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Volumn 37, Issue 6, 2012, Pages 1037-1049

Reactive Oxygen Species-Induced Actin Glutathionylation Controls Actin Dynamics in Neutrophils

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; F ACTIN; GLUTAREDOXIN; GLUTAREDOXIN 1; LATRUNCULIN B; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG;

EID: 84870878170     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2012.08.017     Document Type: Article
Times cited : (166)

References (35)
  • 2
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra E.S., Higgs H.N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 2007, 9:1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 3
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
    • Chrestensen C.A., Starke D.W., Mieyal J.J. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J. Biol. Chem. 2000, 275:26556-26565.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 4
    • 77955631174 scopus 로고    scopus 로고
    • Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of IkappaB kinases in mice: impact on histone acetylation
    • Chung S., Sundar I.K., Yao H., Ho Y.S., Rahman I. Glutaredoxin 1 regulates cigarette smoke-mediated lung inflammation through differential modulation of IkappaB kinases in mice: impact on histone acetylation. Am. J. Physiol. Lung Cell. Mol. Physiol. 2010, 299:L192-L203.
    • (2010) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.299
    • Chung, S.1    Sundar, I.K.2    Yao, H.3    Ho, Y.S.4    Rahman, I.5
  • 6
    • 12244311183 scopus 로고    scopus 로고
    • Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule
    • Dalle-Donne I., Giustarini D., Rossi R., Colombo R., Milzani A. Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule. Free Radic. Biol. Med. 2003, 34:23-32.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 23-32
    • Dalle-Donne, I.1    Giustarini, D.2    Rossi, R.3    Colombo, R.4    Milzani, A.5
  • 7
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • Dickinson B.C., Chang C.J. Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat. Chem. Biol. 2011, 7:504-511.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 9
    • 33747270499 scopus 로고    scopus 로고
    • Chronic granulomatous disease and other disorders of phagocyte function
    • Dinauer M.C. Chronic granulomatous disease and other disorders of phagocyte function. Hematology (Am. Soc. Hematol. Educ. Program) 2005, 89-95.
    • (2005) Hematology (Am. Soc. Hematol. Educ. Program) , pp. 89-95
    • Dinauer, M.C.1
  • 10
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly M.M., Mieyal J.J. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 2007, 7:381-391.
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 12
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi P. Regulation of protein function by glutathionylation. Free Radic. Res. 2005, 39:573-580.
    • (2005) Free Radic. Res. , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 13
    • 34547107098 scopus 로고    scopus 로고
    • RNAi screen identifies UBE2D3 as a mediator of all-trans retinoic acid-induced cell growth arrest in human acute promyelocytic NB4 cells
    • Hattori H., Zhang X., Jia Y., Subramanian K.K., Jo H., Loison F., Newburger P.E., Luo H.R. RNAi screen identifies UBE2D3 as a mediator of all-trans retinoic acid-induced cell growth arrest in human acute promyelocytic NB4 cells. Blood 2007, 110:640-650.
    • (2007) Blood , vol.110 , pp. 640-650
    • Hattori, H.1    Zhang, X.2    Jia, Y.3    Subramanian, K.K.4    Jo, H.5    Loison, F.6    Newburger, P.E.7    Luo, H.R.8
  • 15
    • 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., Xiong Y., Ho D.S., Gao J., Chua B.H., Pai H., Mieyal J.J. 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. 2007, 43:1299-1312.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1299-1312
    • Ho, Y.S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.5    Pai, H.6    Mieyal, J.J.7
  • 18
    • 38849100878 scopus 로고    scopus 로고
    • Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary
    • Johansson M., Lundberg M. Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary. BMC Biochem. 2007, 8:26.
    • (2007) BMC Biochem. , vol.8 , pp. 26
    • Johansson, M.1    Lundberg, M.2
  • 19
    • 70249095029 scopus 로고    scopus 로고
    • Focal adhesion kinase regulates pathogen-killing capability and life span of neutrophils via mediating both adhesion-dependent and -independent cellular signals
    • Kasorn A., Alcaide P., Jia Y., Subramanian K.K., Sarraj B., Li Y., Loison F., Hattori H., Silberstein L.E., Luscinskas W.F., Luo H.R. Focal adhesion kinase regulates pathogen-killing capability and life span of neutrophils via mediating both adhesion-dependent and -independent cellular signals. J. Immunol. 2009, 183:1032-1043.
    • (2009) J. Immunol. , vol.183 , pp. 1032-1043
    • Kasorn, A.1    Alcaide, P.2    Jia, Y.3    Subramanian, K.K.4    Sarraj, B.5    Li, Y.6    Loison, F.7    Hattori, H.8    Silberstein, L.E.9    Luscinskas, W.F.10    Luo, H.R.11
  • 22
    • 33745815327 scopus 로고    scopus 로고
    • Global methods to monitor the thiol-disulfide state of proteins in vivo
    • Leichert L.I., Jakob U. Global methods to monitor the thiol-disulfide state of proteins in vivo. Antioxid. Redox Signal. 2006, 8:763-772.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 763-772
    • Leichert, L.I.1    Jakob, U.2
  • 23
    • 53449095486 scopus 로고    scopus 로고
    • Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse
    • Löfgren S., Fernando M.R., Xing K.Y., Wang Y., Kuszynski C.A., Ho Y.S., Lou M.F. Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse. Invest. Ophthalmol. Vis. Sci. 2008, 49:4497-4505.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4497-4505
    • Löfgren, S.1    Fernando, M.R.2    Xing, K.Y.3    Wang, Y.4    Kuszynski, C.A.5    Ho, Y.S.6    Lou, M.F.7
  • 24
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins: unifying elements in redox biology
    • Meyer Y., Buchanan B.B., Vignols F., Reichheld J.P. Thioredoxins and glutaredoxins: unifying elements in redox biology. Annu. Rev. Genet. 2009, 43:335-367.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.P.4
  • 25
    • 77957652745 scopus 로고    scopus 로고
    • Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
    • Miller E.W., Dickinson B.C., Chang C.J. Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc. Natl. Acad. Sci. USA 2010, 107:15681-15686.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15681-15686
    • Miller, E.W.1    Dickinson, B.C.2    Chang, C.J.3
  • 26
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 2003, 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 28
    • 80052026626 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling
    • Prasad A., Jia Y., Chakraborty A., Li Y., Jain S.K., Zhong J., Roy S.G., Loison F., Mondal S., Sakai J., et al. Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling. Nat. Immunol. 2011, 12:752-760.
    • (2011) Nat. Immunol. , vol.12 , pp. 752-760
    • Prasad, A.1    Jia, Y.2    Chakraborty, A.3    Li, Y.4    Jain, S.K.5    Zhong, J.6    Roy, S.G.7    Loison, F.8    Mondal, S.9    Sakai, J.10
  • 29
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin A.T., Neubert H., Brennan J.P., Eaton P. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc. Natl. Acad. Sci. USA 2004, 101:17982-17987.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 30
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton M.D., Chock P.B., Mieyal J.J. Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid. Redox Signal. 2005, 7:348-366.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 31
    • 84870950759 scopus 로고    scopus 로고
    • Non-classical roles of NADPH-oxidase dependent Reactive Oxygen Species in Phagocytes
    • Nova Science Publishers, Inc., New York, R.H.S. Kohlund (Ed.)
    • Subramanian K.K., Luo H.R. Non-classical roles of NADPH-oxidase dependent Reactive Oxygen Species in Phagocytes. Granulocytes: Classification, Toxic Materials Produced and Pathology 2009, 127-154. Nova Science Publishers, Inc., New York. R.H.S. Kohlund (Ed.).
    • (2009) Granulocytes: Classification, Toxic Materials Produced and Pathology , pp. 127-154
    • Subramanian, K.K.1    Luo, H.R.2
  • 32
    • 34247360789 scopus 로고    scopus 로고
    • Tumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions
    • Subramanian K.K., Jia Y., Zhu D., Simms B.T., Jo H., Hattori H., You J., Mizgerd J.P., Luo H.R. Tumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions. Blood 2007, 109:4028-4037.
    • (2007) Blood , vol.109 , pp. 4028-4037
    • Subramanian, K.K.1    Jia, Y.2    Zhu, D.3    Simms, B.T.4    Jo, H.5    Hattori, H.6    You, J.7    Mizgerd, J.P.8    Luo, H.R.9
  • 33
    • 0032586876 scopus 로고    scopus 로고
    • Expression and characterization of Cys374 mutated human beta-actin in two different mammalian cell lines: impaired microfilament organization and stability
    • Tsapara A., Kardassis D., Moustakas A., Gravanis A., Stournaras C. Expression and characterization of Cys374 mutated human beta-actin in two different mammalian cell lines: impaired microfilament organization and stability. FEBS Lett. 1999, 455:117-122.
    • (1999) FEBS Lett. , vol.455 , pp. 117-122
    • Tsapara, A.1    Kardassis, D.2    Moustakas, A.3    Gravanis, A.4    Stournaras, C.5
  • 35
    • 34548507495 scopus 로고    scopus 로고
    • Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications
    • Ying J., Clavreul N., Sethuraman M., Adachi T., Cohen R.A. Thiol oxidation in signaling and response to stress: detection and quantification of physiological and pathophysiological thiol modifications. Free Radic. Biol. Med. 2007, 43:1099-1108.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1099-1108
    • Ying, J.1    Clavreul, N.2    Sethuraman, M.3    Adachi, T.4    Cohen, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.