메뉴 건너뛰기




Volumn 1203, Issue , 2010, Pages 23-28

Regulation of apoptosis through cysteine oxidation: Implications for fibrotic lung disease

Author keywords

apoptosis; Fas; fibrosis; glutaredoxin; lung; S glutathionylation

Indexed keywords

FAS ANTIGEN;

EID: 77956251878     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2010.05553.x     Document Type: Conference Paper
Times cited : (27)

References (40)
  • 1
    • 23644461803 scopus 로고    scopus 로고
    • Oxidative stress in pulmonary fibrosis: A possible role for redox modulatory therapy
    • Kinnula, V.L. et al. 2005. Oxidative stress in pulmonary fibrosis: a possible role for redox modulatory therapy. Am. J. Respir. Crit. Care Med. 172 : 417 422.
    • (2005) Am. J. Respir. Crit. Care Med. , vol.172 , pp. 417-422
    • Kinnula, V.L.1
  • 2
    • 45049085873 scopus 로고    scopus 로고
    • Redox-based regulation of signal transduction: Principles, pitfalls, and promises
    • Janssen-Heininger, Y.M. et al. 2008. Redox-based regulation of signal transduction: principles, pitfalls, and promises. Free Radic. Biol. Med. 45 : 1 17.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1-17
    • Janssen-Heininger, Y.M.1
  • 3
    • 9444249870 scopus 로고    scopus 로고
    • The transcription factor NRF2 protects against pulmonary fibrosis
    • Cho, H.Y. et al. 2004. The transcription factor NRF2 protects against pulmonary fibrosis. FASEB J. 18 : 1258 1260.
    • (2004) FASEB J. , vol.18 , pp. 1258-1260
    • Cho, H.Y.1
  • 4
    • 31644437328 scopus 로고    scopus 로고
    • Increased sensitivity to asbestos-induced lung injury in mice lacking extracellular superoxide dismutase
    • Fattman, C.L. et al. 2006. Increased sensitivity to asbestos-induced lung injury in mice lacking extracellular superoxide dismutase. Free Radic. Biol. Med. 40 : 601 607.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 601-607
    • Fattman, C.L.1
  • 5
    • 0033909952 scopus 로고    scopus 로고
    • Aerosolized administration of N-acetylcysteine attenuates lung fibrosis induced by bleomycin in mice
    • Hagiwara, S.I., Y. Ishii S. Kitamura. 2000. Aerosolized administration of N-acetylcysteine attenuates lung fibrosis induced by bleomycin in mice. Am. J. Respir. Crit. Care Med. 162 : 225 231.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.162 , pp. 225-231
    • Hagiwara, S.I.1    Ishii, Y.2    Kitamura, S.3
  • 6
    • 69949114515 scopus 로고    scopus 로고
    • NADPH oxidase-4 mediates myofibroblast activation and fibrogenic responses to lung injury
    • Hecker, L. et al. 2009. NADPH oxidase-4 mediates myofibroblast activation and fibrogenic responses to lung injury. Nat. Med. 15 : 1077 1081.
    • (2009) Nat. Med. , vol.15 , pp. 1077-1081
    • Hecker, L.1
  • 7
    • 12244286790 scopus 로고    scopus 로고
    • Oxidative stress in lung epithelial cells from patients with idiopathic interstitial pneumonias
    • Kuwano, K. et al. 2003. Oxidative stress in lung epithelial cells from patients with idiopathic interstitial pneumonias. Eur. Respir. J. 21 : 232 240.
    • (2003) Eur. Respir. J. , vol.21 , pp. 232-240
    • Kuwano, K.1
  • 8
    • 28144459814 scopus 로고    scopus 로고
    • High-dose acetylcysteine in idiopathic pulmonary fibrosis
    • Demedts, M. et al. 2005. High-dose acetylcysteine in idiopathic pulmonary fibrosis. N. Engl. J. Med. 353 : 2229 2242.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2229-2242
    • Demedts, M.1
  • 9
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan, M. et al. 1995. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270 : 296 299.
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1
  • 10
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J.D. 2004. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4 : 181 189.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 11
    • 22044446501 scopus 로고    scopus 로고
    • Cellular and molecular targets of protein S-glutathiolation
    • Shackelford, R.E. et al. 2005. Cellular and molecular targets of protein S-glutathiolation. Antioxid. Redox Signal. 7 : 940 950.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 940-950
    • Shackelford, R.E.1
  • 12
    • 0035960648 scopus 로고    scopus 로고
    • Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redox-induced inhibition of DNA binding
    • Pineda-Molina, E. et al. 2001. Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. Biochemistry 40 : 14134 14142.
    • (2001) Biochemistry , vol.40 , pp. 14134-14142
    • Pineda-Molina, E.1
  • 13
    • 0034702868 scopus 로고    scopus 로고
    • Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): A potential mechanism of PKC isozyme regulation
    • Ward, N.E. et al. 2000. Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation. Biochemistry 39 : 10319 10329.
    • (2000) Biochemistry , vol.39 , pp. 10319-10329
    • Ward, N.E.1
  • 14
    • 33748339203 scopus 로고    scopus 로고
    • Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta
    • Reynaert, N.L. et al. 2006. Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta. Proc. Natl. Acad. Sci. USA 103 : 13086 13091.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13086-13091
    • Reynaert, N.L.1
  • 15
    • 9144266981 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi, T. et al. 2004. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat. Med. 10 : 1200 1207.
    • (2004) Nat. Med. , vol.10 , pp. 1200-1207
    • Adachi, T.1
  • 16
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi, T. et al. 2004. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 279 : 29857 29862.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29857-29862
    • Adachi, T.1
  • 17
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton, M.D., P.B. Chock J.J. Mieyal. 2005. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid. Redox Signal. 7 : 348 366.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 18
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes, A.P. A. Holmgren. 2004. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6 : 63 74.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 19
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity
    • Yang, Y. et al. 1998. Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry 37 : 17145 17156.
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1
  • 20
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction
    • Starke, D.W., P.B. Chock J.J. Mieyal. 2003. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction. J. Biol. Chem. 278 : 14607 14613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 21
    • 0035734736 scopus 로고    scopus 로고
    • Oxygen-induced pulmonary injury in gamma-glutamyl transpeptidase- deficient mice
    • Barrios, R. et al. 2001. Oxygen-induced pulmonary injury in gamma-glutamyl transpeptidase-deficient mice. Lung 179 : 319 330.
    • (2001) Lung , vol.179 , pp. 319-330
    • Barrios, R.1
  • 22
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • Ho, Y.S. et al. 2007. Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia. Free Radic. Biol. Med. 43 : 1299 1312.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1299-1312
    • Ho, Y.S.1
  • 23
    • 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. et al. 2004. 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. 35 : 1000 1007.
    • (2004) Hum. Pathol. , vol.35 , pp. 1000-1007
    • Peltoniemi, M.1
  • 24
  • 25
    • 34247536682 scopus 로고    scopus 로고
    • The CD95 receptor: Apoptosis revisited
    • Peter, M.E. et al. 2007. The CD95 receptor: apoptosis revisited. Cell 129 : 447 450.
    • (2007) Cell , vol.129 , pp. 447-450
    • Peter, M.E.1
  • 26
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant, H. 2002. The Fas signaling pathway: more than a paradigm. Science 296 : 1635 1636.
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 27
    • 0032185238 scopus 로고    scopus 로고
    • Expression of Fas (CD95) and FasL (CD95L) in human airway epithelium
    • Hamann, K.J. et al. 1998. Expression of Fas (CD95) and FasL (CD95L) in human airway epithelium. Am. J. Respir. Cell Mol Biol. 19 : 537 542.
    • (1998) Am. J. Respir. Cell Mol Biol. , vol.19 , pp. 537-542
    • Hamann, K.J.1
  • 28
    • 0031230494 scopus 로고    scopus 로고
    • Induction of apoptosis and pulmonary fibrosis in mice in response to ligation of Fas antigen
    • Hagimoto, N. et al. 1997. Induction of apoptosis and pulmonary fibrosis in mice in response to ligation of Fas antigen. Am. J. Respir. Cell Mol Biol. 17 : 272 278.
    • (1997) Am. J. Respir. Cell Mol Biol. , vol.17 , pp. 272-278
    • Hagimoto, N.1
  • 29
    • 0032717522 scopus 로고    scopus 로고
    • Essential roles of the Fas-Fas ligand pathway in the development of pulmonary fibrosis
    • Kuwano, K. et al. 1999. Essential roles of the Fas-Fas ligand pathway in the development of pulmonary fibrosis. J. Clin. Invest. 104 : 13 19.
    • (1999) J. Clin. Invest. , vol.104 , pp. 13-19
    • Kuwano, K.1
  • 30
    • 3543109115 scopus 로고    scopus 로고
    • Early growth response gene 1-mediated apoptosis is essential for transforming growth factor beta1-induced pulmonary fibrosis
    • Lee, C.G. et al. 2004. Early growth response gene 1-mediated apoptosis is essential for transforming growth factor beta1-induced pulmonary fibrosis. J. Exp. Med. 200 : 377 389.
    • (2004) J. Exp. Med. , vol.200 , pp. 377-389
    • Lee, C.G.1
  • 31
    • 14344283933 scopus 로고    scopus 로고
    • Attenuation of bleomycin-induced pneumopathy in mice by a caspase inhibitor
    • Kuwano, K. et al. 2001. Attenuation of bleomycin-induced pneumopathy in mice by a caspase inhibitor. Am. J. Physiol. Lung Cell Mol. Physiol. 280 : L316 L325.
    • (2001) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.280
    • Kuwano, K.1
  • 33
    • 0030215822 scopus 로고    scopus 로고
    • P21Waf1/Cip1/Sdi1 and p53 expression in association with DNA strand breaks in idiopathic pulmonary fibrosis
    • Kuwano, K. et al. 1996. P21Waf1/Cip1/Sdi1 and p53 expression in association with DNA strand breaks in idiopathic pulmonary fibrosis. Am. J. Respir. Crit. Care Med. 154 : 477 483.
    • (1996) Am. J. Respir. Crit. Care Med. , vol.154 , pp. 477-483
    • Kuwano, K.1
  • 35
    • 33847625968 scopus 로고    scopus 로고
    • Epithelial cell apoptosis by fas ligand-positive myofibroblasts in lung fibrosis
    • Golan-Gerstl, R. et al. 2007. Epithelial cell apoptosis by fas ligand-positive myofibroblasts in lung fibrosis. Am. J. Respir. Cell Mol Biol. 36 : 270 275.
    • (2007) Am. J. Respir. Cell Mol Biol. , vol.36 , pp. 270-275
    • Golan-Gerstl, R.1
  • 36
    • 38049100595 scopus 로고    scopus 로고
    • Evasion of myofibroblasts from immune surveillance: A mechanism for tissue fibrosis
    • Wallach-Dayan, S.B., R. Golan-Gerstl R. Breuer. 2007. Evasion of myofibroblasts from immune surveillance: a mechanism for tissue fibrosis. Proc. Natl. Acad. Sci. USA 104 : 20460 20465.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20460-20465
    • Wallach-Dayan, S.B.1    Golan-Gerstl, R.2    Breuer, R.3
  • 37
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar, M. et al. 2008. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320 : 1050 1054.
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1
  • 38
    • 0033597449 scopus 로고    scopus 로고
    • Fas-induced caspase denitrosylation
    • Mannick, J.B. et al. 1999. Fas-induced caspase denitrosylation. Science 284 : 651 654.
    • (1999) Science , vol.284 , pp. 651-654
    • Mannick, J.B.1
  • 39
    • 60849086193 scopus 로고    scopus 로고
    • Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
    • Anathy, V. et al. 2009. Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas. J. Cell Biol. 184 : 241 252.
    • (2009) J. Cell Biol. , vol.184 , pp. 241-252
    • Anathy, V.1
  • 40
    • 33846934941 scopus 로고    scopus 로고
    • A classification scheme for redox-based modifications of proteins
    • Forrester, M.T. J.S. Stamler. 2007. A classification scheme for redox-based modifications of proteins. Am. J. Respir. Cell Mol Biol. 36 : 135 137.
    • (2007) Am. J. Respir. Cell Mol Biol. , vol.36 , pp. 135-137
    • Forrester, M.T.1    Stamler, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.