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Volumn 98, Issue 2, 2015, Pages 163-172

Salt, chloride, bleach, and innate host defense

Author keywords

Hypochlorous acid; Myeloperoxidase; Neutrophil oxidants; Phagocytes

Indexed keywords

BLEACHING AGENT; CATION; CHLORIDE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; SODIUM CHLORIDE; VOLTAGE GATED CHLORIDE CHANNEL; CFTR PROTEIN, HUMAN; HYPOCHLOROUS ACID;

EID: 84938338059     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.4RU0315-109R     Document Type: Review
Times cited : (39)

References (168)
  • 1
    • 84859513088 scopus 로고    scopus 로고
    • Salt and hypertension: Is salt dietary reduction worth the effort
    • Frisoli, T. M., Schmieder, R. E., Grodzicki, T., Messerli, F. H. (2012) Salt and hypertension: is salt dietary reduction worth the effort? Am. J. Med. 125, 433–439
    • (2012) Am. J. Med , vol.125 , pp. 433-439
    • Frisoli, T.M.1    Schmieder, R.E.2    Grodzicki, T.3    Messerli, F.H.4
  • 3
    • 84879378546 scopus 로고    scopus 로고
    • Salt in health and disease—a delicate balance
    • Kotchen, T. A., Cowley, Jr., A. W., Frohlich, E. D. (2013) Salt in health and disease—a delicate balance. N. Engl. J. Med. 368, 1229–1237
    • (2013) N. Engl. J. Med , vol.368 , pp. 1229-1237
    • Kotchen, T.A.1    Cowley, A.W.2    Frohlich, E.D.3
  • 4
    • 77952375757 scopus 로고    scopus 로고
    • The earliest salt production in the world: An early Neolithic exploitation in Poiana Slatinei-Lunca, Romania
    • Weller, O., Dumitroaia, G. (2005) The earliest salt production in the world: an early Neolithic exploitation in Poiana Slatinei-Lunca, Romania. Antiquity 79, 1–4
    • (2005) Antiquity , vol.79 , pp. 1-4
    • Weller, O.1    Dumitroaia, G.2
  • 7
    • 0029941507 scopus 로고    scopus 로고
    • The history of salt—aspects of interest to the nephrologist
    • Ritz, E. (1996) The history of salt—aspects of interest to the nephrologist. Nephrol. Dial. Transplant. 11, 969–975 (http://www.academia.edu/936358).
    • (1996) Nephrol. Dial. Transplant , vol.11 , pp. 969-975
    • Ritz, E.1
  • 8
    • 70349270307 scopus 로고
    • The treatment of cholera by intravenous saline injections; with particular reference to the contributions of Dr. Thomas Aitchison Latta of Leith
    • Greig, E. D. (1946) The treatment of cholera by intravenous saline injections; with particular reference to the contributions of Dr. Thomas Aitchison Latta of Leith. Edinburgh Med. J. 53, 256–263
    • (1946) Edinburgh Med. J , vol.53 , pp. 256-263
    • Greig, E.D.1
  • 9
    • 0036891044 scopus 로고    scopus 로고
    • William O’Shaughnessy, Thomas Latta and the origins of intravenous saline
    • Baskett, T. F. (2002) William O’Shaughnessy, Thomas Latta and the origins of intravenous saline. Resuscitation 55, 231–234
    • (2002) Resuscitation , vol.55 , pp. 231-234
    • Baskett, T.F.1
  • 10
    • 0036782737 scopus 로고    scopus 로고
    • Wound cleansing: The evidence for the techniques and solutions used
    • Cunliffe, P. J., Fawcett, T. N. (2002) Wound cleansing: the evidence for the techniques and solutions used. Prof. Nurse 18, 95–99
    • (2002) Prof. Nurse , vol.18 , pp. 95-99
    • Cunliffe, P.J.1    Fawcett, T.N.2
  • 11
    • 84902513767 scopus 로고    scopus 로고
    • Salt fluoridation and oral health
    • Marthaler, T. M. (2013) Salt fluoridation and oral health. Acta Med. Acad. 42, 140–155
    • (2013) Acta Med. Acad , vol.42 , pp. 140-155
    • Marthaler, T.M.1
  • 12
    • 84865020912 scopus 로고    scopus 로고
    • Climatotherapy at the Dead Sea: An effective treatment modality for atopic dermatitis with significant positive impact on quality of life
    • Adler-Cohen, C., Czarnowicki, T., Dreiher, J., Ruzicka, T., Ingber, A., Harari, M. (2012) Climatotherapy at the Dead Sea: an effective treatment modality for atopic dermatitis with significant positive impact on quality of life. Dermatitis 23, 75–80
    • (2012) Dermatitis , vol.23 , pp. 75-80
    • Adler-Cohen, C.1    Czarnowicki, T.2    Dreiher, J.3    Ruzicka, T.4    Ingber, A.5    Harari, M.6
  • 13
    • 0029162548 scopus 로고
    • Halotherapy for treatment of respiratory diseases
    • Chervinskaya, A. V., Zilber, N. A. (1995) Halotherapy for treatment of respiratory diseases. J. Aerosol Med. 8, 221–232
    • (1995) J. Aerosol Med , vol.8 , pp. 221-232
    • Chervinskaya, A.V.1    Zilber, N.A.2
  • 15
    • 84866119915 scopus 로고    scopus 로고
    • Current therapy for bronchiolitis
    • Nagakumar, P., Doull, I. (2012) Current therapy for bronchiolitis. Arch. Dis. Child. 97, 827–830
    • (2012) Arch. Dis. Child , vol.97 , pp. 827-830
    • Nagakumar, P.1    Doull, I.2
  • 16
    • 81155137837 scopus 로고    scopus 로고
    • Nebulised 7% hypertonic saline improves lung function and quality of life in bronchiectasis
    • Kellett, F., Robert, N. M. (2011) Nebulised 7% hypertonic saline improves lung function and quality of life in bronchiectasis. Respir. Med. 105, 1831–1835
    • (2011) Respir. Med , vol.105 , pp. 1831-1835
    • Kellett, F.1    Robert, N.M.2
  • 17
    • 84855986652 scopus 로고    scopus 로고
    • The facilitating effect of hypertonic saline on resolution of airway inflammation in cystic fibrosis
    • Reeves, E. P., McElvaney, N. G. (2012) The facilitating effect of hypertonic saline on resolution of airway inflammation in cystic fibrosis. Am. J. Respir. Crit. Care Med. 185, 226–227
    • (2012) Am. J. Respir. Crit. Care Med , vol.185 , pp. 226-227
    • Reeves, E.P.1    McElvaney, N.G.2
  • 18
    • 84862317515 scopus 로고    scopus 로고
    • Hypertonic saline in treatment of pulmonary disease in cystic fibrosis
    • Reeves, E. P., Molloy, K., Pohl, K., McElvaney, N. G. (2012) Hypertonic saline in treatment of pulmonary disease in cystic fibrosis. ScientificWorldJournal 2012, 465230
    • (2012) Scientificworldjournal , vol.2012
    • Reeves, E.P.1    Molloy, K.2    Pohl, K.3    McElvaney, N.G.4
  • 20
    • 84862276328 scopus 로고    scopus 로고
    • Structure, function and diversity of the healthy human microbiome
    • Human Microbiome Project Consortium
    • Human Microbiome Project Consortium. (2012) Structure, function and diversity of the healthy human microbiome. Nature 486, 207–214
    • (2012) Nature , vol.486 , pp. 207-214
  • 21
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill, D. M., Ozinsky, A. (2002) Phagocytosis of microbes: complexity in action. Annu. Rev. Immunol. 20, 825–852
    • (2002) Annu. Rev. Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 24
    • 80052378182 scopus 로고    scopus 로고
    • The historical milestones in the understanding of leukocyte biology initiated by Elie Metchnikoff
    • Cavaillon, J. M. (2011) The historical milestones in the understanding of leukocyte biology initiated by Elie Metchnikoff. J. Leukoc. Biol. 90, 413–424
    • (2011) J. Leukoc. Biol , vol.90 , pp. 413-424
    • Cavaillon, J.M.1
  • 26
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan, C. (2006) Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6, 173–182
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 27
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • Nauseef, W. M. (2007) How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 219, 88–102
    • (2007) Immunol. Rev , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 28
    • 47749151450 scopus 로고    scopus 로고
    • Biological roles for the NOX family NADPH oxidases
    • Nauseef, W. M. (2008) Biological roles for the NOX family NADPH oxidases. J. Biol. Chem. 283, 16961–16965
    • (2008) J. Biol. Chem , vol.283 , pp. 16961-16965
    • Nauseef, W.M.1
  • 30
    • 0030581632 scopus 로고    scopus 로고
    • Superoxide release and NADPH oxidase components in mature human phagocytes: Correlation between functional capacity and amount of functional proteins
    • Yagisawa, M., Yuo, A., Yonemaru, M., Imajoh-Ohmi, S., Kanegasaki, S., Yazaki, Y., Takaku, F. (1996) Superoxide release and NADPH oxidase components in mature human phagocytes: correlation between functional capacity and amount of functional proteins. Biochem. Biophys. Res. Commun. 228, 510–516
    • (1996) Biochem. Biophys. Res. Commun , vol.228 , pp. 510-516
    • Yagisawa, M.1    Yuo, A.2    Yonemaru, M.3    Imajoh-Ohmi, S.4    Kanegasaki, S.5    Yazaki, Y.6    Takaku, F.7
  • 31
    • 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
  • 32
    • 0037417274 scopus 로고    scopus 로고
    • The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels
    • DeCoursey, T. E., Morgan, D., Cherny, V. V. (2003) The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels. Nature 422, 531–534
    • (2003) Nature , vol.422 , pp. 531-534
    • Decoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 33
    • 78649713698 scopus 로고    scopus 로고
    • Physiological roles of voltagegated proton channels in leukocytes
    • Demaurex, N., El Chemaly, A. (2010) Physiological roles of voltagegated proton channels in leukocytes. J. Physiol. 588, 4659–4665
    • (2010) J. Physiol , vol.588 , pp. 4659-4665
    • Demaurex, N.1    El Chemaly, A.2
  • 34
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I. S., Moran, M. M., Chong, J. A., Clapham, D. E. (2006) A voltage-gated proton-selective channel lacking the pore domain. Nature 440, 1213–1216
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 35
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki, M., Takagi, M., Okamura, Y. (2006) A voltage sensor-domain protein is a voltage-gated proton channel. Science 312, 589–592
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 36
    • 0017330320 scopus 로고
    • Inhibition of some functions of polymorphonuclear leukocytes by in vitro zinc
    • Chvapil, M., Stankova, L., Zukoski IV, C., Zukoski III, C. (1977) Inhibition of some functions of polymorphonuclear leukocytes by in vitro zinc. J. Lab. Clin. Med. 89, 135–146
    • (1977) J. Lab. Clin. Med , vol.89 , pp. 135-146
    • Chvapil, M.1    Stankova, L.2    Zukoski, I.C.3    Zukoski, I.C.4
  • 37
    • 66149104077 scopus 로고    scopus 로고
    • Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst
    • Ramsey, I. S., Ruchti, E., Kaczmarek, J. S., Clapham, D. E. (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
    • (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
  • 38
    • 76149085162 scopus 로고    scopus 로고
    • VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification
    • El Chemaly, A., Okochi, Y., Sasaki, M., Arnaudeau, S., Okamura, Y., Demaurex, N. (2010) VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification. J. Exp. Med. 207, 129–139
    • (2010) J. Exp. Med , vol.207 , pp. 129-139
    • El Chemaly, A.1    Okochi, Y.2    Sasaki, M.3    Arnaudeau, S.4    Okamura, Y.5    Demaurex, N.6
  • 39
    • 0014292067 scopus 로고
    • Myeloperoxidase-halide-hydrogen peroxide antibacterial system
    • Klebanoff, S. J. (1968) Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J. Bacteriol. 95, 2131–2138
    • (1968) J. Bacteriol , vol.95 , pp. 2131-2138
    • Klebanoff, S.J.1
  • 41
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • Winterbourn, C. C., Hampton, M. B., Livesey, J. H., Kettle, A. J. (2006) Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing. J. Biol. Chem. 281, 39860–39869
    • (2006) J. Biol. Chem , vol.281 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 42
    • 0020702109 scopus 로고
    • Assessment of chlorination by human neutrophils
    • Foote, C. S., Goyne, T. E., Lehrer, R. I. (1983) Assessment of chlorination by human neutrophils. Nature 301, 715–716
    • (1983) Nature , vol.301 , pp. 715-716
    • Foote, C.S.1    Goyne, T.E.2    Lehrer, R.I.3
  • 43
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss, S. J., Klein, R., Slivka, A., Wei, M. (1982) Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J. Clin. Invest. 70, 598–607
    • (1982) J. Clin. Invest , vol.70 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 44
    • 0020573713 scopus 로고
    • Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils
    • Thomas, E. L., Grisham, M. B., Jefferson, M. M. (1983) Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils. J. Clin. Invest. 72, 441–454
    • (1983) J. Clin. Invest , vol.72 , pp. 441-454
    • Thomas, E.L.1    Grisham, M.B.2    Jefferson, M.M.3
  • 45
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • Chapman, A. L., Hampton, M. B., Senthilmohan, R., Winterbourn, C. C., Kettle, A. J. (2002) Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. J. Biol. Chem. 277, 9757–9762
    • (2002) J. Biol. Chem , vol.277 , pp. 9757-9762
    • Chapman, A.L.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 46
    • 0030723030 scopus 로고    scopus 로고
    • Uses of inorganic hypochlorite (Bleach) in health-care facilities
    • Rutala, W. A., Weber, D. J. (1997) Uses of inorganic hypochlorite (bleach) in health-care facilities. Clin. Microbiol. Rev. 10, 597–610
    • (1997) Clin. Microbiol. Rev , vol.10 , pp. 597-610
    • Rutala, W.A.1    Weber, D.J.2
  • 47
    • 84872476329 scopus 로고    scopus 로고
    • Redox reactions and microbial killing in the neutrophil phagosome
    • Winterbourn, C. C., Kettle, A. J. (2013) Redox reactions and microbial killing in the neutrophil phagosome. Antioxid. Redox Signal. 18, 642–660
    • (2013) Antioxid. Redox Signal , vol.18 , pp. 642-660
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 48
    • 84863430573 scopus 로고    scopus 로고
    • What really happens in the neutrophil phagosome? Free Radic
    • Hurst, J. K. (2012) What really happens in the neutrophil phagosome? Free Radic. Biol. Med. 53, 508–520
    • (2012) Biol. Med , vol.53 , pp. 508-520
    • Hurst, J.K.1
  • 49
    • 78650750400 scopus 로고    scopus 로고
    • Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
    • Davies, M. J. (2011) Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention. J. Clin. Biochem. Nutr. 48, 8–19
    • (2011) J. Clin. Biochem. Nutr , vol.48 , pp. 8-19
    • Davies, M.J.1
  • 50
    • 67649986506 scopus 로고    scopus 로고
    • What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach
    • Pattison, D. I., Hawkins, C. L., Davies, M. J. (2009) What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chem. Res. Toxicol. 22, 807–817
    • (2009) Chem. Res. Toxicol , vol.22 , pp. 807-817
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 51
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • Pattison, D. I., Davies, M. J. (2001) Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem. Res. Toxicol. 14, 1453–1464
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 52
    • 37549016050 scopus 로고    scopus 로고
    • Reactions of chlorine with inorganic and organic compounds during water treatment-kinetics and mechanisms: A critical review
    • Deborde, M., von Gunten, U. (2008) Reactions of chlorine with inorganic and organic compounds during water treatment-kinetics and mechanisms: a critical review. Water Res. 42, 13–51
    • (2008) Water Res , vol.42 , pp. 13-51
    • Deborde, M.1    Von Gunten, U.2
  • 53
    • 70350222052 scopus 로고    scopus 로고
    • Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils
    • Peskin, A. V., Turner, R., Maghzal, G. J., Winterbourn, C. C., Kettle, A. J. (2009) Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils. Biochemistry 48, 10175–10182
    • (2009) Biochemistry , vol.48 , pp. 10175-10182
    • Peskin, A.V.1    Turner, R.2    Maghzal, G.J.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 54
  • 55
    • 73249129955 scopus 로고    scopus 로고
    • Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils
    • Rosen, H., Klebanoff, S. J., Wang, Y., Brot, N., Heinecke, J. W., Fu, X. (2009) Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils. Proc. Natl. Acad. Sci. USA 106, 18686–18691
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18686-18691
    • Rosen, H.1    Klebanoff, S.J.2    Wang, Y.3    Brot, N.4    Heinecke, J.W.5    Fu, X.6
  • 56
    • 0021337229 scopus 로고
    • Myeloperoxidase-dependent fluorescein chlorination by stimulated neutrophils
    • Hurst, J. K., Albrich, J. M., Green, T. R., Rosen, H., Klebanoff, S. (1984) Myeloperoxidase-dependent fluorescein chlorination by stimulated neutrophils. J. Biol. Chem. 259, 4812–4821
    • (1984) J. Biol. Chem , vol.259 , pp. 4812-4821
    • Hurst, J.K.1    Albrich, J.M.2    Green, T.R.3    Rosen, H.4    Klebanoff, S.5
  • 57
    • 84905007179 scopus 로고    scopus 로고
    • Myeloperoxidase in human neutrophil host defence
    • Nauseef, W. M. (2014) Myeloperoxidase in human neutrophil host defence. Cell. Microbiol. 16, 1146–1155
    • (2014) Cell. Microbiol , vol.16 , pp. 1146-1155
    • Nauseef, W.M.1
  • 58
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. (2003) Pathways of oxidative damage. Annu. Rev. Microbiol. 57, 395–418
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 59
    • 0020363971 scopus 로고
    • Oxidative inactivation of Escherichia coli by hypochlorous acid. Rates and differentiation of respiratory from other reaction sites
    • Albrich, J. M., Hurst, J. K. (1982) Oxidative inactivation of Escherichia coli by hypochlorous acid. Rates and differentiation of respiratory from other reaction sites. FEBS Lett. 144, 157–161
    • (1982) FEBS Lett , vol.144 , pp. 157-161
    • Albrich, J.M.1    Hurst, J.K.2
  • 60
    • 0029112912 scopus 로고
    • Role of compartmentation in promoting toxicity of leukocyte-generated strong oxidants
    • Lymar, S. V., Hurst, J. K. (1995) Role of compartmentation in promoting toxicity of leukocyte-generated strong oxidants. Chem. Res. Toxicol. 8, 833–840
    • (1995) Chem. Res. Toxicol , vol.8 , pp. 833-840
    • Lymar, S.V.1    Hurst, J.K.2
  • 61
    • 12444329704 scopus 로고    scopus 로고
    • Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: Effects on host defense
    • Hirche, T. O., Gaut, J. P., Heinecke, J. W., Belaaouaj, A. (2005) Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: effects on host defense. J. Immunol. 174, 1557–1565
    • (2005) J. Immunol , vol.174 , pp. 1557-1565
    • Hirche, T.O.1    Gaut, J.P.2    Heinecke, J.W.3    Belaaouaj, A.4
  • 62
    • 0022446013 scopus 로고
    • Chloride movements in human neutrophils. Diffusion, exchange, and active transport
    • Simchowitz, L., De Weer, P. (1986) Chloride movements in human neutrophils. Diffusion, exchange, and active transport. J. Gen. Physiol. 88, 167–194
    • (1986) J. Gen. Physiol , vol.88 , pp. 167-194
    • Simchowitz, L.1    De Weer, P.2
  • 64
    • 0014560426 scopus 로고
    • Intracellular concentrations of water and of the principal electrolytes determined by analysis of isolated human leucocytes
    • Baron, D. N., Ahmed, S. A. (1969) Intracellular concentrations of water and of the principal electrolytes determined by analysis of isolated human leucocytes. Clin. Sci. 37, 205–219
    • (1969) Clin. Sci , vol.37 , pp. 205-219
    • Baron, D.N.1    Ahmed, S.A.2
  • 65
    • 35748954358 scopus 로고    scopus 로고
    • Chloride movements in human neutrophils during phagocytosis: Characterization and relationship to granule release
    • Busetto, S., Trevisan, E., Decleva, E., Dri, P., Menegazzi, R. (2007) Chloride movements in human neutrophils during phagocytosis: characterization and relationship to granule release. J. Immunol. 179, 4110–4124
    • (2007) J. Immunol , vol.179 , pp. 4110-4124
    • Busetto, S.1    Trevisan, E.2    Decleva, E.3    Dri, P.4    Menegazzi, R.5
  • 66
    • 84908456643 scopus 로고    scopus 로고
    • Protein chlorination in neutrophil phagosomes and correlation with bacterial killing
    • Green, J. N., Kettle, A. J., Winterbourn, C. C. (2014) Protein chlorination in neutrophil phagosomes and correlation with bacterial killing. Free Radic. Biol. Med. 77, 49–56
    • (2014) Free Radic. Biol. Med , vol.77 , pp. 49-56
    • Green, J.N.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 67
    • 33646537788 scopus 로고    scopus 로고
    • Direct measurement of free chloride concentrations in the phagolysosomes of human neutrophils
    • Painter, R. G., Wang, G. (2006) Direct measurement of free chloride concentrations in the phagolysosomes of human neutrophils. Anal. Chem. 78, 3133–3137
    • (2006) Anal. Chem , vol.78 , pp. 3133-3137
    • Painter, R.G.1    Wang, G.2
  • 72
    • 0032912589 scopus 로고    scopus 로고
    • Structure and function of the CFTR chloride channel
    • Sheppard, D. N., Welsh, M. J. (1999) Structure and function of the CFTR chloride channel. Physiol. Rev. 79 ((1): Suppl) S23–S45
    • (1999) Physiol. Rev , vol.79 , Issue.1
    • Sheppard, D.N.1    Welsh, M.J.2
  • 73
    • 15544371839 scopus 로고    scopus 로고
    • Assembly of functional CFTR chloride channels
    • Riordan, J. R. (2005) Assembly of functional CFTR chloride channels. Annu. Rev. Physiol. 67, 701–718
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 701-718
    • Riordan, J.R.1
  • 74
    • 34548852606 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: A biophysical and physiological perspective
    • Zifarelli, G., Pusch, M. (2007) CLC chloride channels and transporters: a biophysical and physiological perspective. Rev. Physiol. Biochem. Pharmacol. 158, 23–76
    • (2007) Rev. Physiol. Biochem. Pharmacol , vol.158 , pp. 23-76
    • Zifarelli, G.1    Pusch, M.2
  • 77
    • 51549120559 scopus 로고    scopus 로고
    • Expression cloning of TMEM16A as a calcium-activated chloride channel subunit
    • Schroeder, B. C., Cheng, T., Jan, Y. N., Jan, L. Y. (2008) Expression cloning of TMEM16A as a calcium-activated chloride channel subunit. Cell 134, 1019–1029
    • (2008) Cell , vol.134 , pp. 1019-1029
    • Schroeder, B.C.1    Cheng, T.2    Jan, Y.N.3    Jan, L.Y.4
  • 79
    • 70349573000 scopus 로고    scopus 로고
    • TMEM16B induces chloride currents activated by calcium in mammalian cells
    • Pifferi, S., Dibattista, M., Menini, A. (2009) TMEM16B induces chloride currents activated by calcium in mammalian cells. Pflugers Arch. 458, 1023–1038
    • (2009) Pflugers Arch , vol.458 , pp. 1023-1038
    • Pifferi, S.1    Dibattista, M.2    Menini, A.3
  • 80
    • 66149160256 scopus 로고    scopus 로고
    • TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals
    • Stöhr, H., Heisig, J. B., Benz, P. M., Schöberl, S., Milenkovic, V. M., Strauss, O., Aartsen, W. M., Wijnholds, J., Weber, B. H., Schulz, H. L. (2009) TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals. J. Neurosci. 29, 6809–6818
    • (2009) J. Neurosci , vol.29 , pp. 6809-6818
    • Stöhr, H.1    Heisig, J.B.2    Benz, P.M.3    Schöberl, S.4    Milenkovic, V.M.5    Strauss, O.6    Aartsen, W.M.7    Wijnholds, J.8    Weber, B.H.9    Schulz, H.L.10
  • 81
    • 84869992899 scopus 로고    scopus 로고
    • Structure, function, and modulation of GABA(A) receptors
    • Sigel, E., Steinmann, M. E. (2012) Structure, function, and modulation of GABA(A) receptors. J. Biol. Chem. 287, 40224–40231
    • (2012) J. Biol. Chem , vol.287 , pp. 40224-40231
    • Sigel, E.1    Steinmann, M.E.2
  • 83
    • 55949107533 scopus 로고    scopus 로고
    • Physiology of cell volume regulation in vertebrates
    • Hoffmann, E. K., Lambert, I. H., Pedersen, S. F. (2009) Physiology of cell volume regulation in vertebrates. Physiol. Rev. 89, 193–277
    • (2009) Physiol. Rev , vol.89 , pp. 193-277
    • Hoffmann, E.K.1    Lambert, I.H.2    Pedersen, S.F.3
  • 87
    • 33744963881 scopus 로고    scopus 로고
    • Anion channels, including ClC-3, are required for normal neutrophil oxidative function, phagocytosis, and transendothelial migration
    • Moreland, J. G., Davis, A. P., Bailey, G., Nauseef, W. M., Lamb, F. S. (2006) Anion channels, including ClC-3, are required for normal neutrophil oxidative function, phagocytosis, and transendothelial migration. J. Biol. Chem. 281, 12277–12288
    • (2006) J. Biol. Chem , vol.281 , pp. 12277-12288
    • Moreland, J.G.1    Davis, A.P.2    Bailey, G.3    Nauseef, W.M.4    Lamb, F.S.5
  • 89
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan, J. R., et al. (1989) Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066–1073
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1
  • 90
    • 84856629737 scopus 로고    scopus 로고
    • CFTR: Folding, misfolding and correcting the DF508 conformational defect
    • Lukacs, G. L., Verkman, A. S. (2012) CFTR: folding, misfolding and correcting the DF508 conformational defect. Trends Mol. Med. 18, 81–91
    • (2012) Trends Mol. Med , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 92
    • 80051663317 scopus 로고    scopus 로고
    • Role of CFTR expressed by neutrophils in modulating acute lung inflammation and injury in mice
    • Su, X., Looney, M. R., Su, H. E., Lee, J. W., Song, Y., Matthay, M. A. (2011) Role of CFTR expressed by neutrophils in modulating acute lung inflammation and injury in mice. Inflamm. Res. 60, 619–632
    • (2011) Inflamm. Res , vol.60 , pp. 619-632
    • Su, X.1    Looney, M.R.2    Su, H.E.3    Lee, J.W.4    Song, Y.5    Matthay, M.A.6
  • 93
    • 0026625385 scopus 로고
    • Expression of the human cystic fibrosis transmembrane conductance regulator gene in the mouse lung after in vivo intratracheal plasmid-mediated gene transfer
    • Yoshimura, K., Rosenfeld, M. A., Nakamura, H., Scherer, E. M., Pavirani, A., Lecocq, J. P., Crystal, R. G. (1992) Expression of the human cystic fibrosis transmembrane conductance regulator gene in the mouse lung after in vivo intratracheal plasmid-mediated gene transfer. Nucleic Acids Res. 20, 3233–3240
    • (1992) Nucleic Acids Res , vol.20 , pp. 3233-3240
    • Yoshimura, K.1    Rosenfeld, M.A.2    Nakamura, H.3    Scherer, E.M.4    Pavirani, A.5    Lecocq, J.P.6    Crystal, R.G.7
  • 95
    • 78049421626 scopus 로고    scopus 로고
    • Specific resistance to Pseudomonas aeruginosa infection in zebrafish is mediated by the cystic fibrosis transmembrane conductance regulator. Infect
    • Phennicie, R. T., Sullivan, M. J., Singer, J. T., Yoder, J. A., Kim, C. H. (2010) Specific resistance to Pseudomonas aeruginosa infection in zebrafish is mediated by the cystic fibrosis transmembrane conductance regulator. Infect. Immun. 78, 4542–4550
    • (2010) Immun , vol.78 , pp. 4542-4550
    • Phennicie, R.T.1    Sullivan, M.J.2    Singer, J.T.3    Yoder, J.A.4    Kim, C.H.5
  • 96
    • 84906968886 scopus 로고    scopus 로고
    • Neutrophil-mediated phagocytic host defense defect in myeloid Cftr-inactivated mice
    • Ng, H. P., Zhou, Y., Song, K., Hodges, C. A., Drumm, M. L., Wang, G. (2014) Neutrophil-mediated phagocytic host defense defect in myeloid Cftr-inactivated mice. PLoS ONE 9, e106813
    • (2014) Plos ONE , vol.9
    • Ng, H.P.1    Zhou, Y.2    Song, K.3    Hodges, C.A.4    Drumm, M.L.5    Wang, G.6
  • 97
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A., Pusch, M. (2005) Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420–423
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 98
    • 22944479662 scopus 로고    scopus 로고
    • Voltagedependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., Zdebik, A. A., Lourdel, S., Jentsch, T. J. (2005) Voltagedependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424–427
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 99
    • 84868129315 scopus 로고    scopus 로고
    • Cell biology and physiology of CLC chloride channels and transporters
    • Stauber, T., Weinert, S., Jentsch, T. J. (2012) Cell biology and physiology of CLC chloride channels and transporters. Compr. Physiol. 2, 1701–1744
    • (2012) Compr. Physiol , vol.2 , pp. 1701-1744
    • Stauber, T.1    Weinert, S.2    Jentsch, T.J.3
  • 100
    • 77449095180 scopus 로고    scopus 로고
    • The ClC-3 Cl2/H+ antiporter becomes uncoupled at low extracellular pH
    • Matsuda, J. J., Filali, M. S., Collins, M. M., Volk, K. A., Lamb, F. S. (2010) The ClC-3 Cl2/H+ antiporter becomes uncoupled at low extracellular pH. J. Biol. Chem. 285, 2569–2579
    • (2010) J. Biol. Chem , vol.285 , pp. 2569-2579
    • Matsuda, J.J.1    Filali, M.S.2    Collins, M.M.3    Volk, K.A.4    Lamb, F.S.5
  • 101
    • 34548801365 scopus 로고    scopus 로고
    • Regulation of vacuolar pH and its modulation by some microbial species
    • Huynh, K. K., Grinstein, S. (2007) Regulation of vacuolar pH and its modulation by some microbial species. Microbiol. Mol. Biol. Rev. 71, 452–462
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 452-462
    • Huynh, K.K.1    Grinstein, S.2
  • 102
    • 0037155215 scopus 로고    scopus 로고
    • Determinants of the phagosomal pH in neutrophils
    • Jankowski, A., Scott, C. C., Grinstein, S. (2002) Determinants of the phagosomal pH in neutrophils. J. Biol. Chem. 277, 6059–6066
    • (2002) J. Biol. Chem , vol.277 , pp. 6059-6066
    • Jankowski, A.1    Scott, C.C.2    Grinstein, S.3
  • 103
    • 34848885825 scopus 로고    scopus 로고
    • Cytokine activation of nuclear factor kappa B in vascular smooth muscle cells requires signaling endosomes containing Nox1 and ClC-3
    • Miller, Jr., F. J., Filali, M., Huss, G. J., Stanic, B., Chamseddine, A., Barna, T. J., Lamb, F. S. (2007) Cytokine activation of nuclear factor kappa B in vascular smooth muscle cells requires signaling endosomes containing Nox1 and ClC-3. Circ. Res. 101, 663–671
    • (2007) Circ. Res , vol.101 , pp. 663-671
    • Miller, F.J.1    Filali, M.2    Huss, G.J.3    Stanic, B.4    Chamseddine, A.5    Barna, T.J.6    Lamb, F.S.7
  • 104
    • 33748894518 scopus 로고    scopus 로고
    • Charge compensation during the phagocyte respiratory burst
    • Murphy, R., DeCoursey, T. E. (2006) Charge compensation during the phagocyte respiratory burst. Biochim. Biophys. Acta 1757, 996–1011
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 996-1011
    • Murphy, R.1    Decoursey, T.E.2
  • 105
    • 76349113357 scopus 로고    scopus 로고
    • Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes
    • DeCoursey, T. E. (2010) Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes. Physiology (Bethesda) 25, 27–40
    • (2010) Physiology (Bethesda) , vol.25 , pp. 27-40
    • Decoursey, T.E.1
  • 107
    • 84899787829 scopus 로고    scopus 로고
    • Hv1 proton channels differentially regulate the pH of neutrophil and macrophage phagosomes by sustaining the production of phagosomal ROS that inhibit the delivery of vacuolar ATPases
    • El Chemaly, A., Nunes, P., Jimaja, W., Castelbou, C., Demaurex, N. (2014) Hv1 proton channels differentially regulate the pH of neutrophil and macrophage phagosomes by sustaining the production of phagosomal ROS that inhibit the delivery of vacuolar ATPases. J. Leukoc. Biol. 95, 827–839
    • (2014) J. Leukoc. Biol , vol.95 , pp. 827-839
    • El Chemaly, A.1    Nunes, P.2    Jimaja, W.3    Castelbou, C.4    Demaurex, N.5
  • 108
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917–929
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 917-929
    • Forgac, M.1
  • 109
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases—nature’s most versatile proton pumps
    • Nishi, T., Forgac, M. (2002) The vacuolar (H+)-ATPases—nature’s most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94–103
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 110
    • 84896692098 scopus 로고    scopus 로고
    • Eukaryotic VATPase: Novel structural findings and functional insights
    • Marshansky, V., Rubinstein, J. L., Grüber, G. (2014) Eukaryotic VATPase: novel structural findings and functional insights. Biochim. Biophys. Acta 1837, 857–879
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 857-879
    • Marshansky, V.1    Rubinstein, J.L.2    Grüber, G.3
  • 111
    • 84883442790 scopus 로고    scopus 로고
    • Regulation of luminal acidification by the V-ATPase
    • Breton, S., Brown, D. (2013) Regulation of luminal acidification by the V-ATPase. Physiology (Bethesda) 28, 318–329
    • (2013) Physiology (Bethesda) , vol.28 , pp. 318-329
    • Breton, S.1    Brown, D.2
  • 112
    • 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
    • Steinberg, B. E., Touret, N., Vargas-Caballero, M., Grinstein, S. (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
    • (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
  • 113
    • 84864117779 scopus 로고    scopus 로고
    • K⁺-Cl⁻ cotransport mediates the bactericidal activity of neutrophils by regulating NADPH oxidase activation
    • Sun, Y. T., Shieh, C. C., Delpire, E., Shen, M. R. (2012) K⁺-Cl⁻ cotransport mediates the bactericidal activity of neutrophils by regulating NADPH oxidase activation. J. Physiol. 590, 3231–3243
    • (2012) J. Physiol , vol.590 , pp. 3231-3243
    • Sun, Y.T.1    Shieh, C.C.2    Delpire, E.3    Shen, M.R.4
  • 114
    • 8644288484 scopus 로고    scopus 로고
    • Regulation of K-Cl cotransport: From function to genes
    • Adragna, N. C., Di Fulvio, M., Lauf, P. K. (2004) Regulation of K-Cl cotransport: from function to genes. J. Membr. Biol. 201, 109–137
    • (2004) J. Membr. Biol , vol.201 , pp. 109-137
    • Adragna, N.C.1    Di Fulvio, M.2    Lauf, P.K.3
  • 115
    • 15544384004 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters
    • Gamba, G. (2005) Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters. Physiol. Rev. 85, 423–493
    • (2005) Physiol. Rev , vol.85 , pp. 423-493
    • Gamba, G.1
  • 116
    • 0022555398 scopus 로고
    • Volume changes in activated human neutrophils: The role of Na+/H+ exchange
    • Grinstein, S., Furuya, W., Cragoe, Jr., E. J. (1986) Volume changes in activated human neutrophils: the role of Na+/H+ exchange. J. Cell. Physiol. 128, 33–40
    • (1986) J. Cell. Physiol , vol.128 , pp. 33-40
    • Grinstein, S.1    Furuya, W.2    Cragoe, E.J.3
  • 117
    • 84900406113 scopus 로고    scopus 로고
    • Structure and function of TMEM16 proteins (Anoctamins)
    • Pedemonte, N., Galietta, L. J. (2014) Structure and function of TMEM16 proteins (anoctamins). Physiol. Rev. 94, 419–459
    • (2014) Physiol. Rev , vol.94 , pp. 419-459
    • Pedemonte, N.1    Galietta, L.J.2
  • 119
    • 0029757293 scopus 로고    scopus 로고
    • Characteristics and physiological role of the Ca(2+)-activated Cl2 conductance in smooth muscle
    • Large, W. A., Wang, Q. (1996) Characteristics and physiological role of the Ca(2+)-activated Cl2 conductance in smooth muscle. Am. J. Physiol. 271, C435–C454
    • (1996) Am. J. Physiol , vol.271
    • Large, W.A.1    Wang, Q.2
  • 120
    • 0030816336 scopus 로고    scopus 로고
    • Neutrophil receptors for interleukin-8 and related CXC chemokines
    • Murphy, P. M. (1997) Neutrophil receptors for interleukin-8 and related CXC chemokines. Semin. Hematol. 34, 311–318
    • (1997) Semin. Hematol , vol.34 , pp. 311-318
    • Murphy, P.M.1
  • 121
    • 0028202481 scopus 로고
    • The molecular biology of leukocyte chemoattractant receptors
    • Murphy, P. M. (1994) The molecular biology of leukocyte chemoattractant receptors. Annu. Rev. Immunol. 12, 593–633
    • (1994) Annu. Rev. Immunol , vol.12 , pp. 593-633
    • Murphy, P.M.1
  • 122
    • 0026523829 scopus 로고
    • Cystic fibrosis: Molecular biology and therapeutic implications
    • Collins, F. S. (1992) Cystic fibrosis: molecular biology and therapeutic implications. Science 256, 774–779
    • (1992) Science , vol.256 , pp. 774-779
    • Collins, F.S.1
  • 128
    • 84924677754 scopus 로고    scopus 로고
    • Influence of neutrophil defects on Burkholderia cepacia complex pathogenesis
    • Porter, L. A., Goldberg, J. B. (2011) Influence of neutrophil defects on Burkholderia cepacia complex pathogenesis. Front. Cell. Infect. Microbiol. 1, 9
    • (2011) Front. Cell. Infect. Microbiol , vol.1 , Issue.9
    • Porter, L.A.1    Goldberg, J.B.2
  • 129
    • 70449140148 scopus 로고
    • A fatal granulomatosus of childhood: The clinical study of a new syndrome
    • Berendes, H., Bridges, R. A., Good, R. A. (1957) A fatal granulomatosus of childhood: the clinical study of a new syndrome. Minn. Med. 40, 309–312
    • (1957) Minn. Med , vol.40 , pp. 309-312
    • Berendes, H.1    Bridges, R.A.2    Good, R.A.3
  • 130
    • 0014124339 scopus 로고
    • Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function
    • Holmes, B., Page, A. R., Good, R. A. (1967) Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function. J. Clin. Invest. 46, 1422–1432
    • (1967) J. Clin. Invest , vol.46 , pp. 1422-1432
    • Holmes, B.1    Page, A.R.2    Good, R.A.3
  • 132
    • 84859620802 scopus 로고    scopus 로고
    • Cystic fibrosis: A mucosal immunodeficiency syndrome
    • Cohen, T. S., Prince, A. (2012) Cystic fibrosis: a mucosal immunodeficiency syndrome. Nat. Med. 18, 509–519
    • (2012) Nat. Med , vol.18 , pp. 509-519
    • Cohen, T.S.1    Prince, A.2
  • 133
    • 0036194724 scopus 로고    scopus 로고
    • Mucus clearance as a primary innate defense mechanism for mammalian airways
    • Knowles, M. R., Boucher, R. C. (2002) Mucus clearance as a primary innate defense mechanism for mammalian airways. J. Clin. Invest. 109, 571–577
    • (2002) J. Clin. Invest , vol.109 , pp. 571-577
    • Knowles, M.R.1    Boucher, R.C.2
  • 134
    • 0037279811 scopus 로고    scopus 로고
    • Regulation of airway surface liquid volume by human airway epithelia
    • Boucher, R. C. (2003) Regulation of airway surface liquid volume by human airway epithelia. Pflugers Arch. 445, 495–498
    • (2003) Pflugers Arch , vol.445 , pp. 495-498
    • Boucher, R.C.1
  • 136
    • 0036197412 scopus 로고    scopus 로고
    • [beta]-Defensins in lung host defense
    • Schutte, B. C., McCray, Jr., P. B. (2002) [beta]-Defensins in lung host defense. Annu. Rev. Physiol. 64, 709–748
    • (2002) Annu. Rev. Physiol , vol.64 , pp. 709-748
    • Schutte, B.C.1    McCray, P.B.2
  • 137
    • 84868322168 scopus 로고    scopus 로고
    • Absence of the cystic fibrosis transmembrane regulator (Cftr) from myeloid-derived cells slows resolution of inflammation and infection
    • Bonfield, T. L., Hodges, C. A., Cotton, C. U., Drumm, M. L. (2012) Absence of the cystic fibrosis transmembrane regulator (Cftr) from myeloid-derived cells slows resolution of inflammation and infection. J. Leukoc. Biol. 92, 1111–1122
    • (2012) J. Leukoc. Biol , vol.92 , pp. 1111-1122
    • Bonfield, T.L.1    Hodges, C.A.2    Cotton, C.U.3    Drumm, M.L.4
  • 143
    • 0034676433 scopus 로고    scopus 로고
    • ClC-5 Cl2 -channel disruption impairs endocytosis in a mouse model for Dent’s disease
    • Piwon, N., Günther, W., Schwake, M., Bösl, M. R., Jentsch, T. J. (2000) ClC-5 Cl2 -channel disruption impairs endocytosis in a mouse model for Dent’s disease. Nature 408, 369–373
    • (2000) Nature , vol.408 , pp. 369-373
    • Piwon, N.1    Günther, W.2    Schwake, M.3    Bösl, M.R.4    Jentsch, T.J.5
  • 144
    • 84888432895 scopus 로고    scopus 로고
    • A single point mutation reveals gating of the human ClC-5 Cl2/H+ antiporter
    • De Stefano, S., Pusch, M., Zifarelli, G. (2013) A single point mutation reveals gating of the human ClC-5 Cl2/H+ antiporter. J. Physiol. 591, 5879–5893
    • (2013) J. Physiol , vol.591 , pp. 5879-5893
    • De Stefano, S.1    Pusch, M.2    Zifarelli, G.3
  • 145
    • 77953555147 scopus 로고    scopus 로고
    • Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis
    • Novarino, G., Weinert, S., Rickheit, G., Jentsch, T. J. (2010) Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis. Science 328, 1398–1401
    • (2010) Science , vol.328 , pp. 1398-1401
    • Novarino, G.1    Weinert, S.2    Rickheit, G.3    Jentsch, T.J.4
  • 146
    • 83555168269 scopus 로고    scopus 로고
    • Decreased renal accumulation of aminoglycoside reflects defective receptor-mediated endocytosis in cystic fibrosis and Dent’s disease
    • Raggi, C., Fujiwara, K., Leal, T., Jouret, F., Devuyst, O., Terryn, S. (2011) Decreased renal accumulation of aminoglycoside reflects defective receptor-mediated endocytosis in cystic fibrosis and Dent’s disease. Pflugers Arch. 462, 851–860
    • (2011) Pflugers Arch , vol.462 , pp. 851-860
    • Raggi, C.1    Fujiwara, K.2    Leal, T.3    Jouret, F.4    Devuyst, O.5    Terryn, S.6
  • 150
    • 44849107047 scopus 로고    scopus 로고
    • The Cl2/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
    • Graves, A. R., Curran, P. K., Smith, C. L., Mindell, J. A. (2008) The Cl2/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes. Nature 453, 788–792
    • (2008) Nature , vol.453 , pp. 788-792
    • Graves, A.R.1    Curran, P.K.2    Smith, C.L.3    Mindell, J.A.4
  • 151
    • 77954357979 scopus 로고    scopus 로고
    • The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression
    • Neagoe, I., Stauber, T., Fidzinski, P., Bergsdorf, E. Y., Jentsch, T. J. (2010) The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression. J. Biol. Chem. 285, 21689–21697
    • (2010) J. Biol. Chem , vol.285 , pp. 21689-21697
    • Neagoe, I.1    Stauber, T.2    Fidzinski, P.3    Bergsdorf, E.Y.4    Jentsch, T.J.5
  • 154
    • 72749119040 scopus 로고    scopus 로고
    • Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC-7
    • Wartosch, L., Fuhrmann, J. C., Schweizer, M., Stauber, T., Jentsch, T. J. (2009) Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC-7. FASEB J. 23, 4056–4068
    • (2009) FASEB J , vol.23 , pp. 4056-4068
    • Wartosch, L.1    Fuhrmann, J.C.2    Schweizer, M.3    Stauber, T.4    Jentsch, T.J.5
  • 155
  • 156
    • 79960843311 scopus 로고    scopus 로고
    • Ca2+-activated Cl2 currents are dispensable for olfaction
    • Billig, G. M., Pál, B., Fidzinski, P., Jentsch, T. J. (2011) Ca2+-activated Cl2 currents are dispensable for olfaction. Nat. Neurosci. 14, 763–769
    • (2011) Nat. Neurosci , vol.14 , pp. 763-769
    • Billig, G.M.1    Pál, B.2    Fidzinski, P.3    Jentsch, T.J.4
  • 158
    • 0033621752 scopus 로고    scopus 로고
    • Neuronal Ca2+ -activated Cl2 channels—homing in on an elusive channel species
    • Frings, S., Reuter, D., Kleene, S. J. (2000) Neuronal Ca2+ -activated Cl2 channels—homing in on an elusive channel species. Prog. Neurobiol. 60, 247–289
    • (2000) Prog. Neurobiol , vol.60 , pp. 247-289
    • Frings, S.1    Reuter, D.2    Kleene, S.J.3
  • 159
    • 65749107143 scopus 로고    scopus 로고
    • Phenomics of cardiac chloride channels: The systematic study of chloride channel function in the heart
    • Duan, D. (2009) Phenomics of cardiac chloride channels: the systematic study of chloride channel function in the heart. J. Physiol. 587, 2163–2177
    • (2009) J. Physiol , vol.587 , pp. 2163-2177
    • Duan, D.1
  • 161
    • 79958153355 scopus 로고    scopus 로고
    • Physiological roles and diseases of Tmem16/anoctamin proteins: Are they all chloride channels?
    • Duran, C., Hartzell, H. C. (2011) Physiological roles and diseases of Tmem16/anoctamin proteins: are they all chloride channels? Acta Pharmacol. Sin. 32, 685–692
    • (2011) Acta Pharmacol. Sin , vol.32 , pp. 685-692
    • Duran, C.1    Hartzell, H.C.2
  • 162
    • 49049118639 scopus 로고    scopus 로고
    • The transmembrane protein TMEM16A is required for normal development of the murine trachea
    • Rock, J. R., Futtner, C. R., Harfe, B. D. (2008) The transmembrane protein TMEM16A is required for normal development of the murine trachea. Dev. Biol. 321, 141–149
    • (2008) Dev. Biol , vol.321 , pp. 141-149
    • Rock, J.R.1    Futtner, C.R.2    Harfe, B.D.3
  • 164
    • 84887386469 scopus 로고    scopus 로고
    • Subdued, a TMEM16 family Ca²⁺-activated Cl⁻channel in Drosophila melanogaster with an unexpected role in host defense
    • Wong, X. M., Younger, S., Peters, C. J., Jan, Y. N., Jan, L. Y. (2013) Subdued, a TMEM16 family Ca²⁺-activated Cl⁻channel in Drosophila melanogaster with an unexpected role in host defense. eLife 2, e00862
    • (2013) Elife , vol.2
    • Wong, X.M.1    Younger, S.2    Peters, C.J.3    Jan, Y.N.4    Jan, L.Y.5
  • 165
    • 0025633960 scopus 로고
    • Evidence for a DIOA-sensitive [K+,Cl2-cotransport system in cultured vascular smooth muscle cells
    • Saitta, M., Cavalier, S., Garay, R., Cragoe, Jr., E., Hannaert, P. (1990) Evidence for a DIOA-sensitive [K+,Cl2-cotransport system in cultured vascular smooth muscle cells. Am. J. Hypertens. 3, 939–942
    • (1990) Am. J. Hypertens , vol.3 , pp. 939-942
    • Saitta, M.1    Cavalier, S.2    Garay, R.3    Cragoe, E.4    Hannaert, P.5
  • 167
    • 0034531318 scopus 로고    scopus 로고
    • K-Cl cotransport: Properties and molecular mechanism
    • Lauf, P. K., Adragna, N. C. (2000) K-Cl cotransport: properties and molecular mechanism. Cell. Physiol. Biochem. 10, 341–354
    • (2000) Cell. Physiol. Biochem , vol.10 , pp. 341-354
    • Lauf, P.K.1    Adragna, N.C.2
  • 168
    • 0036193948 scopus 로고    scopus 로고
    • Human and murine phenotypes associated with defects in cation-chloride cotransport
    • Delpire, E., Mount, D. B. (2002) Human and murine phenotypes associated with defects in cation-chloride cotransport. Annu. Rev. Physiol. 64, 803–843.
    • (2002) Annu. Rev. Physiol , vol.64 , pp. 803-843
    • Delpire, E.1    Mount, D.B.2


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