메뉴 건너뛰기




Volumn 90, Issue , 2016, Pages 85-90

A reaction-diffusion model of cytosolic hydrogen peroxide

Author keywords

Cytosol; Hydrogen peroxide; Membrane gradient; Pseudo steady state; Reaction diffusion model; Redox signaling

Indexed keywords

HYDROGEN PEROXIDE;

EID: 84947983166     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.11.005     Document Type: Article
Times cited : (51)

References (39)
  • 1
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • J.R. Stone, and S. Yang Hydrogen peroxide: a signaling messenger Antioxid. Redox Signal. 8 2006 243 270 10.1089/ars.2006.8.243
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 2
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • R.H. Burdon Superoxide and hydrogen peroxide in relation to mammalian cell proliferation Free Radic. Biol. Med. 18 1995 775 794 10.1016/0891-5849(94)00198-S
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 3
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • M.L. Circu, and T.Y. Aw Reactive oxygen species, cellular redox systems, and apoptosis Free Radic. Biol. Med. 48 2010 749 762 10.1016/j.freeradbiomed.2009.12.022
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 4
    • 33847660853 scopus 로고    scopus 로고
    • 2 in studies of signal transduction
    • 2 in studies of signal transduction Free Radic. Biol. Med. 42 2007 926 932 10.1016/j.freeradbiomed.2007.01.011
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 5
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • N.J. Adimora, D.P. Jones, and M.L. Kemp A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses Antioxid. Redox Signal. 13 2010 731 743 10.1089/ars.2009.2968
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 6
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • B.C. Dickinson, and C.J. Chang Chemistry and biology of reactive oxygen species in signaling or stress responses Nat. Chem. Biol. 7 2011 504 511 10.1038/nchembio.607
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 7
    • 84880105471 scopus 로고    scopus 로고
    • Cysteine-mediated redox signaling: Chemistry, biology, and tools for discovery
    • C.E. Paulsen, and K.S. Carroll Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Chem. Rev. 113 2013 4633 4679 10.1021/cr300163e
    • (2013) Chem. Rev. , vol.113 , pp. 4633-4679
    • Paulsen, C.E.1    Carroll, K.S.2
  • 8
    • 79958238542 scopus 로고    scopus 로고
    • Hydrogen peroxide as a signaling molecule
    • E. Veal, and A. Day Hydrogen peroxide as a signaling molecule Antioxid. Redox Signal. 15 2011 147 151 10.1089/ars.2011.3968
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 147-151
    • Veal, E.1    Day, A.2
  • 9
    • 84941657986 scopus 로고    scopus 로고
    • Analysis of the lifetime and spatial localization of hydrogen peroxide generated in the cytosol using a reduced kinetic model
    • J.B. Lim, B.K. Huang, W.M. Deen, and H.D. Sikes Analysis of the lifetime and spatial localization of hydrogen peroxide generated in the cytosol using a reduced kinetic model Free Radic. Biol. Med. 89 2015 47 53 10.1016/j.freeradbiomed.2015.07.009
    • (2015) Free Radic. Biol. Med. , vol.89 , pp. 47-53
    • Lim, J.B.1    Huang, B.K.2    Deen, W.M.3    Sikes, H.D.4
  • 12
    • 84879760966 scopus 로고    scopus 로고
    • H2O2 delivery to cells: Steady-state versus bolus addition
    • H.S. Marinho, L. Cyrne, E. Cadenas, and F. Antunes H2O2 delivery to cells: steady-state versus bolus addition Methods Enzym. 526 2013 159 173 10.1016/B978-0-12-405883-5.00010-7
    • (2013) Methods Enzym. , vol.526 , pp. 159-173
    • Marinho, H.S.1    Cyrne, L.2    Cadenas, E.3    Antunes, F.4
  • 13
    • 84925357881 scopus 로고    scopus 로고
    • Functional manipulation of dendritic cells by photoswitchable generation of intracellular reactive oxygen species
    • T.-C. Cheong, E.P. Shin, E.-K. Kwon, J.-H. Choi, K.-K. Wang, P. Sharma, and et al. Functional manipulation of dendritic cells by photoswitchable generation of intracellular reactive oxygen species ACS Chem. Biol. 2014 10.1021/cb5009124
    • (2014) ACS Chem. Biol.
    • Cheong, T.-C.1    Shin, E.P.2    Kwon, E.-K.3    Choi, J.-H.4    Wang, K.-K.5    Sharma, P.6
  • 14
    • 74949106146 scopus 로고    scopus 로고
    • The GOX/CAT system: A novel enzymatic method to independently control hydrogen peroxide and hypoxia in cell culture
    • S. Mueller, G. Millonig, and G.N. Waite The GOX/CAT system: a novel enzymatic method to independently control hydrogen peroxide and hypoxia in cell culture Adv. Med. Sci. 54 2009 121 135 10.2478/v10039-009-0042-3
    • (2009) Adv. Med. Sci. , vol.54 , pp. 121-135
    • Mueller, S.1    Millonig, G.2    Waite, G.N.3
  • 15
    • 84894073943 scopus 로고    scopus 로고
    • How Much H2O2 Is Produced by recombinant d-amino acid oxidase in mammalian cells?
    • M.E. Matlashov, V.V. Belousov, E. Grigori, and How Much H2O2 Is Produced by recombinant d-amino acid oxidase in mammalian cells? Antioxid. Redox Signal. 20 2014 1039 1044 10.1089/ars.2013.5618
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 1039-1044
    • Matlashov, M.E.1    Belousov, V.V.2    Grigori, E.3
  • 16
    • 78049233238 scopus 로고    scopus 로고
    • Controlled enzymatic production of astrocytic hydrogen peroxide protects neurons from oxidative stress via an Nrf2-independent pathway
    • R.E. Haskew-Layton, J.B. Payappilly, N.A. Smirnova, T.C. Ma, K.K. Chan, T.H. Murphy, and et al. Controlled enzymatic production of astrocytic hydrogen peroxide protects neurons from oxidative stress via an Nrf2-independent pathway Proc. Natl. Acad. Sci. USA 107 2010 17385 17390 10.1073/pnas.1003996107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17385-17390
    • Haskew-Layton, R.E.1    Payappilly, J.B.2    Smirnova, N.A.3    Ma, T.C.4    Chan, K.K.5    Murphy, T.H.6
  • 17
    • 48749131250 scopus 로고    scopus 로고
    • Transfection of the DAAO gene and subsequent induction of cytotoxic oxidative stress by d-alanine in 9L cells
    • J. Li, Y. Shen, A. Liu, X. Wang, and C. Zhao Transfection of the DAAO gene and subsequent induction of cytotoxic oxidative stress by d-alanine in 9L cells Oncol. Rep. 20 2008 341 346 10.3892/or-00000012
    • (2008) Oncol. Rep. , vol.20 , pp. 341-346
    • Li, J.1    Shen, Y.2    Liu, A.3    Wang, X.4    Zhao, C.5
  • 19
    • 84925443050 scopus 로고    scopus 로고
    • Spatial, temporal, and quantitative manipulation of intracellular hydrogen peroxide in cultured cells
    • I. Alim, R.E. Haskew-Layton, H. Aleyasin, H. Guo, and R.R. Ratan Spatial, temporal, and quantitative manipulation of intracellular hydrogen peroxide in cultured cells Methods Enzym. 547 2014 251 273 10.1016/B978-0-12-801415-8.00014-X
    • (2014) Methods Enzym. , vol.547 , pp. 251-273
    • Alim, I.1    Haskew-Layton, R.E.2    Aleyasin, H.3    Guo, H.4    Ratan, R.R.5
  • 20
    • 84886787647 scopus 로고    scopus 로고
    • Two-photon fluorescence imaging of intracellular hydrogen peroxide with chemoselective fluorescent probes
    • H. Guo, H. Aleyasin, S.S. Howard, B.C. Dickinson, V.S. Lin, R.E. Haskew-Layton, and et al. Two-photon fluorescence imaging of intracellular hydrogen peroxide with chemoselective fluorescent probes J. Biomed. Opt. 18 2013 106002 10.1117/1.JBO.18.10.106002
    • (2013) J. Biomed. Opt. , vol.18 , pp. 106002
    • Guo, H.1    Aleyasin, H.2    Howard, S.S.3    Dickinson, B.C.4    Lin, V.S.5    Haskew-Layton, R.E.6
  • 21
    • 78650116633 scopus 로고    scopus 로고
    • Light-activated regulation of cofilin dynamics using a photocaged hydrogen peroxide generator
    • E.W. Miller, N. Taulet, C.S. Onak, E.J. New, J.K. Lanselle, G.S. Smelick, and et al. Light-activated regulation of cofilin dynamics using a photocaged hydrogen peroxide generator J. Am. Chem. Soc. 132 2010 17071 17073 10.1021/ja107783j
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 17071-17073
    • Miller, E.W.1    Taulet, N.2    Onak, C.S.3    New, E.J.4    Lanselle, J.K.5    Smelick, G.S.6
  • 22
    • 0031871607 scopus 로고    scopus 로고
    • Diffusion and reaction of nitric oxide in suspension cell cultures
    • B. Chen, M. Keshive, and W.M. Deen Diffusion and reaction of nitric oxide in suspension cell cultures Biophys. J. 75 1998 745 754 10.1016/S0006-3495(98)77564-2
    • (1998) Biophys. J. , vol.75 , pp. 745-754
    • Chen, B.1    Keshive, M.2    Deen, W.M.3
  • 23
    • 0041461886 scopus 로고    scopus 로고
    • Analysis of cellular exposure to peroxynitrite in suspension cultures
    • N. Nalwaya, and W.M. Deen Analysis of cellular exposure to peroxynitrite in suspension cultures Chem. Res. Toxicol. 16 2003 920 932 10.1021/tx025664w
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 920-932
    • Nalwaya, N.1    Deen, W.M.2
  • 24
    • 77951245162 scopus 로고    scopus 로고
    • Nitric oxide, oxygen, and superoxide formation and consumption in macrophages and colonic epithelial cells
    • M.P. Chin, D.B. Schauer, and W.M. Deen Nitric oxide, oxygen, and superoxide formation and consumption in macrophages and colonic epithelial cells Chem. Res. Toxicol. 23 2010 778 787 10.1021/tx900415k
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 778-787
    • Chin, M.P.1    Schauer, D.B.2    Deen, W.M.3
  • 25
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • L.C. Seaver, and J.A. Imlay Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli J. Bacteriol. 183 2001 7182 7189 10.1128/JB.183.24.7182-7189.2001
    • (2001) J. Bacteriol. , vol.183 , pp. 7182-7189
    • Seaver, L.C.1    Imlay, J.A.2
  • 26
    • 40449112970 scopus 로고    scopus 로고
    • Intracellular water-specific MR of microbead-adherent cells: The HeLa cell intracellular water exchange lifetime
    • L. Zhao, C.D. Kroenke, J. Song, D. Piwnica-Worms, J.J.H. Ackerman, and J.J. Neil Intracellular water-specific MR of microbead-adherent cells: the HeLa cell intracellular water exchange lifetime NMR Biomed. 21 2008 159 164 10.1002/nbm.1173
    • (2008) NMR Biomed. , vol.21 , pp. 159-164
    • Zhao, L.1    Kroenke, C.D.2    Song, J.3    Piwnica-Worms, D.4    Ackerman, J.J.H.5    Neil, J.J.6
  • 27
    • 84908664771 scopus 로고    scopus 로고
    • Quantifying intracellular hydrogen peroxide perturbations in terms of concentration
    • B.K. Huang, and H.D. Sikes Quantifying intracellular hydrogen peroxide perturbations in terms of concentration Redox Biol. 2C 2014 955 962 10.1016/j.redox.2014.08.001
    • (2014) Redox Biol. , vol.2 C , pp. 955-962
    • Huang, B.K.1    Sikes, H.D.2
  • 28
    • 0027533592 scopus 로고
    • Diffusion coefficients of oxygen, hydrogen peroxide and glucose in a hydrogel
    • S.A.M. van Stroe-Biezen, F.M. Everaerts, L.J.J. Janssen, and R.A. Tacken Diffusion coefficients of oxygen, hydrogen peroxide and glucose in a hydrogel Anal. Chim. Acta 273 1993 553 560 10.1016/0003-2670(93)80202-V
    • (1993) Anal. Chim. Acta , vol.273 , pp. 553-560
    • Van Stroe-Biezen, S.A.M.1    Everaerts, F.M.2    Janssen, L.J.J.3    Tacken, R.A.4
  • 29
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • D.P. Jones Radical-free biology of oxidative stress Am. J. Physiol. Cell. Physiol. 295 2008 C849 C868 10.1152/ajpcell.00283.2008
    • (2008) Am. J. Physiol. Cell. Physiol. , vol.295 , pp. C849-C868
    • Jones, D.P.1
  • 31
    • 84878874865 scopus 로고    scopus 로고
    • An assay for the rate of removal of extracellular hydrogen peroxide by cells
    • B.A. Wagner, J.R. Witmer, T.J. van't Erve, and G.R. Buettner An assay for the rate of removal of extracellular hydrogen peroxide by cells Redox Biol. 1 2013 210 217 10.1016/j.redox.2013.01.011
    • (2013) Redox Biol. , vol.1 , pp. 210-217
    • Wagner, B.A.1    Witmer, J.R.2    Van't Erve, T.J.3    Buettner, G.R.4
  • 32
    • 80052157671 scopus 로고    scopus 로고
    • A nuclear-localized fluorescent hydrogen peroxide probe for monitoring sirtuin-mediated oxidative stress responses in vivo
    • B.C. Dickinson, Y. Tang, Z. Chang, and C.J. Chang A nuclear-localized fluorescent hydrogen peroxide probe for monitoring sirtuin-mediated oxidative stress responses in vivo Chem. Biol. 18 2011 943 948 10.1016/j.chembiol.2011.07.005
    • (2011) Chem. Biol. , vol.18 , pp. 943-948
    • Dickinson, B.C.1    Tang, Y.2    Chang, Z.3    Chang, C.J.4
  • 33
    • 77950192252 scopus 로고    scopus 로고
    • Organelle-targetable fluorescent probes for imaging hydrogen peroxide in living cells via SNAP-Tag protein labeling
    • D. Srikun, A.E. Albers, C.I. Nam, A.T. Iavarone, and C.J. Chang Organelle-targetable fluorescent probes for imaging hydrogen peroxide in living cells via SNAP-Tag protein labeling J. Am. Chem. Soc. 132 2010 4455 4465 10.1021/ja100117u
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4455-4465
    • Srikun, D.1    Albers, A.E.2    Nam, C.I.3    Iavarone, A.T.4    Chang, C.J.5
  • 34
    • 79251603273 scopus 로고    scopus 로고
    • Hydrogen peroxide probes directed to different cellular compartments
    • M. Malinouski, Y. Zhou, V.V. Belousov, D.L. Hatfield, and V.N. Gladyshev Hydrogen peroxide probes directed to different cellular compartments PLoS One 6 2011 e14564 10.1371/journal.pone.0014564
    • (2011) PLoS One , vol.6
    • Malinouski, M.1    Zhou, Y.2    Belousov, V.V.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 36
    • 84901842374 scopus 로고    scopus 로고
    • Imaging dynamic redox processes with genetically encoded probes
    • D. Ezerina, B. Morgan, and T.P. Dick Imaging dynamic redox processes with genetically encoded probes J. Mol. Cell. Cardiol. 73 2014 43 49 10.1016/j.yjmcc.2013.12.023
    • (2014) J. Mol. Cell. Cardiol. , vol.73 , pp. 43-49
    • Ezerina, D.1    Morgan, B.2    Dick, T.P.3
  • 37
    • 84928203283 scopus 로고    scopus 로고
    • 2000-fold parallelized dual-color STED fluorescence nanoscopy
    • F. Bergermann, L. Alber, S.J. Sahl, J. Engelhardt, and S.W. Hell 2000-fold parallelized dual-color STED fluorescence nanoscopy Opt. Express 23 2015 2000 211 223 10.1364/OE.23.000211
    • (2000) Opt. Express , vol.23 , Issue.2015 , pp. 211-223
    • Bergermann, F.1    Alber, L.2    Sahl, S.J.3    Engelhardt, J.4    Hell, S.W.5
  • 38
    • 84875451079 scopus 로고    scopus 로고
    • The tumor suppressor Mst1 promotes changes in the cellular redox state by phosphorylation and inactivation of peroxiredoxin-1 protein
    • S.J. Rawat, C.L. Creasy, J.R. Peterson, and J. Chernoff The tumor suppressor Mst1 promotes changes in the cellular redox state by phosphorylation and inactivation of peroxiredoxin-1 protein J. Biol. Chem. 288 2013 8762 8771 10.1074/jbc.M112.414524
    • (2013) J. Biol. Chem. , vol.288 , pp. 8762-8771
    • Rawat, S.J.1    Creasy, C.L.2    Peterson, J.R.3    Chernoff, J.4
  • 39
    • 84904329372 scopus 로고    scopus 로고
    • Hydrogen peroxide metabolism and sensing in human erythrocytes: A validated kinetic model and reappraisal of the role of peroxiredoxin II
    • R. Benfeitas, G. Selvaggio, F. Antunes, P.M.B.M. Coelho, and A. Salvador Hydrogen peroxide metabolism and sensing in human erythrocytes: a validated kinetic model and reappraisal of the role of peroxiredoxin II Free Radic. Biol. Med. 74 2014 35 49 10.1016/j.freeradbiomed.2014.06.007
    • (2014) Free Radic. Biol. Med. , vol.74 , pp. 35-49
    • Benfeitas, R.1    Selvaggio, G.2    Antunes, F.3    Coelho, P.M.B.M.4    Salvador, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.