopus 로고    scopus 로고
    • Biological activities of reactive oxygen and nitrogen species: oxidative stress versus signal transduction
    • Weidinger A., Kozlov A.V. Biological activities of reactive oxygen and nitrogen species: oxidative stress versus signal transduction. Biomolecules 2015, 5:472-484.
    • (2015) Biomolecules , vol.5 , pp. 472-484
    • Weidinger, A.1    Kozlov, A.V.2
  • 76
    • 0035078341 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) mediates the mitochondrial-dependent apoptosis induced by transforming growth factor (beta) in fetal hepatocytes
    • Herrera B., Alvarez A.M., Sanchez A., Fernandez M., Roncero C., Benito M., Fabregat I. Reactive oxygen species (ROS) mediates the mitochondrial-dependent apoptosis induced by transforming growth factor (beta) in fetal hepatocytes. FASEB J. 2001, 15:741-751.
    • (2001) FASEB J. , vol.15 , pp. 741-751
    • Herrera, B.1    Alvarez, A.M.2    Sanchez, A.3    Fernandez, M.4    Roncero, C.5    Benito, M.6    Fabregat, I.7
  • 77
    • 0037696460 scopus 로고    scopus 로고
    • Mitochondrial and microsomal derived reactive oxygen species mediate apoptosis induced by transforming growth factor-beta1 in immortalized rat hepatocytes
    • Albright C.D., Salganik R.I., Craciunescu C.N., Mar M.H., Zeisel S.H. Mitochondrial and microsomal derived reactive oxygen species mediate apoptosis induced by transforming growth factor-beta1 in immortalized rat hepatocytes. J. Cell. Biochem. 2003, 89:254-261.
    • (2003) J. Cell. Biochem. , vol.89 , pp. 254-261
    • Albright, C.D.1    Salganik, R.I.2    Craciunescu, C.N.3    Mar, M.H.4    Zeisel, S.H.5
  • 78
    • 0347318117 scopus 로고    scopus 로고
    • Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-[beta] in fetal rat hepatocytes
    • Herrera B., Murillo M.M., Alvarez-Barrientos A., Beltran J., Fernandez M., Fabregat I. Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-[beta] in fetal rat hepatocytes. Free Radic. Biol. Med. 2004, 36:16-26.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 16-26
    • Herrera, B.1    Murillo, M.M.2    Alvarez-Barrientos, A.3    Beltran, J.4    Fernandez, M.5    Fabregat, I.6
  • 79
    • 36248990744 scopus 로고    scopus 로고
    • Transforming growth factor beta mediates hepatocyte apoptosis through Smad3 generation of reactive oxygen species
    • Black D., Lyman S., Qian T., Lemasters J.J., Rippe R.A., Nitta T., Kim J.S., Behrns K.E. Transforming growth factor beta mediates hepatocyte apoptosis through Smad3 generation of reactive oxygen species. Biochimie 2007, 89:1464-1473.
    • (2007) Biochimie , vol.89 , pp. 1464-1473
    • Black, D.1    Lyman, S.2    Qian, T.3    Lemasters, J.J.4    Rippe, R.A.5    Nitta, T.6    Kim, J.S.7    Behrns, K.E.8
  • 80
    • 84860850926 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B (PTP1B) deficiency confers resistance to transforming growth factor-beta (TGF-beta)-induced suppressor effects in hepatocytes
    • Ortiz C., Caja L., Bertran E., Gonzalez-Rodriguez A., Valverde A.M., Fabregat I., Sancho P. Protein-tyrosine phosphatase 1B (PTP1B) deficiency confers resistance to transforming growth factor-beta (TGF-beta)-induced suppressor effects in hepatocytes. J. Biol. Chem. 2012, 287:15263-15274.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15263-15274
    • Ortiz, C.1    Caja, L.2    Bertran, E.3    Gonzalez-Rodriguez, A.4    Valverde, A.M.5    Fabregat, I.6    Sancho, P.7
  • 81
    • 16244377705 scopus 로고    scopus 로고
    • TGF beta1 induces prolonged mitochondrial ROS generation through decreased complex IV activity with senescent arrest in Mv1Lu cells
    • Yoon Y.S., Lee J.H., Hwang S.C., Choi K.S., Yoon G. TGF beta1 induces prolonged mitochondrial ROS generation through decreased complex IV activity with senescent arrest in Mv1Lu cells. Oncogene 2005, 24:1895-1903.
    • (2005) Oncogene , vol.24 , pp. 1895-1903
    • Yoon, Y.S.1    Lee, J.H.2    Hwang, S.C.3    Choi, K.S.4    Yoon, G.5
  • 82
    • 84863785173 scopus 로고    scopus 로고
    • GSK3 inactivation is involved in mitochondrial complex IV defect in transforming growth factor (TGF) beta1-induced senescence
    • Byun H.O., Jung H.J., Seo Y.H., Lee Y.K., Hwang S.C., Hwang E.S., Yoon G. GSK3 inactivation is involved in mitochondrial complex IV defect in transforming growth factor (TGF) beta1-induced senescence. Exp. Cell Res. 2012, 318:1808-1819.
    • (2012) Exp. Cell Res. , vol.318 , pp. 1808-1819
    • Byun, H.O.1    Jung, H.J.2    Seo, Y.H.3    Lee, Y.K.4    Hwang, S.C.5    Hwang, E.S.6    Yoon, G.7
  • 83
    • 84901484906 scopus 로고    scopus 로고
    • TGF-beta1 induces senescence of bone marrow mesenchymal stem cells via increase of mitochondrial ROS production
    • Wu J., Niu J., Li X., Wang X., Guo Z., Zhang F. TGF-beta1 induces senescence of bone marrow mesenchymal stem cells via increase of mitochondrial ROS production. BMC Dev. Biol. 2014, 14:21.
    • (2014) BMC Dev. Biol. , vol.14 , pp. 21
    • Wu, J.1    Niu, J.2    Li, X.3    Wang, X.4    Guo, Z.5    Zhang, F.6
  • 87
    • 84887578740 scopus 로고    scopus 로고
    • TGF-beta1 stimulates mitochondrial oxidative phosphorylation and generation of reactive oxygen species in cultured mouse podocytes, mediated in part by the mTOR pathway
    • Abe Y., Sakairi T., Beeson C., Kopp J.B. TGF-beta1 stimulates mitochondrial oxidative phosphorylation and generation of reactive oxygen species in cultured mouse podocytes, mediated in part by the mTOR pathway. Am. J. Physiol. Ren. Physiol. 2013, 305:F1477-F1490.
    • (2013) Am. J. Physiol. Ren. Physiol. , vol.305 , pp. F1477-F1490
    • Abe, Y.1    Sakairi, T.2    Beeson, C.3    Kopp, J.B.4
  • 88
    • 84879398211 scopus 로고    scopus 로고
    • TGF-beta signalling and reactive oxygen species drive fibrosis and matrix remodelling in myxomatous mitral valves
    • Hagler M.A., Hadley T.M., Zhang H., Mehra K., Roos C.M., Schaff H.V., Suri R.M., Miller J.D. TGF-beta signalling and reactive oxygen species drive fibrosis and matrix remodelling in myxomatous mitral valves. Cardiovasc. Res. 2013, 99:175-184.
    • (2013) Cardiovasc. Res. , vol.99 , pp. 175-184
    • Hagler, M.A.1    Hadley, T.M.2    Zhang, H.3    Mehra, K.4    Roos, C.M.5    Schaff, H.V.6    Suri, R.M.7    Miller, J.D.8
  • 89
    • 3543056882 scopus 로고    scopus 로고
    • Asbestos-derived reactive oxygen species activate TGF-beta1
    • Pociask D.A., Sime P.J., Brody A.R. Asbestos-derived reactive oxygen species activate TGF-beta1. Lab. Investig. 2004, 84:1013-1023.
    • (2004) Lab. Investig. , vol.84 , pp. 1013-1023
    • Pociask, D.A.1    Sime, P.J.2    Brody, A.R.3
  • 90
    • 84892882170 scopus 로고    scopus 로고
    • Activation of NADPH oxidase subunit NCF4 induces ROS-mediated EMT signaling in HeLa cells
    • Kim Y.M., Cho M. Activation of NADPH oxidase subunit NCF4 induces ROS-mediated EMT signaling in HeLa cells. Cell. Signal. 2014, 26:784-796.
    • (2014) Cell. Signal. , vol.26 , pp. 784-796
    • Kim, Y.M.1    Cho, M.2
  • 91
    • 58549101268 scopus 로고    scopus 로고
    • The inhibition of the epidermal growth factor (EGF) pathway enhances TGF-beta-induced apoptosis in rat hepatoma cells through inducing oxidative stress coincident with a change in the expression pattern of the NADPH oxidases (NOX) isoforms
    • Sancho P., Bertran E., Caja L., Carmona-Cuenca I., Murillo M.M., Fabregat I. The inhibition of the epidermal growth factor (EGF) pathway enhances TGF-beta-induced apoptosis in rat hepatoma cells through inducing oxidative stress coincident with a change in the expression pattern of the NADPH oxidases (NOX) isoforms. Biochim. Biophys. Acta 2009, 1793:253-263.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 253-263
    • Sancho, P.1    Bertran, E.2    Caja, L.3    Carmona-Cuenca, I.4    Murillo, M.M.5    Fabregat, I.6
  • 95
    • 64249168985 scopus 로고    scopus 로고
    • NOX4 mediates hypoxia-induced proliferation of human pulmonary artery smooth muscle cells: the role of autocrine production of transforming growth factor-{beta}1 and insulin-like growth factor binding protein-3
    • Ismail S., Sturrock A., Wu P., Cahill B., Norman K., Huecksteadt T., Sanders K., Kennedy T., Hoidal J. NOX4 mediates hypoxia-induced proliferation of human pulmonary artery smooth muscle cells: the role of autocrine production of transforming growth factor-{beta}1 and insulin-like growth factor binding protein-3. Am. J. Physiol. Lung Cell. Mol. Physiol. 2009, 296:L489-L499.
    • (2009) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.296 , pp. L489-L499
    • Ismail, S.1    Sturrock, A.2    Wu, P.3    Cahill, B.4    Norman, K.5    Huecksteadt, T.6    Sanders, K.7    Kennedy, T.8    Hoidal, J.9
  • 96
    • 27644456575 scopus 로고    scopus 로고
    • NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts
    • Cucoranu I., Clempus R., Dikalova A., Phelan P.J., Ariyan S., Dikalov S., Sorescu D. NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts. Circ. Res. 2005, 97:900-907.
    • (2005) Circ. Res. , vol.97 , pp. 900-907
    • Cucoranu, I.1    Clempus, R.2    Dikalova, A.3    Phelan, P.J.4    Ariyan, S.5    Dikalov, S.6    Sorescu, D.7
  • 97
    • 34447122529 scopus 로고    scopus 로고
    • Activation of NADPH oxidase by transforming growth factor-beta in hepatocytes mediates up-regulation of epidermal growth factor receptor ligands through a nuclear factor-kappaB-dependent mechanism
    • Murillo M.M., Carmona-Cuenca I., Del Castillo G., Ortiz C., Roncero C., Sanchez A., Fernandez M., Fabregat I. Activation of NADPH oxidase by transforming growth factor-beta in hepatocytes mediates up-regulation of epidermal growth factor receptor ligands through a nuclear factor-kappaB-dependent mechanism. Biochem. J. 2007, 405:251-259.
    • (2007) Biochem. J. , vol.405 , pp. 251-259
    • Murillo, M.M.1    Carmona-Cuenca, I.2    Del Castillo, G.3    Ortiz, C.4    Roncero, C.5    Sanchez, A.6    Fernandez, M.7    Fabregat, I.8
  • 98
    • 55549098874 scopus 로고    scopus 로고
    • Upregulation of the NADPH oxidase NOX4 by TGF-beta in hepatocytes is required for its pro-apoptotic activity
    • Carmona-Cuenca I., Roncero C., Sancho P., Caja L., Fausto N., Fernandez M., Fabregat I. Upregulation of the NADPH oxidase NOX4 by TGF-beta in hepatocytes is required for its pro-apoptotic activity. J. Hepatol. 2008, 49:965-976.
    • (2008) J. Hepatol. , vol.49 , pp. 965-976
    • Carmona-Cuenca, I.1    Roncero, C.2    Sancho, P.3    Caja, L.4    Fausto, N.5    Fernandez, M.6    Fabregat, I.7
  • 101
    • 84866390484 scopus 로고    scopus 로고
    • Nox4 involvement in TGF-beta and SMAD3-driven induction of the epithelial-to-mesenchymal transition and migration of breast epithelial cells
    • Boudreau H.E., Casterline B.W., Rada B., Korzeniowska A., Leto T.L. Nox4 involvement in TGF-beta and SMAD3-driven induction of the epithelial-to-mesenchymal transition and migration of breast epithelial cells. Free Radic. Biol. Med. 2012, 53:1489-1499.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1489-1499
    • Boudreau, H.E.1    Casterline, B.W.2    Rada, B.3    Korzeniowska, A.4    Leto, T.L.5
  • 103
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • Chen K., Kirber M.T., Xiao H., Yang Y., Keaney J.F. Regulation of ROS signal transduction by NADPH oxidase 4 localization. J. Cell Biol. 2008, 181:1129-1139.
    • (2008) J. Cell Biol. , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 104
    • 65349125859 scopus 로고    scopus 로고
    • Identification of structural elements in Nox1 and Nox4 controlling localization and activity
    • Helmcke I., Heumuller S., Tikkanen R., Schroder K., Brandes R.P. Identification of structural elements in Nox1 and Nox4 controlling localization and activity. Antioxid. Redox Signal. 2009, 11:1279-1287.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1279-1287
    • Helmcke, I.1    Heumuller, S.2    Tikkanen, R.3    Schroder, K.4    Brandes, R.P.5
  • 107
    • 84879587980 scopus 로고    scopus 로고
    • Mitochondrial-localized NADPH oxidase 4 is a source of superoxide in angiotensin II-stimulated neurons
    • Case A.J., Li S., Basu U., Tian J., Zimmerman M.C. Mitochondrial-localized NADPH oxidase 4 is a source of superoxide in angiotensin II-stimulated neurons. Am. J. Physiol. Heart Circ. Physiol. 2013, 305:H19-H28.
    • (2013) Am. J. Physiol. Heart Circ. Physiol. , vol.305 , pp. H19-H28
    • Case, A.J.1    Li, S.2    Basu, U.3    Tian, J.4    Zimmerman, M.C.5
  • 108
    • 70149091965 scopus 로고    scopus 로고
    • Subcellular localization of Nox4 and regulation in diabetes
    • Block K., Gorin Y., Abboud H.E. Subcellular localization of Nox4 and regulation in diabetes. Proc. Natl. Acad. Sci. USA 2009, 106:14385-14390.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14385-14390
    • Block, K.1    Gorin, Y.2    Abboud, H.E.3
  • 109
    • 84863631208 scopus 로고    scopus 로고
    • Angiotensin II-induced mitochondrial Nox4 is a major endogenous source of oxidative stress in kidney tubular cells
    • Kim S.M., Kim Y.G., Jeong K.H., Lee S.H., Lee T.W., Ihm C.G., Moon J.Y. Angiotensin II-induced mitochondrial Nox4 is a major endogenous source of oxidative stress in kidney tubular cells. PloS One 2012, 7:e39739.
    • (2012) PloS One , vol.7 , pp. e39739
    • Kim, S.M.1    Kim, Y.G.2    Jeong, K.H.3    Lee, S.H.4    Lee, T.W.5    Ihm, C.G.6    Moon, J.Y.7
  • 110
    • 84864150374 scopus 로고    scopus 로고
    • Transforming growth factor-beta, bioenergetics, and mitochondria in renal disease
    • Casalena G., Daehn I., Bottinger E. Transforming growth factor-beta, bioenergetics, and mitochondria in renal disease. Semin. Nephrol. 2012, 32:295-303.
    • (2012) Semin. Nephrol. , vol.32 , pp. 295-303
    • Casalena, G.1    Daehn, I.2    Bottinger, E.3
  • 112
    • 84907033145 scopus 로고    scopus 로고
    • C-Jun N terminal kinase modulates NOX-4 derived ROS production and myofibroblasts differentiation in human breast stromal cells
    • Tobar N., Toyos M., Urra C., Mendez N., Arancibia R., Smith P.C., Martinez J. c-Jun N terminal kinase modulates NOX-4 derived ROS production and myofibroblasts differentiation in human breast stromal cells. BMC Cancer 2014, 14:640.
    • (2014) BMC Cancer , vol.14 , pp. 640
    • Tobar, N.1    Toyos, M.2    Urra, C.3    Mendez, N.4    Arancibia, R.5    Smith, P.C.6    Martinez, J.7
  • 113
    • 84903159199 scopus 로고    scopus 로고
    • Nox4 and redox signaling mediate TGF-beta-induced endothelial cell apoptosis and phenotypic switch
    • Yan F., Wang Y., Wu X., Peshavariya H.M., Dusting G.J., Zhang M., Jiang F. Nox4 and redox signaling mediate TGF-beta-induced endothelial cell apoptosis and phenotypic switch. Cell Death Dis. 2014, 5:e1010.
    • (2014) Cell Death Dis. , vol.5 , pp. e1010
    • Yan, F.1    Wang, Y.2    Wu, X.3    Peshavariya, H.M.4    Dusting, G.J.5    Zhang, M.6    Jiang, F.7
  • 114
    • 70350212686 scopus 로고    scopus 로고
    • Overactivation of the MEK/ERK pathway in liver tumor cells confers resistance to TGF-{beta}-induced cell death through impairing up-regulation of the NADPH oxidase NOX4
    • Caja L., Sancho P., Bertran E., Iglesias-Serret D., Gil J., Fabregat I. Overactivation of the MEK/ERK pathway in liver tumor cells confers resistance to TGF-{beta}-induced cell death through impairing up-regulation of the NADPH oxidase NOX4. Cancer Res. 2009, 69:7595-7602.
    • (2009) Cancer Res. , vol.69 , pp. 7595-7602
    • Caja, L.1    Sancho, P.2    Bertran, E.3    Iglesias-Serret, D.4    Gil, J.5    Fabregat, I.6
  • 116
    • 77956036249 scopus 로고    scopus 로고
    • NOX4/NADPH oxidase expression is increased in pulmonary fibroblasts from patients with idiopathic pulmonary fibrosis and mediates TGFbeta1-induced fibroblast differentiation into myofibroblasts
    • Amara N., Goven D., Prost F., Muloway R., Crestani B., Boczkowski J. NOX4/NADPH oxidase expression is increased in pulmonary fibroblasts from patients with idiopathic pulmonary fibrosis and mediates TGFbeta1-induced fibroblast differentiation into myofibroblasts. Thorax 2010, 65:733-738.
    • (2010) Thorax , vol.65 , pp. 733-738
    • Amara, N.1    Goven, D.2    Prost, F.3    Muloway, R.4    Crestani, B.5    Boczkowski, J.6
  • 120
    • 84884507857 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide phosphate oxidase 4 mediates the differential responsiveness of atrial versus ventricular fibroblasts to transforming growth factor-beta
    • Yeh Y.H., Kuo C.T., Chang G.J., Qi X.Y., Nattel S., Chen W.J. Nicotinamide adenine dinucleotide phosphate oxidase 4 mediates the differential responsiveness of atrial versus ventricular fibroblasts to transforming growth factor-beta. Circ. Arrhythm. Electrophysiol. 2013, 6:790-798.
    • (2013) Circ. Arrhythm. Electrophysiol. , vol.6 , pp. 790-798
    • Yeh, Y.H.1    Kuo, C.T.2    Chang, G.J.3    Qi, X.Y.4    Nattel, S.5    Chen, W.J.6
  • 121
    • 53449086013 scopus 로고    scopus 로고
    • Hypoxia activates NADPH oxidase to increase [ROS]i and [Ca2+]i through the mitochondrial ROS-PKCepsilon signaling axis in pulmonary artery smooth muscle cells
    • Rathore R., Zheng Y.M., Niu C.F., Liu Q.H., Korde A., Ho Y.S., Wang Y.X. Hypoxia activates NADPH oxidase to increase [ROS]i and [Ca2+]i through the mitochondrial ROS-PKCepsilon signaling axis in pulmonary artery smooth muscle cells. Free Radic. Biol. Med. 2008, 45:1223-1231.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1223-1231
    • Rathore, R.1    Zheng, Y.M.2    Niu, C.F.3    Liu, Q.H.4    Korde, A.5    Ho, Y.S.6    Wang, Y.X.7
  • 122
    • 65349088460 scopus 로고    scopus 로고
    • Cross-talk between mitochondria and NADPH oxidase: effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells
    • Wosniak J., Santos C.X., Kowaltowski A.J., Laurindo F.R. Cross-talk between mitochondria and NADPH oxidase: effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells. Antioxid. Redox Signal. 2009, 11:1265-1278.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1265-1278
    • Wosniak, J.1    Santos, C.X.2    Kowaltowski, A.J.3    Laurindo, F.R.4
  • 123
    • 77953807521 scopus 로고    scopus 로고
    • Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species
    • Daiber A. Redox signaling (cross-talk) from and to mitochondria involves mitochondrial pores and reactive oxygen species. Biochim. Biophys. Acta 2010, 1797:897-906.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 897-906
    • Daiber, A.1
  • 124
    • 80052266526 scopus 로고    scopus 로고
    • Cross talk between mitochondria and NADPH oxidases
    • Dikalov S. Cross talk between mitochondria and NADPH oxidases. Free Radic. Biol. Med. 2011, 51:1289-1301.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1289-1301
    • Dikalov, S.1
  • 129
    • 0026048230 scopus 로고
    • Deficiency of alveolar fluid glutathione in patients with sepsis and the adult respiratory distress syndrome
    • Pacht E.R., Timerman A.P., Lykens M.G., Merola A.J. Deficiency of alveolar fluid glutathione in patients with sepsis and the adult respiratory distress syndrome. Chest 1991, 100:1397-1403.
    • (1991) Chest , vol.100 , pp. 1397-1403
    • Pacht, E.R.1    Timerman, A.P.2    Lykens, M.G.3    Merola, A.J.4
  • 130
    • 0027331598 scopus 로고
    • Oxidized glutathione is increased in the alveolar fluid of patients with the adult respiratory distress syndrome
    • Bunnell E., Pacht E.R. Oxidized glutathione is increased in the alveolar fluid of patients with the adult respiratory distress syndrome. Am. Rev. Respir. Dis. 1993, 148:1174-1178.
    • (1993) Am. Rev. Respir. Dis. , vol.148 , pp. 1174-1178
    • Bunnell, E.1    Pacht, E.R.2
  • 131
    • 0030028401 scopus 로고    scopus 로고
    • Oxidant-antioxidant balance in granulocytes during ARDS. Effect of N-acetylcysteine
    • Laurent T., Markert M., Feihl F., Schaller M.D., Perret C. Oxidant-antioxidant balance in granulocytes during ARDS. Effect of N-acetylcysteine. Chest 1996, 109:163-166.
    • (1996) Chest , vol.109 , pp. 163-166
    • Laurent, T.1    Markert, M.2    Feihl, F.3    Schaller, M.D.4    Perret, C.5
  • 132
    • 0030807230 scopus 로고    scopus 로고
    • A trial of antioxidants N-acetylcysteine and procysteine in ARDS. The Antioxidant in ARDS Study Group
    • Bernard G.R., Wheeler A.P., Arons M.M., Morris P.E., Paz H.L., Russell J.A., Wright P.E. A trial of antioxidants N-acetylcysteine and procysteine in ARDS. The Antioxidant in ARDS Study Group. Chest 1997, 112:164-172.
    • (1997) Chest , vol.112 , pp. 164-172
    • Bernard, G.R.1    Wheeler, A.P.2    Arons, M.M.3    Morris, P.E.4    Paz, H.L.5    Russell, J.A.6    Wright, P.E.7
  • 133
    • 36348948474 scopus 로고    scopus 로고
    • Improvement by N-acetylcysteine of acute respiratory distress syndrome through increasing intracellular glutathione, and extracellular thiol molecules and anti-oxidant power: evidence for underlying toxicological mechanisms
    • Soltan-Sharifi M.S., Mojtahedzadeh M., Najafi A., Reza Khajavi M., Reza Rouini M., Moradi M., Mohammadirad A., Abdollahi M. Improvement by N-acetylcysteine of acute respiratory distress syndrome through increasing intracellular glutathione, and extracellular thiol molecules and anti-oxidant power: evidence for underlying toxicological mechanisms. Hum. Exp. Toxicol. 2007, 26:697-703.
    • (2007) Hum. Exp. Toxicol. , vol.26 , pp. 697-703
    • Soltan-Sharifi, M.S.1    Mojtahedzadeh, M.2    Najafi, A.3    Reza Khajavi, M.4    Reza Rouini, M.5    Moradi, M.6    Mohammadirad, A.7    Abdollahi, M.8
  • 135
    • 0028230612 scopus 로고
    • The effect of oral N-acetylcysteine on lung glutathione levels in idiopathic pulmonary fibrosis
    • Meyer A., Buhl R., Magnussen H. The effect of oral N-acetylcysteine on lung glutathione levels in idiopathic pulmonary fibrosis. Eur. Respir. J. 1994, 7:431-436.
    • (1994) Eur. Respir. J. , vol.7 , pp. 431-436
    • Meyer, A.1    Buhl, R.2    Magnussen, H.3
  • 136
    • 0031449645 scopus 로고    scopus 로고
    • Antioxidative and clinical effects of high-dose N-acetylcysteine in fibrosing alveolitis. Adjunctive therapy to maintenance immunosuppression
    • Behr J., Maier K., Degenkolb B., Krombach F., Vogelmeier C. Antioxidative and clinical effects of high-dose N-acetylcysteine in fibrosing alveolitis. Adjunctive therapy to maintenance immunosuppression. Am. J. Respir. Crit. Care Med. 1997, 156:1897-1901.
    • (1997) Am. J. Respir. Crit. Care Med. , vol.156 , pp. 1897-1901
    • Behr, J.1    Maier, K.2    Degenkolb, B.3    Krombach, F.4    Vogelmeier, C.5
  • 137
    • 0036014536 scopus 로고    scopus 로고
    • Intracellular glutathione and bronchoalveolar cells in fibrosing alveolitis: effects of N-acetylcysteine
    • Behr J., Degenkolb B., Krombach F., Vogelmeier C. Intracellular glutathione and bronchoalveolar cells in fibrosing alveolitis: effects of N-acetylcysteine. Eur. Respir. J. 2002, 19:906-911.
    • (2002) Eur. Respir. J. , vol.19 , pp. 906-911
    • Behr, J.1    Degenkolb, B.2    Krombach, F.3    Vogelmeier, C.4
  • 139
    • 0035991339 scopus 로고    scopus 로고
    • Glutathione deficiency of the lower respiratory tract in patients with idiopathic pulmonary fibrosis
    • Beeh K.M., Beier J., Haas I.C., Kornmann O., Micke P., Buhl R. Glutathione deficiency of the lower respiratory tract in patients with idiopathic pulmonary fibrosis. Eur. Respir. J. 2002, 19:1119-1123.
    • (2002) Eur. Respir. J. , vol.19 , pp. 1119-1123
    • Beeh, K.M.1    Beier, J.2    Haas, I.C.3    Kornmann, O.4    Micke, P.5    Buhl, R.6
  • 141
    • 59349092007 scopus 로고    scopus 로고
    • Antioxidant status associated with inflammation in sarcoidosis: a potential role for antioxidants
    • Boots A.W., Drent M., Swennen E.L.R., Moonen H.J.J., Bast A., Haenen G.R.M.M. Antioxidant status associated with inflammation in sarcoidosis: a potential role for antioxidants. Respir. Med. 2009, 103:364-372.
    • (2009) Respir. Med. , vol.103 , pp. 364-372
    • Boots, A.W.1    Drent, M.2    Swennen, E.L.R.3    Moonen, H.J.J.4    Bast, A.5    Haenen, G.R.M.M.6
  • 144
    • 0037218573 scopus 로고    scopus 로고
    • Oxidative stress in viral and alcoholic hepatitis
    • Loguercio C., Federico A. Oxidative stress in viral and alcoholic hepatitis. Free Radic. Biol. Med. 2003, 34:1-10.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1-10
    • Loguercio, C.1    Federico, A.2
  • 145
    • 33645236156 scopus 로고    scopus 로고
    • Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma
    • Czeczot H., Scibior D., Skrzycki M., Podsiad M. Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma. Acta Biochim. Pol. 2006, 53:237-242.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 237-242
    • Czeczot, H.1    Scibior, D.2    Skrzycki, M.3    Podsiad, M.4
  • 146
    • 20844458616 scopus 로고    scopus 로고
    • Antioxidant levels in peripheral blood, disease activity and fibrotic stage in chronic hepatitis C
    • Priyanka Bandara J.G., Geoffrey Mc.Caughan, Daya Naidoo, Ora Lux, Chris Salonikas, Kench James, Byth Karen, Geoffrey C.Farrell Antioxidant levels in peripheral blood, disease activity and fibrotic stage in chronic hepatitis C. Liver Int. 2005, 25:518-526.
    • (2005) Liver Int. , vol.25 , pp. 518-526
    • Priyanka Bandara, J.G.1    Geoffrey, M.2    Daya, N.3    Ora, L.4    Chris, S.5    Kench, J.6    Byth, K.7    Geoffrey, C.F.8
  • 147
    • 34247229057 scopus 로고    scopus 로고
    • Oxidative-inflammatory damage in cirrhosis: effect of vitamin E and a fermented papaya preparation
    • Marotta F., Yoshida C., Barreto R., Naito Y., Packer L. Oxidative-inflammatory damage in cirrhosis: effect of vitamin E and a fermented papaya preparation. J. Gastroenterol. Hepatol. 2007, 22:697-703.
    • (2007) J. Gastroenterol. Hepatol. , vol.22 , pp. 697-703
    • Marotta, F.1    Yoshida, C.2    Barreto, R.3    Naito, Y.4    Packer, L.5
  • 148
    • 37549026458 scopus 로고    scopus 로고
    • Serum levels of bcl-2 and cellular oxidative stress in patients with viral hepatitis
    • Osman H., Gabr O., Lotfy S., Gabr S. Serum levels of bcl-2 and cellular oxidative stress in patients with viral hepatitis. Indian J. Med. Microbiol. 2007, 25:323-329.
    • (2007) Indian J. Med. Microbiol. , vol.25 , pp. 323-329
    • Osman, H.1    Gabr, O.2    Lotfy, S.3    Gabr, S.4
  • 149
    • 0033603522 scopus 로고    scopus 로고
    • Use of tetrandrine to differentiate between mechanisms involved in silica-versus bleomycin-induced fibrosis
    • Ma J.Y., Barger M.W., Hubbs A.F., Castranova V., Weber S.L., Ma J.K. Use of tetrandrine to differentiate between mechanisms involved in silica-versus bleomycin-induced fibrosis. J. Toxicol. Environ. Healh A 1999, 57:247-266.
    • (1999) J. Toxicol. Environ. Healh A , vol.57 , pp. 247-266
    • Ma, J.Y.1    Barger, M.W.2    Hubbs, A.F.3    Castranova, V.4    Weber, S.L.5    Ma, J.K.6
  • 150
    • 0035733450 scopus 로고    scopus 로고
    • Captopril inhibits the pulmonary toxicity of paraquat in rats
    • Candan F., Alagozlu H. Captopril inhibits the pulmonary toxicity of paraquat in rats. Hum. Exp. Toxicol. 2001, 20:637-641.
    • (2001) Hum. Exp. Toxicol. , vol.20 , pp. 637-641
    • Candan, F.1    Alagozlu, H.2
  • 151
    • 0036164087 scopus 로고    scopus 로고
    • The effect of melatonin on bleomycin-induced pulmonary fibrosis in rats
    • Arslan S.O., Zerin M., Vural H., Coskun A. The effect of melatonin on bleomycin-induced pulmonary fibrosis in rats. J. Pineal Res. 2002, 32:21-25.
    • (2002) J. Pineal Res. , vol.32 , pp. 21-25
    • Arslan, S.O.1    Zerin, M.2    Vural, H.3    Coskun, A.4
  • 152
    • 24744448896 scopus 로고    scopus 로고
    • S-adenosylmethionine blocks collagen I production by preventing transforming growth factor-{beta} induction of the COL1A2 promoter
    • Nieto N., Cederbaum A.I. S-adenosylmethionine blocks collagen I production by preventing transforming growth factor-{beta} induction of the COL1A2 promoter. J. Biol. Chem. 2005, 280:30963-30974.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30963-30974
    • Nieto, N.1    Cederbaum, A.I.2
  • 154
    • 1542719757 scopus 로고    scopus 로고
    • Attenuation of bleomycin induced pulmonary fibrosis in mice using the heme oxygenase inhibitor Zn-deuteroporphyrin IX-2,4-bisethylene glycol
    • Atzori L., Chua F., Dunsmore S.E., Willis D., Barbarisi M., McAnulty R.J., Laurent G.J. Attenuation of bleomycin induced pulmonary fibrosis in mice using the heme oxygenase inhibitor Zn-deuteroporphyrin IX-2,4-bisethylene glycol. Thorax 2004, 59:217-223.
    • (2004) Thorax , vol.59 , pp. 217-223
    • Atzori, L.1    Chua, F.2    Dunsmore, S.E.3    Willis, D.4    Barbarisi, M.5    McAnulty, R.J.6    Laurent, G.J.7
  • 157
    • 38449100797 scopus 로고    scopus 로고
    • Protective effect of alpha-tocopherol on oxidative stress in experimental pulmonary fibrosis in rats
    • Deger Yeter, Yur F., Ertekin Ali, Mert Nihat, Dede Semiha, Mert Handan Protective effect of alpha-tocopherol on oxidative stress in experimental pulmonary fibrosis in rats. Cell Biochem. Funct. 2007, 25:633-637.
    • (2007) Cell Biochem. Funct. , vol.25 , pp. 633-637
    • Deger, Y.1    Yur, F.2    Ertekin, A.3    Mert, N.4    Dede, S.5    Mert, H.6
  • 159
    • 0026841119 scopus 로고
    • Reduction of glutathione is associated with growth restriction and enlargement of bovine pulmonary artery endothelial cells produced by transforming growth factor-beta 1
    • White A.C., Das S.K., Fanburg B.L. Reduction of glutathione is associated with growth restriction and enlargement of bovine pulmonary artery endothelial cells produced by transforming growth factor-beta 1. Am. J. Respir. Cell Mol. Biol. 1992, 6:364-368.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 364-368
    • White, A.C.1    Das, S.K.2    Fanburg, B.L.3
  • 160
    • 0029872210 scopus 로고    scopus 로고
    • Apoptosis induced by transforming growth factor-beta in fetal hepatocyte primary cultures: involvement of reactive oxygen intermediates
    • Sanchez A., Alvarez A.M., Benito M., Fabregat I. Apoptosis induced by transforming growth factor-beta in fetal hepatocyte primary cultures: involvement of reactive oxygen intermediates. J. Biol. Chem. 1996, 271:7416-7422.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7416-7422
    • Sanchez, A.1    Alvarez, A.M.2    Benito, M.3    Fabregat, I.4
  • 161
    • 0030817668 scopus 로고    scopus 로고
    • Cycloheximide prevents apoptosis, reactive oxygen species production, and glutathione depletion induced by transforming growth factor beta in fetal rat hepatocytes in primary culture
    • Sanchez A., Alvarez A.M., Benito M., Fabregat I. Cycloheximide prevents apoptosis, reactive oxygen species production, and glutathione depletion induced by transforming growth factor beta in fetal rat hepatocytes in primary culture. Hepatology 1997, 26:935-943.
    • (1997) Hepatology , vol.26 , pp. 935-943
    • Sanchez, A.1    Alvarez, A.M.2    Benito, M.3    Fabregat, I.4
  • 162
    • 0031280268 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: transcriptional effect on the GSH rate-limiting enzyme gamma-glutamylcysteine synthetase
    • Arsalane K., Dubois C.M., Muanza T., Begin R., Boudreau F., Asselin C., Cantin A.M. Transforming growth factor-beta1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: transcriptional effect on the GSH rate-limiting enzyme gamma-glutamylcysteine synthetase. Am. J. Respir. Cell Mol. Biol. 1997, 17:599-607.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 599-607
    • Arsalane, K.1    Dubois, C.M.2    Muanza, T.3    Begin, R.4    Boudreau, F.5    Asselin, C.6    Cantin, A.M.7
  • 164
    • 0037077204 scopus 로고    scopus 로고
    • Molecular mechanism of transforming growth factor (TGF)-beta1-induced glutathione depletion in alveolar epithelial cells. Involvement of AP-1/ARE and Fra-1
    • Jardine H., MacNee W., Donaldson K., Rahman I. Molecular mechanism of transforming growth factor (TGF)-beta1-induced glutathione depletion in alveolar epithelial cells. Involvement of AP-1/ARE and Fra-1. J. Biol. Chem. 2002, 277:21158-21166.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21158-21166
    • Jardine, H.1    MacNee, W.2    Donaldson, K.3    Rahman, I.4
  • 165
    • 0041703021 scopus 로고    scopus 로고
    • TGFbeta1-induced suppression of glutathione antioxidant defenses in hepatocytes: caspase-dependent post-translational and caspase-independent transcriptional regulatory mechanisms
    • Franklin C.C., Rosenfeld-Franklin M.E., White C., Kavanagh T.J., Fausto N. TGFbeta1-induced suppression of glutathione antioxidant defenses in hepatocytes: caspase-dependent post-translational and caspase-independent transcriptional regulatory mechanisms. FASEB J. 2003, 17:1535-1537.
    • (2003) FASEB J. , vol.17 , pp. 1535-1537
    • Franklin, C.C.1    Rosenfeld-Franklin, M.E.2    White, C.3    Kavanagh, T.J.4    Fausto, N.5
  • 166
    • 0347318117 scopus 로고    scopus 로고
    • Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes
    • Herrera B., Murillo M.M., Alvarez-Barrientos A., Beltran J., Fernandez M., Fabregat I. Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes. Free Radic. Biol. Med. 2004, 36:16-26.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 16-26
    • Herrera, B.1    Murillo, M.M.2    Alvarez-Barrientos, A.3    Beltran, J.4    Fernandez, M.5    Fabregat, I.6
  • 168
    • 0347357969 scopus 로고    scopus 로고
    • Glutathione regulates transforming growth factor-{beta}-stimulated collagen production in fibroblasts
    • Liu R.-M., Liu Y., Forman H.J., Olman M., Tarpey M.M. Glutathione regulates transforming growth factor-{beta}-stimulated collagen production in fibroblasts. Am. J. Physiol. Lung Cell. Mol. Physiol. 2004, 286:L121-L128.
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.286 , pp. L121-L128
    • Liu, R.-M.1    Liu, Y.2    Forman, H.J.3    Olman, M.4    Tarpey, M.M.5
  • 170
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 2001, 30:1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 171
    • 52049098968 scopus 로고    scopus 로고
    • The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii
    • Dayer R., Fischer B.B., Eggen R.I., Lemaire S.D. The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii. Genetics 2008, 179:41-57.
    • (2008) Genetics , vol.179 , pp. 41-57
    • Dayer, R.1    Fischer, B.B.2    Eggen, R.I.3    Lemaire, S.D.4
  • 172
    • 0028222546 scopus 로고
    • Suppression of antioxidative enzyme expression by transforming growth factor-beta 1 in rat hepatocytes
    • Kayanoki Y., Fujii J., Suzuki K., Kawata S., Matsuzawa Y., Taniguchi N. Suppression of antioxidative enzyme expression by transforming growth factor-beta 1 in rat hepatocytes. J. Biol. Chem. 1994, 269:15488-15492.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15488-15492
    • Kayanoki, Y.1    Fujii, J.2    Suzuki, K.3    Kawata, S.4    Matsuzawa, Y.5    Taniguchi, N.6
  • 173
    • 0030614518 scopus 로고    scopus 로고
    • TGF-beta1 triggers oxidative modifications and enhances apoptosis in HIT cells through accumulation of reactive oxygen species by suppression of catalase and glutathione peroxidase
    • Islam K.N., Kayanoki Y., Kaneto H., Suzuki K., Asahi M., Fujii J., Taniguchi N. TGF-beta1 triggers oxidative modifications and enhances apoptosis in HIT cells through accumulation of reactive oxygen species by suppression of catalase and glutathione peroxidase. Free Radic. Biol. Med. 1997, 22:1007-1017.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 1007-1017
    • Islam, K.N.1    Kayanoki, Y.2    Kaneto, H.3    Suzuki, K.4    Asahi, M.5    Fujii, J.6    Taniguchi, N.7
  • 174
    • 3843142866 scopus 로고    scopus 로고
    • Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo
    • Peltoniemi M., Kaarteenaho-Wiik R., Saily M., Sormunen R., Paakko P., Holmgren A., Soini Y., Kinnula V.L. Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo. Hum. Pathol. 2004, 35:1000-1007.
    • (2004) Hum. Pathol. , vol.35 , pp. 1000-1007
    • Peltoniemi, M.1    Kaarteenaho-Wiik, R.2    Saily, M.3    Sormunen, R.4    Paakko, P.5    Holmgren, A.6    Soini, Y.7    Kinnula, V.L.8
  • 177
    • 0032540880 scopus 로고    scopus 로고
    • Identification and characterization of a new latent transforming growth factor-beta -binding protein, LTBP-4
    • Saharinen J., Taipale J., Monni O., Keski-Oja J. Identification and characterization of a new latent transforming growth factor-beta -binding protein, LTBP-4. J. Biol. Chem. 1998, 273:18459-18469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18459-18469
    • Saharinen, J.1    Taipale, J.2    Monni, O.3    Keski-Oja, J.4
  • 179
    • 0027305971 scopus 로고
    • Thrombospondin causes activation of latent transforming growth factor-beta secreted by endothelial cells by a novel mechanism
    • Schultz-Cherry S., Murphy-Ullrich J.E. Thrombospondin causes activation of latent transforming growth factor-beta secreted by endothelial cells by a novel mechanism. J. Cell Biol. 1993, 122:923-932.
    • (1993) J. Cell Biol. , vol.122 , pp. 923-932
    • Schultz-Cherry, S.1    Murphy-Ullrich, J.E.2
  • 180
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology
    • Murphy-Ullrich J.E., Poczatek M. Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine Growth Factor Rev. 2000, 11:59-69.
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 183
    • 0023916551 scopus 로고
    • Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium
    • Lyons R.M., Keski-Oja J., Moses H.L. Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium. J. Cell Biol. 1988, 106:1659-1665.
    • (1988) J. Cell Biol. , vol.106 , pp. 1659-1665
    • Lyons, R.M.1    Keski-Oja, J.2    Moses, H.L.3
  • 184
    • 0028956737 scopus 로고
    • Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J., Lohi J., Saarinen J., Kovanen P.T., Keski-Oja J. Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J. Biol. Chem. 1995, 270:4689-4696.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3    Kovanen, P.T.4    Keski-Oja, J.5
  • 185
    • 0026447801 scopus 로고
    • Release of transforming growth factor-beta 1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin
    • Taipale J., Koli K., Keski-Oja J. Release of transforming growth factor-beta 1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin. J. Biol. Chem. 1992, 267:25378-25384.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25378-25384
    • Taipale, J.1    Koli, K.2    Keski-Oja, J.3
  • 186
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q., Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000, 14:163-176.
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 187
    • 0029736871 scopus 로고    scopus 로고
    • Redox-mediated activation of latent transforming growth factor-beta 1
    • Barcellos-Hoff M., Dix T. Redox-mediated activation of latent transforming growth factor-beta 1. Mol. Endocrinol. 1996, 10:1077-1083.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1077-1083
    • Barcellos-Hoff, M.1    Dix, T.2
  • 189
    • 25444443392 scopus 로고    scopus 로고
    • Activation of TGF-{beta}1/p38/Smad3 signaling in stromal cells requires ROS-mediated MMP-2 activity during bone marrow damage
    • Wang L., Clutter S., Benincosa J., Fortney J., Gibson L.F. Activation of TGF-{beta}1/p38/Smad3 signaling in stromal cells requires ROS-mediated MMP-2 activity during bone marrow damage. Stem Cells 2005, 23:1122-1134.
    • (2005) Stem Cells , vol.23 , pp. 1122-1134
    • Wang, L.1    Clutter, S.2    Benincosa, J.3    Fortney, J.4    Gibson, L.F.5
  • 190
    • 36549005035 scopus 로고    scopus 로고
    • Endogenous TGF-beta activation by reactive oxygen species is key to Foxp3 induction in TCR-stimulated and HIV-1-infected human CD4+CD25- T cells
    • Amarnath S., Dong L., Li J., Wu Y., Chen W. Endogenous TGF-beta activation by reactive oxygen species is key to Foxp3 induction in TCR-stimulated and HIV-1-infected human CD4+CD25- T cells. Retrovirology 2007, 4:57.
    • (2007) Retrovirology , vol.4 , pp. 57
    • Amarnath, S.1    Dong, L.2    Li, J.3    Wu, Y.4    Chen, W.5
  • 191
    • 37549027570 scopus 로고    scopus 로고
    • Transforming growth factor-beta activation in the lung: focus on fibrosis and reactive oxygen species
    • Koli K., Myllarniemi M., Keski-Oja J., Kinnula V.L. Transforming growth factor-beta activation in the lung: focus on fibrosis and reactive oxygen species. Antioxid. Redox Signal. 2008, 10:333-342.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 333-342
    • Koli, K.1    Myllarniemi, M.2    Keski-Oja, J.3    Kinnula, V.L.4
  • 192
    • 45849148542 scopus 로고    scopus 로고
    • The latent form of TGFbeta(1) is induced by TNFalpha through an ERK specific pathway and is activated by asbestos-derived reactive oxygen species in vitro and in vivo
    • Sullivan D.E., Ferris M., Pociask D., Brody A.R. The latent form of TGFbeta(1) is induced by TNFalpha through an ERK specific pathway and is activated by asbestos-derived reactive oxygen species in vitro and in vivo. J. Immunotoxicol. 2008, 5:145-149.
    • (2008) J. Immunotoxicol. , vol.5 , pp. 145-149
    • Sullivan, D.E.1    Ferris, M.2    Pociask, D.3    Brody, A.R.4
  • 195
    • 53149102406 scopus 로고    scopus 로고
    • Oxidative stress mediates cardiac fibrosis by enhancing transforming growth factor-beta1 in hypertensive rats
    • Zhao W., Zhao T., Chen Y., Ahokas R.A., Sun Y. Oxidative stress mediates cardiac fibrosis by enhancing transforming growth factor-beta1 in hypertensive rats. Mol. Cell. Biochem. 2008, 317:43-50.
    • (2008) Mol. Cell. Biochem. , vol.317 , pp. 43-50
    • Zhao, W.1    Zhao, T.2    Chen, Y.3    Ahokas, R.A.4    Sun, Y.5
  • 196
    • 49549102011 scopus 로고    scopus 로고
    • Increased accumulation of neutrophils and decreased fibrosis in the lung of NADPH oxidase-deficient C57BL/6 mice exposed to carbon nanotubes
    • Shvedova A.A., Kisin E.R., Murray A.R., Kommineni C., Castranova V., Fadeel B., Kagan V.E. Increased accumulation of neutrophils and decreased fibrosis in the lung of NADPH oxidase-deficient C57BL/6 mice exposed to carbon nanotubes. Toxicol. Appl. Pharmacol. 2008, 231:235-240.
    • (2008) Toxicol. Appl. Pharmacol. , vol.231 , pp. 235-240
    • Shvedova, A.A.1    Kisin, E.R.2    Murray, A.R.3    Kommineni, C.4    Castranova, V.5    Fadeel, B.6    Kagan, V.E.7
  • 197
    • 77952722154 scopus 로고    scopus 로고
    • Hepatitis C virus regulates transforming growth factor beta1 production through the generation of reactive oxygen species in a nuclear factor kappaB-dependent manner
    • 2518. e1
    • Lin W., Tsai W.L., Shao R.X., Wu G., Peng L.F., Barlow L.L., Chung W.J., Zhang L., Zhao H., Jang J.Y., Chung R.T. Hepatitis C virus regulates transforming growth factor beta1 production through the generation of reactive oxygen species in a nuclear factor kappaB-dependent manner. Gastroenterology 2010, 138:2509-2518. 2518. e1.
    • (2010) Gastroenterology , vol.138 , pp. 2509-2518
    • Lin, W.1    Tsai, W.L.2    Shao, R.X.3    Wu, G.4    Peng, L.F.5    Barlow, L.L.6    Chung, W.J.7    Zhang, L.8    Zhao, H.9    Jang, J.Y.10    Chung, R.T.11
  • 201
    • 0033163392 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates increase transforming growth factor-beta1 release from human epithelial alveolar cells through two different mechanisms
    • Bellocq A., Azoulay E., Marullo S., Flahault A., Fouqueray B., Philippe C., Cadranel J., Baud L. Reactive oxygen and nitrogen intermediates increase transforming growth factor-beta1 release from human epithelial alveolar cells through two different mechanisms. Am. J. Respir. Cell Mol. Biol. 1999, 21:128-136.
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.21 , pp. 128-136
    • Bellocq, A.1    Azoulay, E.2    Marullo, S.3    Flahault, A.4    Fouqueray, B.5    Philippe, C.6    Cadranel, J.7    Baud, L.8
  • 202
    • 84864223696 scopus 로고    scopus 로고
    • Nox4 mediates hypoxia-stimulated myofibroblast differentiation in nasal polyp-derived fibroblasts
    • Moon Y.M., Kang H.J., Cho J.S., Park I.H., Lee H.M. Nox4 mediates hypoxia-stimulated myofibroblast differentiation in nasal polyp-derived fibroblasts. Int. Arch. Allergy Immunol. 2012, 159:399-409.
    • (2012) Int. Arch. Allergy Immunol. , vol.159 , pp. 399-409
    • Moon, Y.M.1    Kang, H.J.2    Cho, J.S.3    Park, I.H.4    Lee, H.M.5
  • 206
    • 25444512363 scopus 로고    scopus 로고
    • Altered expression of membrane-bound and soluble CD95/Fas contributes to the resistance of fibrotic lung fibroblasts to FasL induced apoptosis
    • Buhling F., Wille A., Rocken C., Wiesner O., Baier A., Meinecke I., Welte T., Pap T. Altered expression of membrane-bound and soluble CD95/Fas contributes to the resistance of fibrotic lung fibroblasts to FasL induced apoptosis. Respir. Res 2005, 6:37.
    • (2005) Respir. Res , vol.6 , pp. 37
    • Buhling, F.1    Wille, A.2    Rocken, C.3    Wiesner, O.4    Baier, A.5    Meinecke, I.6    Welte, T.7    Pap, T.8
  • 207
    • 84913530827 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor 1, fibroblast apoptosis resistance, and aging-related susceptibility to lung fibrosis
    • Huang W.T., Akhter H., Jiang C., MacEwen M., Ding Q., Antony V., Thannickal V.J., Liu R.M. Plasminogen activator inhibitor 1, fibroblast apoptosis resistance, and aging-related susceptibility to lung fibrosis. Exp. Gerontol. 2015, 61:62-75.
    • (2015) Exp. Gerontol. , vol.61 , pp. 62-75
    • Huang, W.T.1    Akhter, H.2    Jiang, C.3    MacEwen, M.4    Ding, Q.5    Antony, V.6    Thannickal, V.J.7    Liu, R.M.8
  • 208
    • 0035141395 scopus 로고    scopus 로고
    • Evidence of type II pneumocyte apoptosis in the pathogenesis of idiopathic pulmonary fibrosis (IFP)/usual interstitial pneumonia (UIP)
    • Barbas-Filho J.V., Ferreira M.A., Sesso A., Kairalla R.A., Carvalho C.R., Capelozzi V.L. Evidence of type II pneumocyte apoptosis in the pathogenesis of idiopathic pulmonary fibrosis (IFP)/usual interstitial pneumonia (UIP). J. Clin. Pathol. 2001, 54:132-138.
    • (2001) J. Clin. Pathol. , vol.54 , pp. 132-138
    • Barbas-Filho, J.V.1    Ferreira, M.A.2    Sesso, A.3    Kairalla, R.A.4    Carvalho, C.R.5    Capelozzi, V.L.6
  • 209
    • 13844314302 scopus 로고    scopus 로고
    • Expression of apoptotic and antiapoptotic markers in epithelial cells in idiopathic pulmonary fibrosis
    • Plataki M., Koutsopoulos A.V., Darivianaki K., Delides G., Siafakas N.M., Bouros D. Expression of apoptotic and antiapoptotic markers in epithelial cells in idiopathic pulmonary fibrosis. Chest 2005, 127:266-274.
    • (2005) Chest , vol.127 , pp. 266-274
    • Plataki, M.1    Koutsopoulos, A.V.2    Darivianaki, K.3    Delides, G.4    Siafakas, N.M.5    Bouros, D.6
  • 211
    • 1842583833 scopus 로고    scopus 로고
    • Comparison of the morphological and biochemical changes in normal human lung fibroblasts and fibroblasts derived from lungs of patients with idiopathic pulmonary fibrosis during FasL-induced apoptosis
    • Moodley Y.P., Caterina P., Scaffidi A.K., Misso N.L., Papadimitriou J.M., McAnulty R.J., Laurent G.J., Thompson P.J., Knight D.A. Comparison of the morphological and biochemical changes in normal human lung fibroblasts and fibroblasts derived from lungs of patients with idiopathic pulmonary fibrosis during FasL-induced apoptosis. J. Pathol. 2004, 202:486-495.
    • (2004) J. Pathol. , vol.202 , pp. 486-495
    • Moodley, Y.P.1    Caterina, P.2    Scaffidi, A.K.3    Misso, N.L.4    Papadimitriou, J.M.5    McAnulty, R.J.6    Laurent, G.J.7    Thompson, P.J.8    Knight, D.A.9
  • 212
    • 0030638505 scopus 로고    scopus 로고
    • Apoptosis and expression of Fas/Fas ligand mRNA in bleomycin-induced pulmonary fibrosis in mice
    • Hagimoto N., Kuwano K., Nomoto Y., Kunitake R., Hara N. Apoptosis and expression of Fas/Fas ligand mRNA in bleomycin-induced pulmonary fibrosis in mice. Am. J. Respir. Cell. Mol. Biol. 1997, 16:91-101.
    • (1997) Am. J. Respir. Cell. Mol. Biol. , vol.16 , pp. 91-101
    • Hagimoto, N.1    Kuwano, K.2    Nomoto, Y.3    Kunitake, R.4    Hara, N.5
  • 216
    • 25144460253 scopus 로고    scopus 로고
    • Cyclosporine A-induced renal fibrosis: a role for epithelial-mesenchymal transition
    • Slattery C., Campbell E., McMorrow T., Ryan M.P. Cyclosporine A-induced renal fibrosis: a role for epithelial-mesenchymal transition. Am. J. Pathol. 2005, 167:395-407.
    • (2005) Am. J. Pathol. , vol.167 , pp. 395-407
    • Slattery, C.1    Campbell, E.2    McMorrow, T.3    Ryan, M.P.4
  • 220
    • 34347364932 scopus 로고    scopus 로고
    • Detection of epithelial to mesenchymal transition in airways of a bleomycin induced pulmonary fibrosis model derived from an alpha-smooth muscle actin-Cre transgenic mouse
    • Wu Z., Yang L., Cai L., Zhang M., Cheng X., Yang X., Xu J. Detection of epithelial to mesenchymal transition in airways of a bleomycin induced pulmonary fibrosis model derived from an alpha-smooth muscle actin-Cre transgenic mouse. Respir. Res 2007, 8:1.
    • (2007) Respir. Res , vol.8 , pp. 1
    • Wu, Z.1    Yang, L.2    Cai, L.3    Zhang, M.4    Cheng, X.5    Yang, X.6    Xu, J.7
  • 221
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • Thiery J.P., Acloque H., Huang R.Y., Nieto M.A. Epithelial-mesenchymal transitions in development and disease. Cell 2009, 139:871-890.
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 222
    • 79951805332 scopus 로고    scopus 로고
    • Epithelial-mesenchymal interactions in pulmonary fibrosis
    • Chapman H.A. Epithelial-mesenchymal interactions in pulmonary fibrosis. Annu. Rev. Physiol. 2011, 73:413-435.
    • (2011) Annu. Rev. Physiol. , vol.73 , pp. 413-435
    • Chapman, H.A.1
  • 224
    • 77953769774 scopus 로고    scopus 로고
    • Identification of epithelial to mesenchymal transition as a novel source of fibroblasts in intestinal fibrosis
    • Flier S.N., Tanjore H., Kokkotou E.G., Sugimoto H., Zeisberg M., Kalluri R. Identification of epithelial to mesenchymal transition as a novel source of fibroblasts in intestinal fibrosis. J. Biol. Chem. 2010, 285:20202-20212.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20202-20212
    • Flier, S.N.1    Tanjore, H.2    Kokkotou, E.G.3    Sugimoto, H.4    Zeisberg, M.5    Kalluri, R.6
  • 227
    • 34347228684 scopus 로고    scopus 로고
    • Endothelin-1 induces alveolar epithelial-mesenchymal transition through endothelin type A receptor-mediated production of TGF-beta1
    • Jain R., Shaul P.W., Borok Z., Willis B.C. Endothelin-1 induces alveolar epithelial-mesenchymal transition through endothelin type A receptor-mediated production of TGF-beta1. Am. J. Respir. Cell Mol. Biol. 2007, 37:38-47.
    • (2007) Am. J. Respir. Cell Mol. Biol. , vol.37 , pp. 38-47
    • Jain, R.1    Shaul, P.W.2    Borok, Z.3    Willis, B.C.4
  • 228
    • 20544437490 scopus 로고    scopus 로고
    • Role of reactive oxygen species in TGF-beta1-induced mitogen-activated protein kinase activation and epithelial-mesenchymal transition in renal tubular epithelial cells
    • Rhyu D.Y., Yang Y., Ha H., Lee G.T., Song J.S., Uh S.T., Lee H.B. Role of reactive oxygen species in TGF-beta1-induced mitogen-activated protein kinase activation and epithelial-mesenchymal transition in renal tubular epithelial cells. J. Am. Soc. Nephrol. 2005, 16:667-675.
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 667-675
    • Rhyu, D.Y.1    Yang, Y.2    Ha, H.3    Lee, G.T.4    Song, J.S.5    Uh, S.T.6    Lee, H.B.7
  • 229
    • 72949098078 scopus 로고    scopus 로고
    • Decreased expression of glutaredoxin 1 is required for transforming growth factor-beta1-mediated epithelial-mesenchymal transition of EpRas mammary epithelial cells
    • Lee E.K., Jeon W.K., Chae M.Y., Hong H.Y., Lee Y.S., Kim J.H., Kwon J.Y., Kim B.C., Park S.H. Decreased expression of glutaredoxin 1 is required for transforming growth factor-beta1-mediated epithelial-mesenchymal transition of EpRas mammary epithelial cells. Biochem. Biophys. Res. Commun. 2010, 391:1021-1027.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1021-1027
    • Lee, E.K.1    Jeon, W.K.2    Chae, M.Y.3    Hong, H.Y.4    Lee, Y.S.5    Kim, J.H.6    Kwon, J.Y.7    Kim, B.C.8    Park, S.H.9
  • 230
    • 84883169793 scopus 로고    scopus 로고
    • MiR-30a negatively regulates TGF-beta1-induced epithelial-mesenchymal transition and peritoneal fibrosis by targeting Snai1
    • Zhou Q., Yang M., Lan H., Yu X. miR-30a negatively regulates TGF-beta1-induced epithelial-mesenchymal transition and peritoneal fibrosis by targeting Snai1. Am. J. Pathol. 2013, 183:808-819.
    • (2013) Am. J. Pathol. , vol.183 , pp. 808-819
    • Zhou, Q.1    Yang, M.2    Lan, H.3    Yu, X.4
  • 231
    • 84907520196 scopus 로고    scopus 로고
    • Signaling pathway cooperation in TGF-beta-induced epithelial-mesenchymal transition
    • Derynck R., Muthusamy B.P., Saeteurn K.Y. Signaling pathway cooperation in TGF-beta-induced epithelial-mesenchymal transition. Curr. Opin. Cell Biol. 2014, 31:56-66.
    • (2014) Curr. Opin. Cell Biol. , vol.31 , pp. 56-66
    • Derynck, R.1    Muthusamy, B.P.2    Saeteurn, K.Y.3
  • 232
    • 84894593599 scopus 로고    scopus 로고
    • Molecular mechanisms of epithelial-mesenchymal transition
    • Lamouille S., Xu J., Derynck R. Molecular mechanisms of epithelial-mesenchymal transition. Nat. Rev. Mol. Cell. Biol. 2014, 15:178-196.
    • (2014) Nat. Rev. Mol. Cell. Biol. , vol.15 , pp. 178-196
    • Lamouille, S.1    Xu, J.2    Derynck, R.3
  • 233
    • 84891351058 scopus 로고    scopus 로고
    • Nox4-derived R.O.S. Signaling contributes to TGF-beta-induced epithelial-mesenchymal transition in pancreatic cancer cells
    • Hiraga R., Kato M., Miyagawa S., Kamata T., Nox4-derived R.O.S. signaling contributes to TGF-beta-induced epithelial-mesenchymal transition in pancreatic cancer cells. Anticancer Res. 2013, 33:4431-4438.
    • (2013) Anticancer Res. , vol.33 , pp. 4431-4438
    • Hiraga, R.1    Kato, M.2    Miyagawa, S.3    Kamata, T.4
  • 236
    • 84877928942 scopus 로고    scopus 로고
    • AMP-activated protein kinase inhibits TGF-beta-, angiotensin II-, aldosterone-, high glucose-, and albumin-induced epithelial-mesenchymal transition
    • Lee J.H., Kim J.H., Kim J.S., Chang J.W., Kim S.B., Park J.S., Lee S.K. AMP-activated protein kinase inhibits TGF-beta-, angiotensin II-, aldosterone-, high glucose-, and albumin-induced epithelial-mesenchymal transition. Am. J. Physiol. Ren. Physiol. 2013, 304:F686-F697.
    • (2013) Am. J. Physiol. Ren. Physiol. , vol.304 , pp. F686-F697
    • Lee, J.H.1    Kim, J.H.2    Kim, J.S.3    Chang, J.W.4    Kim, S.B.5    Park, J.S.6    Lee, S.K.7
  • 237
    • 85027931724 scopus 로고    scopus 로고
    • NADPH oxidase-dependent formation of reactive oxygen species contributes to transforming growth factor beta1-induced epithelial-mesenchymal transition in rat peritoneal mesothelial cells, and the role of astragalus intervention
    • Liu X.X., Zhou H.J., Cai L., Zhang W., Ma J.L., Tao X.J., Yu J.N. NADPH oxidase-dependent formation of reactive oxygen species contributes to transforming growth factor beta1-induced epithelial-mesenchymal transition in rat peritoneal mesothelial cells, and the role of astragalus intervention. Chin. J. Integr. Med. 2014, 20:667-674.
    • (2014) Chin. J. Integr. Med. , vol.20 , pp. 667-674
    • Liu, X.X.1    Zhou, H.J.2    Cai, L.3    Zhang, W.4    Ma, J.L.5    Tao, X.J.6    Yu, J.N.7
  • 238
    • 0031777597 scopus 로고    scopus 로고
    • Expression of plasminogen activator inhibitors type-1 and type-2 in the mouse lung after administration of crystalline silica
    • Lardot C., Heusterpreute M., Mertens P., Philippe M., Lison D. Expression of plasminogen activator inhibitors type-1 and type-2 in the mouse lung after administration of crystalline silica. Eur. Respir. J. 1998, 11:912-921.
    • (1998) Eur. Respir. J. , vol.11 , pp. 912-921
    • Lardot, C.1    Heusterpreute, M.2    Mertens, P.3    Philippe, M.4    Lison, D.5
  • 241
    • 0028929665 scopus 로고
    • Increased procoagulant and antifibrinolytic activities in the lungs with idiopathic pulmonary fibrosis
    • Kotani I., Sato A., Hayakawa H., Urano T., Takada Y., Takada A. Increased procoagulant and antifibrinolytic activities in the lungs with idiopathic pulmonary fibrosis. Thromb. Res. 1995, 77:493-504.
    • (1995) Thromb. Res. , vol.77 , pp. 493-504
    • Kotani, I.1    Sato, A.2    Hayakawa, H.3    Urano, T.4    Takada, Y.5    Takada, A.6
  • 243
    • 77950896262 scopus 로고    scopus 로고
    • SPARC suppresses apoptosis of idiopathic pulmonary fibrosis fibroblasts through constitutive activation of beta-catenin
    • Chang W., Wei K., Jacobs S.S., Upadhyay D., Weill D., Rosen G.D. SPARC suppresses apoptosis of idiopathic pulmonary fibrosis fibroblasts through constitutive activation of beta-catenin. J. Biol. Chem. 2010, 285:8196-8206.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8196-8206
    • Chang, W.1    Wei, K.2    Jacobs, S.S.3    Upadhyay, D.4    Weill, D.5    Rosen, G.D.6
  • 244
    • 0029118192 scopus 로고
    • Changes in procoagulant and fibrinolytic gene expression during bleomycin-induced lung injury in the mouse
    • Olman M.A., Mackman N., Gladson C.L., Moser K.M., Loskutoff D.J. Changes in procoagulant and fibrinolytic gene expression during bleomycin-induced lung injury in the mouse. J. Clin. Investig. 1995, 96:1621-1630.
    • (1995) J. Clin. Investig. , vol.96 , pp. 1621-1630
    • Olman, M.A.1    Mackman, N.2    Gladson, C.L.3    Moser, K.M.4    Loskutoff, D.J.5
  • 245
    • 37549070801 scopus 로고    scopus 로고
    • Changes of coagulation and fibrinolysis systen in bronchoalveolar lavage fluid in lung fibrosis
    • Zhang Y., Ma J. Changes of coagulation and fibrinolysis systen in bronchoalveolar lavage fluid in lung fibrosis. Beijing Da Xue Xue Bao 2005, 37:516-519.
    • (2005) Beijing Da Xue Xue Bao , vol.37 , pp. 516-519
    • Zhang, Y.1    Ma, J.2
  • 246
    • 0030054203 scopus 로고    scopus 로고
    • Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhibitor-1 gene
    • Eitzman D.T., McCoy R.D., Zheng X., Fay W.P., Shen T., Ginsburg D., Simon R.H. Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhibitor-1 gene. J. Clin. Investig. 1996, 97:232-237.
    • (1996) J. Clin. Investig. , vol.97 , pp. 232-237
    • Eitzman, D.T.1    McCoy, R.D.2    Zheng, X.3    Fay, W.P.4    Shen, T.5    Ginsburg, D.6    Simon, R.H.7
  • 249
    • 20144375510 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type-1 gene expression and induced migration in TGF-beta1-stimulated smooth muscle cells is pp60(c-src)/MEK-dependent
    • Samarakoon R., Higgins C.E., Higgins S.P., Kutz S.M., Higgins P.J. Plasminogen activator inhibitor type-1 gene expression and induced migration in TGF-beta1-stimulated smooth muscle cells is pp60(c-src)/MEK-dependent. J. Cell. Physiol. 2005, 204:236-246.
    • (2005) J. Cell. Physiol. , vol.204 , pp. 236-246
    • Samarakoon, R.1    Higgins, C.E.2    Higgins, S.P.3    Kutz, S.M.4    Higgins, P.J.5
  • 251
    • 33947229059 scopus 로고    scopus 로고
    • Regulation of TGF-[beta]1/MAPK-mediated PAI-1 gene expression by the actin cytoskeleton in human mesangial cells
    • Yang C., Patel K., Harding P., Sorokin A., Glass W.F. Regulation of TGF-[beta]1/MAPK-mediated PAI-1 gene expression by the actin cytoskeleton in human mesangial cells. Exp. Cell Res. 2007, 313:1240-1250.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1240-1250
    • Yang, C.1    Patel, K.2    Harding, P.3    Sorokin, A.4    Glass, W.F.5
  • 252
    • 0035960347 scopus 로고    scopus 로고
    • Protease-activated receptor 1 and plasminogen activator inhibitor 1 expression in chronic allograft nephropathy: the role of coagulation and fibrinolysis in renal graft fibrosis
    • Grandaliano G., Di Paolo S., Monno R., Stallone G., Ranieri E., Pontrelli P., Gesualdo L., Schena F.P. Protease-activated receptor 1 and plasminogen activator inhibitor 1 expression in chronic allograft nephropathy: the role of coagulation and fibrinolysis in renal graft fibrosis. Transplantation 2001, 72:1437-1443.
    • (2001) Transplantation , vol.72 , pp. 1437-1443
    • Grandaliano, G.1    Di Paolo, S.2    Monno, R.3    Stallone, G.4    Ranieri, E.5    Pontrelli, P.6    Gesualdo, L.7    Schena, F.P.8
  • 254
    • 37549068860 scopus 로고    scopus 로고
    • Oxidative stress, plasminogen activator inhibitor 1, and lung fibrosis
    • Liu R.M. Oxidative stress, plasminogen activator inhibitor 1, and lung fibrosis. Antioxid. Redox Signal. 2008, 10:303-319.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 303-319
    • Liu, R.M.1
  • 256
  • 257
    • 79960882925 scopus 로고    scopus 로고
    • Redox-induced Src kinase and caveolin-1 signaling in TGF-beta1-initiated SMAD2/3 activation and PAI-1 expression
    • Samarakoon R., Chitnis S.S., Higgins S.P., Higgins C.E., Krepinsky J.C., Higgins P.J. Redox-induced Src kinase and caveolin-1 signaling in TGF-beta1-initiated SMAD2/3 activation and PAI-1 expression. PloS One 2011, 6:e22896.
    • (2011) PloS One , vol.6 , pp. e22896
    • Samarakoon, R.1    Chitnis, S.S.2    Higgins, S.P.3    Higgins, C.E.4    Krepinsky, J.C.5    Higgins, P.J.6
  • 259
    • 80053635010 scopus 로고    scopus 로고
    • Modulators of induction of plasminogen activator inhibitor type-1 in HepG2 cells by transforming growth factor-beta
    • Nakayama N., Nakamura T., Okada H., Iwaki S., Sobel B.E., Fujii S. Modulators of induction of plasminogen activator inhibitor type-1 in HepG2 cells by transforming growth factor-beta. Coron. Artery Dis. 2011, 22:468-478.
    • (2011) Coron. Artery Dis. , vol.22 , pp. 468-478
    • Nakayama, N.1    Nakamura, T.2    Okada, H.3    Iwaki, S.4    Sobel, B.E.5    Fujii, S.6
  • 260
    • 0042388115 scopus 로고    scopus 로고
    • A mutant, noninhibitory plasminogen activator inhibitor type 1 decreases matrix accumulation in experimental glomerulonephritis
    • Huang Y., Haraguchi M., Lawrence D.A., Border W.A., Yu L., Noble N.A. A mutant, noninhibitory plasminogen activator inhibitor type 1 decreases matrix accumulation in experimental glomerulonephritis. J. Clin. Investig. 2003, 112:379-388.
    • (2003) J. Clin. Investig. , vol.112 , pp. 379-388
    • Huang, Y.1    Haraguchi, M.2    Lawrence, D.A.3    Border, W.A.4    Yu, L.5    Noble, N.A.6
  • 261
    • 70349644472 scopus 로고    scopus 로고
    • Mechanisms underlying the antifibrotic properties of noninhibitory PAI-1 (PAI-1R) in experimental nephritis
    • Huang Y., Border W.A., Lawrence D.A., Noble N.A. Mechanisms underlying the antifibrotic properties of noninhibitory PAI-1 (PAI-1R) in experimental nephritis. Am. J. Physiol. Ren. Physiol. 2009, 297:F1045-F1054.
    • (2009) Am. J. Physiol. Ren. Physiol. , vol.297 , pp. F1045-F1054
    • Huang, Y.1    Border, W.A.2    Lawrence, D.A.3    Noble, N.A.4
  • 262
    • 33746539889 scopus 로고    scopus 로고
    • Noninhibitory PAI-1 enhances plasmin-mediated matrix degradation both in vitro and in experimental nephritis
    • Huang Y., Border W.A., Lawrence D.A., Noble N.A. Noninhibitory PAI-1 enhances plasmin-mediated matrix degradation both in vitro and in experimental nephritis. Kidney Int. 2006, 70:515-522.
    • (2006) Kidney Int. , vol.70 , pp. 515-522
    • Huang, Y.1    Border, W.A.2    Lawrence, D.A.3    Noble, N.A.4
  • 263
    • 84859516083 scopus 로고    scopus 로고
    • Role of reactive oxygen species in transforming growth factor-beta1-induced extracellular matrix accumulation in renal tubular epithelial cells
    • Rhyu D.Y., Park J., Sharma B.R., Ha H. Role of reactive oxygen species in transforming growth factor-beta1-induced extracellular matrix accumulation in renal tubular epithelial cells. Transplant. Proc. 2012, 44:625-628.
    • (2012) Transplant. Proc. , vol.44 , pp. 625-628
    • Rhyu, D.Y.1    Park, J.2    Sharma, B.R.3    Ha, H.4
  • 264
    • 40849139148 scopus 로고    scopus 로고
    • TGF-beta1-induced plasminogen activator inhibitor-1 expression in vascular smooth muscle cells requires pp60(c-src)/EGFR(Y845) and Rho/ROCK signaling
    • Samarakoon R., Higgins S.P., Higgins C.E., Higgins P.J. TGF-beta1-induced plasminogen activator inhibitor-1 expression in vascular smooth muscle cells requires pp60(c-src)/EGFR(Y845) and Rho/ROCK signaling. J. Mol. Cell. Cardiol. 2008, 44:527-538.
    • (2008) J. Mol. Cell. Cardiol. , vol.44 , pp. 527-538
    • Samarakoon, R.1    Higgins, S.P.2    Higgins, C.E.3    Higgins, P.J.4


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