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Volumn 207, Issue 1, 2010, Pages 129-139

VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CALCIUM IONOPHORE; CHEMOATTRACTANT; GRAMICIDIN; HYDROGEN PEROXIDE; ION CHANNEL; OXIDOREDUCTASE; PROTON; SUPEROXIDE; UNCLASSIFIED DRUG; VOLTAGE SENSING DOMAIN ONLY PROTEIN;

EID: 76149085162     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20091837     Document Type: Article
Times cited : (161)

References (57)
  • 1
    • 36249028250 scopus 로고    scopus 로고
    • Chloride channels activated by swell can regulate the NADPH oxidase generated membrane depolarisation in activated human neutrophils
    • doi:10.1016/ j.bbrc.2007.10.176
    • Ahluwalia, J. 2008. Chloride channels activated by swell can regulate the NADPH oxidase generated membrane depolarisation in activated human neutrophils. Biochem. Biophys. Res. Commun. 365:328-333. doi:10.1016/ j.bbrc.2007.10.176
    • (2008) Biochem. Biophys. Res. Commun , vol.365 , pp. 328-333
    • Ahluwalia, J.1
  • 2
    • 1542318099 scopus 로고    scopus 로고
    • The large-conductance Ca2+-activated K+ channel is essential for innate immunity
    • doi:10.1038/nature02356
    • Ahluwalia, J., A. Tinker, L.H. Clapp, M.R. Duchen, A.Y. Abramov, S. Pope, M. Nobles, and A.W. Segal. 2004. The large-conductance Ca2+-activated K+ channel is essential for innate immunity. Nature. 427:853-858. doi:10.1038/nature02356
    • (2004) Nature , vol.427 , pp. 853-858
    • Ahluwalia, J.1    Tinker, A.2    Clapp, L.H.3    Duchen, M.R.4    Abramov, A.Y.5    Pope, S.6    Nobles, M.7    Segal, A.W.8
  • 3
    • 0037082101 scopus 로고    scopus 로고
    • The neutrophil NADPH oxidase
    • doi:10.1006/abbi.2001.2642
    • Babior, B.M., J.D. Lambeth, and W. Nauseef. 2002. The neutrophil NADPH oxidase. Arch. Biochem. Biophys. 397:342-344. doi:10.1006/abbi.2001.2642
    • (2002) Arch. Biochem. Biophys , vol.397 , pp. 342-344
    • Babior, B.M.1    Lambeth, J.D.2    Nauseef, W.3
  • 4
    • 0039102450 scopus 로고    scopus 로고
    • A novel H+ conductance in eosinophils: Unique characteristics and absence in chronic granulomatous disease
    • doi:10.1084/jem.190.2.183
    • Bánfi, B., J. Schrenzel, O. Nüsse, D.P. Lew, E. Ligeti, K.H. Krause, and N. Demaurex. 1999. A novel H+ conductance in eosinophils: unique characteristics and absence in chronic granulomatous disease. J. Exp. Med. 190:183-194. doi:10.1084/jem.190.2.183
    • (1999) J. Exp. Med , vol.190 , pp. 183-194
    • Bánfi, B.1    Schrenzel, J.2    Nüsse, O.3    Lew, D.P.4    Ligeti, E.5    Krause, K.H.6    Demaurex, N.7
  • 5
    • 0034614701 scopus 로고    scopus 로고
    • A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1
    • doi:10.1126/science.287.5450.138
    • Bánfi, B., A. Maturana, S. Jaconi, S. Arnaudeau, T. Laforge, B. Sinha, E. Ligeti, N. Demaurex, and K.H. Krause. 2000. A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1. Science. 287:138-142. doi:10.1126/science.287.5450.138
    • (2000) Science , vol.287 , pp. 138-142
    • Bánfi, B.1    Maturana, A.2    Jaconi, S.3    Arnaudeau, S.4    Laforge, T.5    Sinha, B.6    Ligeti, E.7    Demaurex, N.8    Krause, K.H.9
  • 6
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey, T.E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 7
    • 0037417274 scopus 로고    scopus 로고
    • The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels
    • doi:10.1038/nature01523
    • DeCoursey, T.E., D. Morgan, and V.V. Cherny. 2003. The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels. Nature. 422:531-534. doi:10.1038/nature01523
    • (2003) Nature , vol.422 , pp. 531-534
    • DeCoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 8
    • 33744497376 scopus 로고    scopus 로고
    • Electron and proton transport by NADPH oxidases
    • doi:10.1098/rstb.2005.1769
    • Demaurex, N., and G.L. Petheö. 2005. Electron and proton transport by NADPH oxidases. Philos. Trans. R. Soc. Lond. B Biol. Sci. 360:2315-2325. doi:10.1098/rstb.2005.1769
    • (2005) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.360 , pp. 2315-2325
    • Demaurex, N.1    Petheö, G.L.2
  • 9
    • 0026612627 scopus 로고
    • Regulation of Ca2+ influx in myeloid cells. Role of plasma membrane potential, inositol phosphates, cytosolic free [Ca2+], and filling state of intracellular Ca2+ stores
    • doi:10.1172/JCI115958
    • Demaurex, N., W. Schlegel, P. Varnai, G. Mayr, D.P. Lew, and K.H. Krause. 1992. Regulation of Ca2+ influx in myeloid cells. Role of plasma membrane potential, inositol phosphates, cytosolic free [Ca2+], and filling state of intracellular Ca2+ stores. J. Clin. Invest. 90:830-839. doi:10.1172/JCI115958
    • (1992) J. Clin. Invest , vol.90 , pp. 830-839
    • Demaurex, N.1    Schlegel, W.2    Varnai, P.3    Mayr, G.4    Lew, D.P.5    Krause, K.H.6
  • 10
    • 0028118540 scopus 로고
    • Characterization of receptor-mediated and store-regulated Ca2+ influx in human neutrophils
    • Demaurex, N., A. Monod, D.P. Lew, and K.H. Krause. 1994. Characterization of receptor-mediated and store-regulated Ca2+ influx in human neutrophils. Biochem. J. 297:595-601.
    • (1994) Biochem. J , vol.297 , pp. 595-601
    • Demaurex, N.1    Monod, A.2    Lew, D.P.3    Krause, K.H.4
  • 11
    • 0029905493 scopus 로고    scopus 로고
    • Intracellular pH regulation during spreading of human neutrophils
    • doi:10.1083/jcb.133.6.1391
    • Demaurex, N., G.P. Downey, T.K. Waddell, and S. Grinstein. 1996. Intracellular pH regulation during spreading of human neutrophils. J. Cell Biol. 133:1391-1402. doi:10.1083/jcb.133.6.1391
    • (1996) J. Cell Biol , vol.133 , pp. 1391-1402
    • Demaurex, N.1    Downey, G.P.2    Waddell, T.K.3    Grinstein, S.4
  • 12
    • 0037078326 scopus 로고    scopus 로고
    • 2+ changes and calpain activation are required for β integrin-accelerated phagocytosis by human neutrophils
    • doi:10.1083/jcb.200206089
    • 2+ changes and calpain activation are required for β integrin-accelerated phagocytosis by human neutrophils. J. Cell Biol. 159:181-189. doi:10.1083/jcb.200206089
    • (2002) J. Cell Biol , vol.159 , pp. 181-189
    • Dewitt, S.1    Hallett, M.B.2
  • 15
    • 36049032519 scopus 로고    scopus 로고
    • Ca2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages
    • doi:10.1073/pnas.0707719104
    • Evans, J.H., and J.J. Falke. 2007. Ca2+ influx is an essential component of the positive-feedback loop that maintains leading-edge structure and activity in macrophages. Proc. Natl. Acad. Sci. USA. 104:16176-16181. doi:10.1073/pnas.0707719104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16176-16181
    • Evans, J.H.1    Falke, J.J.2
  • 17
    • 0030611889 scopus 로고    scopus 로고
    • Regulation of capacitative Ca2+ influx in human neutrophil granulocytes. Alterations in chronic granulomatous disease
    • doi:10.1074/jbc.272.42.26471
    • Geiszt, M., A. Kapus, K. Német, L. Farkas, and E. Ligeti. 1997. Regulation of capacitative Ca2+ influx in human neutrophil granulocytes. Alterations in chronic granulomatous disease. J. Biol. Chem. 272:26471-26478. doi:10.1074/jbc.272.42.26471
    • (1997) J. Biol. Chem , vol.272 , pp. 26471-26478
    • Geiszt, M.1    Kapus, A.2    Német, K.3    Farkas, L.4    Ligeti, E.5
  • 18
    • 0025598116 scopus 로고
    • Oxidase activation in individual neutrophils is dependent on the onset and magnitude of the Ca2+ signal
    • doi:10.1016/0143-4160(90)90020-U
    • Hallett, M.B., E.V. Davies, and A.K. Campbell. 1990. Oxidase activation in individual neutrophils is dependent on the onset and magnitude of the Ca2+ signal. Cell Calcium. 11:655-663. doi:10.1016/0143-4160(90)90020-U
    • (1990) Cell Calcium , vol.11 , pp. 655-663
    • Hallett, M.B.1    Davies, E.V.2    Campbell, A.K.3
  • 19
    • 0023222602 scopus 로고
    • The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel
    • Henderson, L.M., J.B. Chappell, and O.T. Jones. 1987. The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel. Biochem. J. 246:325-329.
    • (1987) Biochem. J , vol.246 , pp. 325-329
    • Henderson, L.M.1    Chappell, J.B.2    Jones, O.T.3
  • 20
    • 0033564218 scopus 로고    scopus 로고
    • Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012
    • doi:10.1006/abio.1999.4107
    • Imada, I., E.F. Sato, M. Miyamoto, Y. Ichimori, Y. Minamiyama, R. Konaka, and M. Inoue. 1999. Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012. Anal. Biochem. 271:53-58. doi:10.1006/abio.1999.4107
    • (1999) Anal. Biochem , vol.271 , pp. 53-58
    • Imada, I.1    Sato, E.F.2    Miyamoto, M.3    Ichimori, Y.4    Minamiyama, Y.5    Konaka, R.6    Inoue, M.7
  • 21
    • 0025365264 scopus 로고
    • Cytosolic free calcium elevation mediates the phagosome-lysosome fusion during phagocytosis in human neutrophils
    • doi:10.1083/jcb.110.5.1555
    • Jaconi, M.E., D.P. Lew, J.L. Carpentier, K.E. Magnusson, M. Sjögren, and O. Stendahl. 1990. Cytosolic free calcium elevation mediates the phagosome-lysosome fusion during phagocytosis in human neutrophils. J. Cell Biol. 110:1555-1564. doi:10.1083/jcb.110.5.1555
    • (1990) J. Cell Biol , vol.110 , pp. 1555-1564
    • Jaconi, M.E.1    Lew, D.P.2    Carpentier, J.L.3    Magnusson, K.E.4    Sjögren, M.5    Stendahl, O.6
  • 22
    • 0033543695 scopus 로고    scopus 로고
    • A noninvasive fluorimetric procedure for measurement of membrane potential. Quantification of the NADPH oxidase-induced depolarization in activated neutrophils
    • doi:10.1074/jbc.274.37.26098
    • Jankowski, A., and S. Grinstein. 1999. A noninvasive fluorimetric procedure for measurement of membrane potential. Quantification of the NADPH oxidase-induced depolarization in activated neutrophils. J. Biol. Chem. 274:26098-26104. doi:10.1074/jbc.274.37.26098
    • (1999) J. Biol. Chem , vol.274 , pp. 26098-26104
    • Jankowski, A.1    Grinstein, S.2
  • 25
    • 45549106075 scopus 로고    scopus 로고
    • Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1
    • doi:10.1073/pnas.0803277105
    • Lee, S.Y., J.A. Letts, and R. Mackinnon. 2008. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc. Natl. Acad. Sci. USA. 105:7692-7695. doi:10.1073/pnas.0803277105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7692-7695
    • Lee, S.Y.1    Letts, J.A.2    Mackinnon, R.3
  • 26
    • 0033850738 scopus 로고    scopus 로고
    • Dynamic ca(2+)changes in neutrophil phagosomes A source for intracellular ca(2+)during phagolysosome formation?
    • doi:10.1054/ceca.2000. 0130
    • Lundqvist-Gustafsson, H., M. Gustafsson, and C. Dahlgren. 2000. Dynamic ca(2+)changes in neutrophil phagosomes A source for intracellular ca(2+)during phagolysosome formation? Cell Calcium. 27:353-362. doi:10.1054/ceca.2000. 0130
    • (2000) Cell Calcium , vol.27 , pp. 353-362
    • Lundqvist-Gustafsson, H.1    Gustafsson, M.2    Dahlgren, C.3
  • 27
    • 0035839567 scopus 로고    scopus 로고
    • Heme histidine ligands within gp91(phox) modulate proton conduction by the phagocyte NADPH oxidase
    • doi:10.1074/jbc. M010438200
    • Maturana, A., S. Arnaudeau, S. Ryser, B. Banfi, J.P. Hossle, W. Schlegel, K.H. Krause, and N. Demaurex. 2001. Heme histidine ligands within gp91(phox) modulate proton conduction by the phagocyte NADPH oxidase. J. Biol. Chem. 276:30277-30284. doi:10.1074/jbc. M010438200
    • (2001) J. Biol. Chem , vol.276 , pp. 30277-30284
    • Maturana, A.1    Arnaudeau, S.2    Ryser, S.3    Banfi, B.4    Hossle, J.P.5    Schlegel, W.6    Krause, K.H.7    Demaurex, N.8
  • 28
    • 1842845132 scopus 로고    scopus 로고
    • NOX family NADPH oxidases: Do they have built-in proton channels?
    • doi:10.1085/jgp.20028713
    • Maturana, A., K.H. Krause, and N. Demaurex. 2002. NOX family NADPH oxidases: do they have built-in proton channels? J. Gen. Physiol. 120:781-786. doi:10.1085/jgp.20028713
    • (2002) J. Gen. Physiol , vol.120 , pp. 781-786
    • Maturana, A.1    Krause, K.H.2    Demaurex, N.3
  • 29
    • 0036016543 scopus 로고    scopus 로고
    • Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components
    • doi:10.1085/ jgp.20018544
    • Morgan, D., V.V. Cherny, M.O. Price, M.C. Dinauer, and T.E. DeCoursey. 2002. Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components. J. Gen. Physiol. 119:571-580. doi:10.1085/ jgp.20018544
    • (2002) J. Gen. Physiol , vol.119 , pp. 571-580
    • Morgan, D.1    Cherny, V.V.2    Price, M.O.3    Dinauer, M.C.4    DeCoursey, T.E.5
  • 30
    • 29244440845 scopus 로고    scopus 로고
    • The pH dependence of NADPH oxidase in human eosinophils
    • doi:10.1113/jphysiol.2005.094748
    • Morgan, D., V.V. Cherny, R. Murphy, B.Z. Katz, and T.E. DeCoursey. 2005. The pH dependence of NADPH oxidase in human eosinophils. J. Physiol. 569:419-431. doi:10.1113/jphysiol.2005.094748
    • (2005) J. Physiol , vol.569 , pp. 419-431
    • Morgan, D.1    Cherny, V.V.2    Murphy, R.3    Katz, B.Z.4    DeCoursey, T.E.5
  • 31
    • 33847667391 scopus 로고    scopus 로고
    • Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2 alpha activity
    • doi:10.1113/jphysiol.2006.124248
    • Morgan, D., V.V. Cherny, A. Finnegan, J. Bollinger, M.H. Gelb, and T.E. DeCoursey. 2007. Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2 alpha activity. J. Physiol. 579:327-344. doi:10.1113/jphysiol.2006.124248
    • (2007) J. Physiol , vol.579 , pp. 327-344
    • Morgan, D.1    Cherny, V.V.2    Finnegan, A.3    Bollinger, J.4    Gelb, M.H.5    DeCoursey, T.E.6
  • 32
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • doi:10.1038/nature03650
    • Murata, Y., H. Iwasaki, M. Sasaki, K. Inaba, and Y. Okamura. 2005. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature. 435:1239-1243. doi:10.1038/nature03650
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 33
    • 33748894518 scopus 로고    scopus 로고
    • Charge compensation during the phagocyte respiratory burst
    • doi:10.1016/j.bbabio.2006.01.005
    • Murphy, R., and T.E. DeCoursey. 2006. Charge compensation during the phagocyte respiratory burst. Biochim. Biophys. Acta. 1757:996-1011. doi:10.1016/j.bbabio.2006.01.005
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 996-1011
    • Murphy, R.1    DeCoursey, T.E.2
  • 34
    • 57849134544 scopus 로고    scopus 로고
    • The intimate and mysterious relationship between proton channels and NADPH oxidase
    • doi:10.1016/j.febslet.2008.12.005
    • Musset, B., V.V. Cherny, D. Morgan, and T.E. DeCoursey. 2009. The intimate and mysterious relationship between proton channels and NADPH oxidase. FEBS Lett. 583:7-12. doi:10.1016/j.febslet.2008.12.005
    • (2009) FEBS Lett , vol.583 , pp. 7-12
    • Musset, B.1    Cherny, V.V.2    Morgan, D.3    DeCoursey, T.E.4
  • 35
    • 0027943836 scopus 로고
    • Assessment of the contribution of the cytochrome b moiety of the NADPH oxidase to the transmembrane H+ conductance of leukocytes
    • Nanda, A., R. Romanek, J.T. Curnutte, and S. Grinstein. 1994. Assessment of the contribution of the cytochrome b moiety of the NADPH oxidase to the transmembrane H+ conductance of leukocytes. J. Biol. Chem. 269:27280-27285.
    • (1994) J. Biol. Chem , vol.269 , pp. 27280-27285
    • Nanda, A.1    Romanek, R.2    Curnutte, J.T.3    Grinstein, S.4
  • 36
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • doi:10.1111/j.1600-065X.2007. 00550.x
    • Nauseef, W.M. 2007. How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 219:88-102. doi:10.1111/j.1600-065X.2007. 00550.x
    • (2007) Immunol. Rev , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 37
    • 63349109185 scopus 로고    scopus 로고
    • Voltage-gated proton channel is expressed on phagosomes
    • doi:10.1016/j.bbrc.2009.03.036
    • Okochi, Y., M. Sasaki, H. Iwasaki, and Y. Okamura. 2009. Voltage-gated proton channel is expressed on phagosomes. Biochem. Biophys. Res. Commun. 382:274-279. doi:10.1016/j.bbrc.2009.03.036
    • (2009) Biochem. Biophys. Res. Commun , vol.382 , pp. 274-279
    • Okochi, Y.1    Sasaki, M.2    Iwasaki, H.3    Okamura, Y.4
  • 38
    • 20544437867 scopus 로고    scopus 로고
    • Voltage- and NADPH-dependence of electron currents generated by the phagocytic NADPH oxidase
    • doi:10.1042/BJ20041889
    • Petheo, G.L., and N. Demaurex. 2005. Voltage- and NADPH-dependence of electron currents generated by the phagocytic NADPH oxidase. Biochem. J. 388:485-491. doi:10.1042/BJ20041889
    • (2005) Biochem. J , vol.388 , pp. 485-491
    • Petheo, G.L.1    Demaurex, N.2
  • 39
    • 0344304496 scopus 로고    scopus 로고
    • Interactions between electron and proton currents in excised patches from human eosinophils
    • doi:10.1085/jgp.200308891
    • Petheö, G.L., A. Maturana, A. Spät, and N. Demaurex. 2003. Interactions between electron and proton currents in excised patches from human eosinophils. J. Gen. Physiol. 122:713-726. doi:10.1085/jgp.200308891
    • (2003) J. Gen. Physiol , vol.122 , pp. 713-726
    • Petheö, G.L.1    Maturana, A.2    Spät, A.3    Demaurex, N.4
  • 40
    • 33845792042 scopus 로고    scopus 로고
    • Role of nucleotides and phosphoinositides in the stability of electron and proton currents associated with the phagocytic NADPH oxidase
    • doi:10.1042/BJ20060578
    • Petheo, G.L., N.C. Girardin, N. Goossens, G.Z. Molnár, and N. Demaurex. 2006. Role of nucleotides and phosphoinositides in the stability of electron and proton currents associated with the phagocytic NADPH oxidase. Biochem. J. 400:431-438. doi:10.1042/BJ20060578
    • (2006) Biochem. J , vol.400 , pp. 431-438
    • Petheo, G.L.1    Girardin, N.C.2    Goossens, N.3    Molnár, G.Z.4    Demaurex, N.5
  • 41
    • 0037387287 scopus 로고    scopus 로고
    • Calcium signalling is altered in myeloid cells with a deficiency in NADPH oxidase activity
    • doi:10.1046/ j.1365-2249.2003.02138.x
    • Rada, B.K., M. Geiszt, R. Van Bruggen, K. Nemet, D. Roos, and E. Ligeti. 2003. Calcium signalling is altered in myeloid cells with a deficiency in NADPH oxidase activity. Clin. Exp. Immunol. 132:53-60. doi:10.1046/ j.1365-2249.2003.02138.x
    • (2003) Clin. Exp. Immunol , vol.132 , pp. 53-60
    • Rada, B.K.1    Geiszt, M.2    Van Bruggen, R.3    Nemet, K.4    Roos, D.5    Ligeti, E.6
  • 42
    • 33744470441 scopus 로고    scopus 로고
    • Consequences of the electrogenic function of the phagocytic NADPH oxidase
    • doi:10.1098/rstb.2005.1768
    • Rada, B.K., M. Geiszt, C. Hably, and E. Ligeti. 2005. Consequences of the electrogenic function of the phagocytic NADPH oxidase. Philos. Trans. R. Soc. Lond. B Biol. Sci. 360:2293-2300. doi:10.1098/rstb.2005.1768
    • (2005) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.360 , pp. 2293-2300
    • Rada, B.K.1    Geiszt, M.2    Hably, C.3    Ligeti, E.4
  • 43
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • doi:10.1038/nature04700
    • Ramsey, I.S., M.M. Moran, J.A. Chong, and D.E. Clapham. 2006. A voltage-gated proton-selective channel lacking the pore domain. Nature. 440:1213-1216. doi:10.1038/nature04700
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 44
    • 66149104077 scopus 로고    scopus 로고
    • Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst
    • doi:10.1073/pnas.0902761106
    • Ramsey, I.S., E. Ruchti, J.S. Kaczmarek, and D.E. Clapham. 2009. Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst. Proc. Natl. Acad. Sci. USA. 106:7642-7647. doi:10.1073/pnas.0902761106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7642-7647
    • Ramsey, I.S.1    Ruchti, E.2    Kaczmarek, J.S.3    Clapham, D.E.4
  • 46
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • doi:10.1126/science.1122352
    • Sasaki, M., M. Takagi, and Y. Okamura. 2006. A voltage sensor-domain protein is a voltage-gated proton channel. Science. 312:589-592. doi:10.1126/science.1122352
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 47
    • 0027301392 scopus 로고
    • Regulation of cytosolic calcium in blood cells
    • Scharff, O., and B. Foder. 1993. Regulation of cytosolic calcium in blood cells. Physiol. Rev. 73:547-582.
    • (1993) Physiol. Rev , vol.73 , pp. 547-582
    • Scharff, O.1    Foder, B.2
  • 49
    • 0023175462 scopus 로고
    • Absence of both cytochrome b-245 subunits from neutrophils in X-linked chronic granulomatous disease
    • doi:10.1038/326088a0
    • Segal, A.W. 1987. Absence of both cytochrome b-245 subunits from neutrophils in X-linked chronic granulomatous disease. Nature. 326:88-91. doi:10.1038/326088a0
    • (1987) Nature , vol.326 , pp. 88-91
    • Segal, A.W.1
  • 50
    • 0019480640 scopus 로고
    • The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
    • doi:10.1038/290406a0
    • Segal, A.W., M. Geisow, R. Garcia, A. Harper, and R. Miller. 1981. The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH. Nature. 290:406-409. doi:10.1038/290406a0
    • (1981) Nature , vol.290 , pp. 406-409
    • Segal, A.W.1    Geisow, M.2    Garcia, R.3    Harper, A.4    Miller, R.5
  • 51
    • 49049098142 scopus 로고    scopus 로고
    • Identification of formyl peptides from Listeria monocytogenes and Staphylococcus aureus as potent chemoattractants for mouse neutrophils
    • Southgate, E.L., R.L. He, J.L. Gao, P.M. Murphy, M. Nanamori, and R.D. Ye. 2008. Identification of formyl peptides from Listeria monocytogenes and Staphylococcus aureus as potent chemoattractants for mouse neutrophils. J. Immunol. 181:1429-1437.
    • (2008) J. Immunol , vol.181 , pp. 1429-1437
    • Southgate, E.L.1    He, R.L.2    Gao, J.L.3    Murphy, P.M.4    Nanamori, M.5    Ye, R.D.6
  • 52
    • 0031474978 scopus 로고    scopus 로고
    • Voltage-dependent proton transport by the voltage sensor of the Shaker K+ channel
    • doi:10.1016/S0896-6273(00)80422-5
    • Starace, D.M., E. Stefani, and F. Bezanilla. 1997. Voltage-dependent proton transport by the voltage sensor of the Shaker K+ channel. Neuron. 19:1319-1327. doi:10.1016/S0896-6273(00)80422-5
    • (1997) Neuron , vol.19 , pp. 1319-1327
    • Starace, D.M.1    Stefani, E.2    Bezanilla, F.3
  • 53
    • 34547230720 scopus 로고    scopus 로고
    • In situ measurement of the electrical potential across the phagosomal membrane using FRET and its contribution to the proton-motive force
    • doi:10.1073/pnas.0700783104
    • Steinberg, B.E., N. Touret, M. Vargas-Caballero, and S. Grinstein. 2007. In situ measurement of the electrical potential across the phagosomal membrane using FRET and its contribution to the proton-motive force. Proc. Natl. Acad. Sci. USA. 104:9523-9528. doi:10.1073/pnas.0700783104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9523-9528
    • Steinberg, B.E.1    Touret, N.2    Vargas-Caballero, M.3    Grinstein, S.4
  • 54
    • 0019936907 scopus 로고
    • Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones
    • doi:10.1038/299826a0
    • Thomas, R.C., and R.W. Meech. 1982. Hydrogen ion currents and intracellular pH in depolarized voltage-clamped snail neurones. Nature. 299:826-828. doi:10.1038/299826a0
    • (1982) Nature , vol.299 , pp. 826-828
    • Thomas, R.C.1    Meech, R.W.2
  • 55
    • 13244272072 scopus 로고    scopus 로고
    • Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores
    • doi:10.1016/j.neuron.2004.12.047
    • Tombola, F., M.M. Pathak, and E.Y. Isacoff. 2005. Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores. Neuron. 45:379-388. doi:10.1016/j.neuron.2004.12.047
    • (2005) Neuron , vol.45 , pp. 379-388
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 56
    • 43449139690 scopus 로고    scopus 로고
    • The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor
    • doi:10.1016/j.neuron.2008.03.026
    • Tombola, F., M.H. Ulbrich, and E.Y. Isacoff. 2008. The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor. Neuron. 58:546-556. doi:10.1016/j.neuron.2008.03.026
    • (2008) Neuron , vol.58 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 57
    • 0036900969 scopus 로고    scopus 로고
    • Voltage-gated proton "channels": A spectator's viewpoint
    • doi:10.1085/jgp.20028706
    • Touret, N., and S. Grinstein. 2002. Voltage-gated proton "channels": a spectator's viewpoint. J. Gen. Physiol. 120:767-771. doi:10.1085/jgp.20028706
    • (2002) J. Gen. Physiol , vol.120 , pp. 767-771
    • Touret, N.1    Grinstein, S.2


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