메뉴 건너뛰기




Volumn 109, Issue 2, 1997, Pages 201-216

Electrodiffusion, barrier, and gating analysis of DIDS-insensitive chloride conductance in human red blood cells treated with valinomycin or gramicidin

Author keywords

band 3 protein; chloride channels; erythrocyte membrane; ion transport; membrane potentials

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; CHLORIDE CHANNEL; CHLORIDE ION; ERYTHROCYTE BAND 3 PROTEIN; GRAMICIDIN; POTASSIUM ION; VALINOMYCIN;

EID: 0031040792     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.109.2.201     Document Type: Article
Times cited : (13)

References (88)
  • 1
    • 0026070573 scopus 로고
    • The band 3-related anion exchanger (AE) gene family
    • Alper, S.L. 1991. The band 3-related anion exchanger (AE) gene family. Annu. Rev. Physiol. 53:549-564.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 549-564
    • Alper, S.L.1
  • 2
    • 0020630895 scopus 로고
    • Ion movement through gramicidin A channels. Single-channel measurements at very high potentials
    • Andersen, O.S. 1983a. Ion movement through gramicidin A channels. Single-channel measurements at very high potentials. Biophys. J. 41:119-133.
    • (1983) Biophys. J. , vol.41 , pp. 119-133
    • Andersen, O.S.1
  • 3
    • 0020630896 scopus 로고
    • Ion movement through gramicidin A channels. Studies on the diffusion-controlled association step
    • Andersen, O.S. 1983b. Ion movement through gramicidin A channels. Studies on the diffusion-controlled association step. Biophys. J. 41:147-165.
    • (1983) Biophys. J. , vol.41 , pp. 147-165
    • Andersen, O.S.1
  • 5
    • 0018759156 scopus 로고
    • Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids
    • Barzilay, M., S. Ship, and Z.I. Cabantchik. 1979. Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids. Membr. Biochem. 2:227-254.
    • (1979) Membr. Biochem. , vol.2 , pp. 227-254
    • Barzilay, M.1    Ship, S.2    Cabantchik, Z.I.3
  • 6
    • 0027441377 scopus 로고
    • Near-UV circular dichroism of band 3. Evidence for intradomain conformational changes and interdomain interactions
    • Batenjany, M.M., H. Mizukami, and J.M. Salhany. 1993. Near-UV circular dichroism of band 3. Evidence for intradomain conformational changes and interdomain interactions. Biochemistry. 32: 663-668.
    • (1993) Biochemistry , vol.32 , pp. 663-668
    • Batenjany, M.M.1    Mizukami, H.2    Salhany, J.M.3
  • 7
    • 0021169882 scopus 로고
    • +-Valinomycin and chloride conductance of the human red cell membrane. Influence of the membrane protonophore carbonylcyanide m-chlorophenylhydrazone
    • +-Valinomycin and chloride conductance of the human red cell membrane. Influence of the membrane protonophore carbonylcyanide m-chlorophenylhydrazone. Biochim. Biophys. Acta. 776:1-9.
    • (1984) Biochim. Biophys. Acta , vol.776 , pp. 1-9
    • Bennekou, P.1
  • 8
    • 0023877139 scopus 로고
    • Protonophore anion permeability of the human red cell membrane determined in the presence of valinomycin
    • Bennekou, P. 1988. Protonophore anion permeability of the human red cell membrane determined in the presence of valinomycin. J. Membr. Biol. 102:225-234.
    • (1988) J. Membr. Biol. , vol.102 , pp. 225-234
    • Bennekou, P.1
  • 9
    • 0022897994 scopus 로고
    • + fluxes across the human red cell membrane in the presence of the protonophore CCCP
    • + fluxes across the human red cell membrane in the presence of the protonophore CCCP. J. Membr. Biol. 93:221-227.
    • (1986) J. Membr. Biol. , vol.93 , pp. 221-227
    • Bennekou, P.1    Christophersen, P.2
  • 10
    • 0023942263 scopus 로고
    • The effect of ATP, intracellular calcium and the anion exchange inhibitor DIDS on conductive anion fluxes across the human red cell membrane
    • Bennekou, P., and P. Stampe. 1988. The effect of ATP, intracellular calcium and the anion exchange inhibitor DIDS on conductive anion fluxes across the human red cell membrane. Biochim. Biophys. Acta. 942:179-185.
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 179-185
    • Bennekou, P.1    Stampe, P.2
  • 11
  • 12
    • 0021160776 scopus 로고
    • The relationship between the shape and the membrane potential of human red blood cells
    • Bifano, E.M., T.S. Novak, and J.C. Freedman. 1984. The relationship between the shape and the membrane potential of human red blood cells. J. Membr. Biol. 82:1-13.
    • (1984) J. Membr. Biol. , vol.82 , pp. 1-13
    • Bifano, E.M.1    Novak, T.S.2    Freedman, J.C.3
  • 13
    • 0015529173 scopus 로고
    • The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives
    • Cabantchik, Z.I., and A. Rothstein. 1972. The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives. J. Membr. Biol. 10:311-330.
    • (1972) J. Membr. Biol. , vol.10 , pp. 311-330
    • Cabantchik, Z.I.1    Rothstein, A.2
  • 14
    • 0020564299 scopus 로고
    • Characterization of a chloride conductance activated by hyperpolarization in Aplysia neurones
    • Chesnoy-Marchais, D. 1983. Characterization of a chloride conductance activated by hyperpolarization in Aplysia neurones. J. Physiol. (Lond.). 342:277-308.
    • (1983) J. Physiol. (Lond.) , vol.342 , pp. 277-308
    • Chesnoy-Marchais, D.1
  • 15
    • 0020078507 scopus 로고
    • Discrimination of three parallel pathways of lactate transport in the human erythrocyte membrane by inhibitors and kinetic properties
    • Deuticke, B., E. Beyer, and B. Forst. 1982. Discrimination of three parallel pathways of lactate transport in the human erythrocyte membrane by inhibitors and kinetic properties. Biochim. Biophys. Acta. 684:96-110.
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 96-110
    • Deuticke, B.1    Beyer, E.2    Forst, B.3
  • 16
    • 0022887603 scopus 로고
    • Molecular mechanism of band 3 inhibitors. I. Transport site inhibitors
    • Falke, J.J., and S.I. Chan. 1986a. Molecular mechanism of band 3 inhibitors. I. Transport site inhibitors. Biochemistry. 25:7888-7894.
    • (1986) Biochemistry , vol.25 , pp. 7888-7894
    • Falke, J.J.1    Chan, S.I.2
  • 17
    • 0022899863 scopus 로고
    • Molecular mechanism of band 3 inhibitors. 2. Channel blockers
    • Falke, J.J., and S.I. Chan. 1986b. Molecular mechanism of band 3 inhibitors. 2. Channel blockers. Biochemistry. 25:7895-7898.
    • (1986) Biochemistry , vol.25 , pp. 7895-7898
    • Falke, J.J.1    Chan, S.I.2
  • 18
    • 0024150398 scopus 로고
    • Membrane potential and the cytotoxic Ca cascade of human red blood cells
    • R.B. Gunn and J.C. Parker, editors. Society of General Physiologists Series, The Rockefeller University Press, New York, NY
    • Freedman, J.C., E.M. Bifano, L.M. Crespo, P.R. Pratap, R. Walenga, R.E. Bailey, S. Zuk, and T.S. Novak. 1988. Membrane potential and the cytotoxic Ca cascade of human red blood cells. In Cell Physiology of Blood. R.B. Gunn and J.C. Parker, editors. Society of General Physiologists Series, The Rockefeller University Press, New York, NY. 218-231.
    • (1988) Cell Physiology of Blood , pp. 218-231
    • Freedman, J.C.1    Bifano, E.M.2    Crespo, L.M.3    Pratap, P.R.4    Walenga, R.5    Bailey, R.E.6    Zuk, S.7    Novak, T.S.8
  • 19
    • 0018392170 scopus 로고
    • Ionic and osmotic equilibria of human red blood cells treated with nystatin
    • Freedman, J.C., and J.F. Hoffman. 1979a. Ionic and osmotic equilibria of human red blood cells treated with nystatin. J. Gen. Physiol. 74:157-185.
    • (1979) J. Gen. Physiol. , vol.74 , pp. 157-185
    • Freedman, J.C.1    Hoffman, J.F.2
  • 20
    • 0018289772 scopus 로고
    • The relation between dicarbo-cyanine dye fluorescence and the membrane potential of human red blood cells set at varying Donnan equilibria
    • Freedman, J.C., and J.F. Hoffman. 1979b. The relation between dicarbo-cyanine dye fluorescence and the membrane potential of human red blood cells set at varying Donnan equilibria. J. Gen. Physiol. 174:187-212.
    • (1979) J. Gen. Physiol. , vol.174 , pp. 187-212
    • Freedman, J.C.1    Hoffman, J.F.2
  • 21
    • 84987012958 scopus 로고
    • Membrane vesicles from human red blood cells in planar lipid bilayers
    • Freedman, J.C., and C. Miller. 1984. Membrane vesicles from human red blood cells in planar lipid bilayers. Ann. NY Acad. Sci. 435:541-544.
    • (1984) Ann. NY Acad. Sci. , vol.435 , pp. 541-544
    • Freedman, J.C.1    Miller, C.2
  • 22
    • 0020636789 scopus 로고
    • Membrane potentials associated with Ca-induced K conductance in human red blood cells. Studies with a fluorescent oxonol dye, WW781
    • Freedman, J.C., and T.S. Novak. 1983. Membrane potentials associated with Ca-induced K conductance in human red blood cells. Studies with a fluorescent oxonol dye, WW781. J. Membr. Biol. 72: 59-74.
    • (1983) J. Membr. Biol. , vol.72 , pp. 59-74
    • Freedman, J.C.1    Novak, T.S.2
  • 23
    • 85012414286 scopus 로고
    • K and Cl conductance of valinomycin treated human red blood cells, as determined the fluorescent potentiometric indicator WW781
    • Abstr.
    • Freedman, J.C., and T.S. Novak. 1984. K and Cl conductance of valinomycin treated human red blood cells, as determined the fluorescent potentiometric indicator WW781. J. Gen. Physiol. 184:18a. (Abstr.)
    • (1984) J. Gen. Physiol. , vol.184
    • Freedman, J.C.1    Novak, T.S.2
  • 25
    • 0024413230 scopus 로고
    • Optical measurements of membrane potential in cells, organelles, and vesicles
    • Freedman, J.C., and T.S. Novak. 1989. Optical measurements of membrane potential in cells, organelles, and vesicles. Methods Enzymol. 172:102-122.
    • (1989) Methods Enzymol. , vol.172 , pp. 102-122
    • Freedman, J.C.1    Novak, T.S.2
  • 26
    • 15444346659 scopus 로고    scopus 로고
    • Equivalent gating charge of DIDS-insensitive chloride conductance in human red blood cells treated with valinomycin or gramicidin
    • Abstr.
    • Freedman, J.C., and T.S. Novak. 1996. Equivalent gating charge of DIDS-insensitive chloride conductance in human red blood cells treated with valinomycin or gramicidin. Biophys. J. 70:A241. (Abstr.)
    • (1996) Biophys. J. , vol.70
    • Freedman, J.C.1    Novak, T.S.2
  • 27
    • 0027986935 scopus 로고
    • Voltage dependence of DIDS-insensitive chloride conductance in human red blood cells treated with valinomycin or gramicidin
    • Freedman, J.C., T.S. Novak, J.D. Bisognano, and P.R. Pratap. 1994. Voltage dependence of DIDS-insensitive chloride conductance in human red blood cells treated with valinomycin or gramicidin. J. Gen. Physiol. 104:961-983.
    • (1994) J. Gen. Physiol. , vol.104 , pp. 961-983
    • Freedman, J.C.1    Novak, T.S.2    Bisognano, J.D.3    Pratap, P.R.4
  • 28
    • 0020660721 scopus 로고
    • Chloride net efflux from intact erythrocytes under slippage conditions
    • Fröhlich, O., C. Leibson, and R.B. Gunn. 1983. Chloride net efflux from intact erythrocytes under slippage conditions. J. Gen. Physiol. 81:127-152.
    • (1983) J. Gen. Physiol. , vol.81 , pp. 127-152
    • Fröhlich, O.1    Leibson, C.2    Gunn, R.B.3
  • 29
    • 0017021505 scopus 로고
    • Chloride transport in human erythrocytes and ghosts: A quantitative comparison
    • Funder, J., and J.O. Wieth. 1976. Chloride transport in human erythrocytes and ghosts: a quantitative comparison. J. Physiol. (Lond.). 262:679-698.
    • (1976) J. Physiol. (Lond.) , vol.262 , pp. 679-698
    • Funder, J.1    Wieth, J.O.2
  • 30
    • 0024316827 scopus 로고
    • Lysine 539 of human band 3 is not essential for ion transport or inhibition by stilbene disulfonates
    • Garcia, A.M., and H.F. Lodish. 1989. Lysine 539 of human band 3 is not essential for ion transport or inhibition by stilbene disulfonates. J. Biol. Chem. 264:19607-19613.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19607-19613
    • Garcia, A.M.1    Lodish, H.F.2
  • 31
    • 0027294886 scopus 로고
    • Kinetics of residual chloride transport in human red blood cells after maximum covalent 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid binding
    • Gasbjerg, P.K., J. Funder, and J. Brahm. 1993. Kinetics of residual chloride transport in human red blood cells after maximum covalent 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid binding. J. On. Physiol. 101:715-732.
    • (1993) J. On. Physiol. , vol.101 , pp. 715-732
    • Gasbjerg, P.K.1    Funder, J.2    Brahm, J.3
  • 32
    • 85012319658 scopus 로고
    • Potential, impedance and rectification in membranes
    • Goldman, D.E. 1943. Potential, impedance and rectification in membranes. J. Gen. Physiol. 27:37-60.
    • (1943) J. Gen. Physiol. , vol.27 , pp. 37-60
    • Goldman, D.E.1
  • 33
    • 0011834540 scopus 로고
    • Considerations of the titratable carrier model for sulfate transport in human red blood cells
    • J.F. Hoffman, editor. Raven Press, New York, NY
    • Gunn, R.B. 1978. Considerations of the titratable carrier model for sulfate transport in human red blood cells. In Membrane Transport Processes. Vol. 1. J.F. Hoffman, editor. Raven Press, New York, NY. 61-77.
    • (1978) Membrane Transport Processes , vol.1 , pp. 61-77
    • Gunn, R.B.1
  • 34
    • 0018638065 scopus 로고
    • Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time
    • Gunn, R.B., and O. Fröhlich. 1979. Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time. J. Gen. Physiol. 74:351-374.
    • (1979) J. Gen. Physiol. , vol.74 , pp. 351-374
    • Gunn, R.B.1    Fröhlich, O.2
  • 35
    • 0000856782 scopus 로고
    • A barrier model for current flow in lipid bilayer membranes
    • Hall, J.E., C.A. Mead, and G. Szabo. 1973. A barrier model for current flow in lipid bilayer membranes. J. Membr. Biol. 11:75-97.
    • (1973) J. Membr. Biol. , vol.11 , pp. 75-97
    • Hall, J.E.1    Mead, C.A.2    Szabo, G.3
  • 36
    • 0344402568 scopus 로고
    • Single anion-selective channels in basolateral membrane of a mammalian tight epithelium
    • Hanrahan, J.W., W.P. Alles, and S.A. Lewis. 1985. Single anion-selective channels in basolateral membrane of a mammalian tight epithelium. Proc. Natl. Acad. Sci. USA. 82:7791-7795.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7791-7795
    • Hanrahan, J.W.1    Alles, W.P.2    Lewis, S.A.3
  • 39
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin, A.L., and A.F. Huxley. 1952. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. (Lond.). 117:500-544.
    • (1952) J. Physiol. (Lond.) , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 40
    • 78651026696 scopus 로고
    • The effect of Na ions on the electrical activity of the giant axon of the squid
    • Hodgkin, A.L., and B. Katz. 1949. The effect of Na ions on the electrical activity of the giant axon of the squid. J. Physiol. (Lond.). 108:37-77.
    • (1949) J. Physiol. (Lond.) , vol.108 , pp. 37-77
    • Hodgkin, A.L.1    Katz, B.2
  • 41
    • 0016243216 scopus 로고
    • Determination of membrane potential in human and amphiuma red blood cells by means of a fluorescent probe
    • Hoffman, J.F., and P.C. Laris. 1974. Determination of membrane potential in human and amphiuma red blood cells by means of a fluorescent probe. J. Physiol. (Lond.). 239:519-552.
    • (1974) J. Physiol. (Lond.) , vol.239 , pp. 519-552
    • Hoffman, J.F.1    Laris, P.C.2
  • 42
    • 0018881647 scopus 로고
    • Electrical resistance of the red cell membrane and the relation between net anion transport and the anion exchange mechanism
    • Hoffman, J.F., J.H. Kaplan, T.J. Callahan, and J.C. Freedman. 1980. Electrical resistance of the red cell membrane and the relation between net anion transport and the anion exchange mechanism. Ann. NY Acad. Sci. 341:357-360.
    • (1980) Ann. NY Acad. Sci. , vol.341 , pp. 357-360
    • Hoffman, J.F.1    Kaplan, J.H.2    Callahan, T.J.3    Freedman, J.C.4
  • 43
    • 0015137073 scopus 로고
    • A quantitative estimate of the non-exchange-restricted chloride permeability of the human red cell
    • Abstr.
    • Hunter, M.J. 1971. A quantitative estimate of the non-exchange-restricted chloride permeability of the human red cell. J. Physiol. (Lond.). 218:49-50P. (Abstr.)
    • (1971) J. Physiol. (Lond.) , vol.218
    • Hunter, M.J.1
  • 44
    • 0017373958 scopus 로고
    • Human erythrocyte anion permeabilities measured under conditions of net charge transfer
    • Hunter, M.J. 1977. Human erythrocyte anion permeabilities measured under conditions of net charge transfer. J. Physiol. (Lond.). 268:35-49.
    • (1977) J. Physiol. (Lond.) , vol.268 , pp. 35-49
    • Hunter, M.J.1
  • 45
    • 0004023417 scopus 로고
    • Nonlinear properties of excitable membranes
    • Oxford University Press, Oxford
    • Jack, J.J.B., D. Noble, and R.W. Tsien. 1983. Nonlinear properties of excitable membranes. In Electric Current Flow in Excitable Cells. Oxford University Press, Oxford, pp. 225-234.
    • (1983) Electric Current Flow in Excitable Cells , pp. 225-234
    • Jack, J.J.B.1    Noble, D.2    Tsien, R.W.3
  • 46
    • 0008066915 scopus 로고
    • The role of carbonic anhydrase in certain ionic exchanges involving the erythrocyte
    • Jacobs, M.H., and D.R. Stewart. 1942. The role of carbonic anhydrase in certain ionic exchanges involving the erythrocyte. J. Gen. Physiol. 25:539-552.
    • (1942) J. Gen. Physiol. , vol.25 , pp. 539-552
    • Jacobs, M.H.1    Stewart, D.R.2
  • 47
    • 0024425163 scopus 로고
    • Kinetics of reversible DIDS inhibition of chloride self exchange in human erythrocytes
    • Janas, T., P.J. Bjerrum, J. Brahm, and J.O. Wieth. 1989. Kinetics of reversible DIDS inhibition of chloride self exchange in human erythrocytes. Am. J. Physiol. 257:C601-C606.
    • (1989) Am. J. Physiol. , vol.257
    • Janas, T.1    Bjerrum, P.J.2    Brahm, J.3    Wieth, J.O.4
  • 48
    • 0017185295 scopus 로고
    • Proton fluxes associated with erythrocyte membrane anion exchange
    • Jennings, M.L. 1976. Proton fluxes associated with erythrocyte membrane anion exchange. J. Membr. Biol. 28:187-205.
    • (1976) J. Membr. Biol. , vol.28 , pp. 187-205
    • Jennings, M.L.1
  • 49
    • 0020057001 scopus 로고
    • Stoichiometry of a half-turnover of band 3, the chloride transport protein of human erythrocytes
    • Jennings, M.L. 1982. Stoichiometry of a half-turnover of band 3, the chloride transport protein of human erythrocytes. J. Gen. Physiol. 79:169-185.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 169-185
    • Jennings, M.L.1
  • 50
    • 0024534816 scopus 로고
    • Structure and function of the red blood cell anion transport protein
    • Jennings, M.L. 1989. Structure and function of the red blood cell anion transport protein. Annu. Rev. Biophys. Biophys. Chem. 18: 397-430.
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 397-430
    • Jennings, M.L.1
  • 51
    • 15444359139 scopus 로고
    • Inorganic anion transport
    • P. Yeagle, editor. CRC Press, Boca Raton, FL
    • Jennings, M.L. 1992. Inorganic anion transport. In The Structure of Biological Membranes. P. Yeagle, editor. CRC Press, Boca Raton, FL. 781-832.
    • (1992) The Structure of Biological Membranes , pp. 781-832
    • Jennings, M.L.1
  • 52
    • 0028897503 scopus 로고
    • Rapid electrogenic sulfate-chloride exchange mediated by chemically modified band 3 in human erythrocytes
    • Jennings, M.L. 1995. Rapid electrogenic sulfate-chloride exchange mediated by chemically modified band 3 in human erythrocytes. J. Gen. Physiol. 105:21-47.
    • (1995) J. Gen. Physiol. , vol.105 , pp. 21-47
    • Jennings, M.L.1
  • 53
    • 0025245753 scopus 로고
    • Effects of membrane potential on electrically silent transport. Potential-independent translocation and asymmetric potential-dependent substrate binding to the red blood cell anion exchange protein
    • Jennings, M.L., R.K. Schulz, and M. Allen. 1990. Effects of membrane potential on electrically silent transport. Potential-independent translocation and asymmetric potential-dependent substrate binding to the red blood cell anion exchange protein. J. Gen. Physiol. 96:991-1012.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 991-1012
    • Jennings, M.L.1    Schulz, R.K.2    Allen, M.3
  • 54
    • 0026689374 scopus 로고
    • Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681
    • Jennings, M.L., and J.S. Smith. 1992. Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681. J. Biol. Chem. 267:13964-13971.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13964-13971
    • Jennings, M.L.1    Smith, J.S.2
  • 55
    • 0026760577 scopus 로고
    • A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment
    • Kang, D., K. Okubo, N. Hamasaki, N. Kuroda, and H. Shiraki. 1992. A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment. J. Biol. Chem, 267:19211-19217.
    • (1992) J. Biol. Chem , vol.267 , pp. 19211-19217
    • Kang, D.1    Okubo, K.2    Hamasaki, N.3    Kuroda, N.4    Shiraki, H.5
  • 56
    • 0020546158 scopus 로고
    • Band-3 protein mediated anion conductance of the red cell membrane. Slippage vs ionic diffusion
    • Kaplan, J.H., M. Pring, and H. Passow. 1983. Band-3 protein mediated anion conductance of the red cell membrane. Slippage vs ionic diffusion. FEBS Lett. 156:175-179.
    • (1983) FEBS Lett. , vol.156 , pp. 175-179
    • Kaplan, J.H.1    Pring, M.2    Passow, H.3
  • 58
    • 77957092777 scopus 로고
    • Erythrocyte anion exchange and the band 3 protein: Transport kinetics and molecular structure
    • Knauf, P.A. 1979. Erythrocyte anion exchange and the band 3 protein: transport kinetics and molecular structure. Curr. Top. Membr. Transp. 12:249-363.
    • (1979) Curr. Top. Membr. Transp. , vol.12 , pp. 249-363
    • Knauf, P.A.1
  • 59
    • 0017328329 scopus 로고
    • The relationship between anion exchange and net anion flow across the human red blood cell membrane
    • Knauf, P.A., G.F. Fuhrmann, S. Rothstein, and A. Rothstein. 1977. The relationship between anion exchange and net anion flow across the human red blood cell membrane. J. Gen. Physiol. 69: 363-386.
    • (1977) J. Gen. Physiol. , vol.69 , pp. 363-386
    • Knauf, P.A.1    Fuhrmann, G.F.2    Rothstein, S.3    Rothstein, A.4
  • 60
    • 0020687368 scopus 로고
    • Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism
    • Knauf, P.A., F.-Y. Law, and P.J. Marchant. 1983. Relationship of net chloride flow across the human erythrocyte membrane to the anion exchange mechanism. J. Gen. Physiol. 81:95-126.
    • (1983) J. Gen. Physiol. , vol.81 , pp. 95-126
    • Knauf, P.A.1    Law, F.-Y.2    Marchant, P.J.3
  • 61
    • 0022428478 scopus 로고
    • Primary structure and transmembrane orientation of the murine anion exchange protein
    • Kopito, R.R., and H.F. Lodish. 1985. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature (Lond.). 316:234-238.
    • (1985) Nature (Lond.) , vol.316 , pp. 234-238
    • Kopito, R.R.1    Lodish, H.F.2
  • 62
    • 14144251687 scopus 로고
    • Membrane potential and membrane resistance of red cells
    • M. Rorth and P. Astrup, editors. Academic Press, New York, NY
    • Lassen, U.V. 1972. Membrane potential and membrane resistance of red cells. In Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status. M. Rorth and P. Astrup, editors. Academic Press, New York, NY. 291-304.
    • (1972) Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status , pp. 291-304
    • Lassen, U.V.1
  • 63
    • 0015788893 scopus 로고
    • Ion transport through pores: A rate-theory analysis
    • Läuger, P. 1973. Ion transport through pores: a rate-theory analysis. Biochim. Biophys. Acta. 311:423-441.
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 423-441
    • Läuger, P.1
  • 64
    • 0014949706 scopus 로고
    • Kinetics of carrier-mediated ion transport across lipid bilayer membranes
    • Lauger, P., and G. Stark. 1970. Kinetics of carrier-mediated ion transport across lipid bilayer membranes. Biochim. Biophys. Acta. 211:458-466.
    • (1970) Biochim. Biophys. Acta , vol.211 , pp. 458-466
    • Lauger, P.1    Stark, G.2
  • 65
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion exchange protein (AE1)
    • Lux, S. E., K. M. John, R. Kopito, and H. F. Lodish. 1989. Cloning and characterization of band 3, the human erythrocyte anion exchange protein (AE1). Proc. Natl. Acad. Sci. USA. 86:9089-9093.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9089-9093
    • Lux, S.E.1    John, K.M.2    Kopito, R.3    Lodish, H.F.4
  • 66
    • 0018133516 scopus 로고
    • Erythrocyte membrane potentials determined by hydrogen ion distribution
    • Macey, R. I., J. S. Adorante, and F. W. Orme. 1978. Erythrocyte membrane potentials determined by hydrogen ion distribution. Biochim. Biophys. Acta. 512:284-295.
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 284-295
    • Macey, R.I.1    Adorante, J.S.2    Orme, F.W.3
  • 67
    • 0021490558 scopus 로고
    • Proton-sulfate cotransport: External proton activation of sulfate influx into human red blood cells
    • Milanick, M. A., and R. B. Gunn. 1984. Proton-sulfate cotransport: external proton activation of sulfate influx into human red blood cells. Am. J. Physiol. 247:C247-C259.
    • (1984) Am. J. Physiol. , vol.247
    • Milanick, M.A.1    Gunn, R.B.2
  • 68
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller, C., and M. M. White. 1984. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl. Acad. Sci. USA. 81:2772-2775.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 69
    • 0014575043 scopus 로고
    • Nonlinear electrical effects in lipid bilayer membranes. II. Integration of the generalized Nernst-Planck equations
    • Neumke, B., and P. Länger. 1969. Nonlinear electrical effects in lipid bilayer membranes. II. Integration of the generalized Nernst-Planck equations. Biophys. J. 9:1160-1170.
    • (1969) Biophys. J. , vol.9 , pp. 1160-1170
    • Neumke, B.1    Länger, P.2
  • 70
    • 0023137863 scopus 로고
    • Ionic channels in mouse astrocytes in culture
    • Nowak, L., P. Ascher, and Y. Berwald-Netter. 1987. Ionic channels in mouse astrocytes in culture. J. Neurosci. 7:101-109.
    • (1987) J. Neurosci. , vol.7 , pp. 101-109
    • Nowak, L.1    Ascher, P.2    Berwald-Netter, Y.3
  • 71
    • 0022615649 scopus 로고
    • Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane
    • Passow, H. 1986. Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane. Rev. Physiol. Biochem. Pharmacol. 103:61-203.
    • (1986) Rev. Physiol. Biochem. Pharmacol. , vol.103 , pp. 61-203
    • Passow, H.1
  • 72
    • 0026694987 scopus 로고
    • Exploration of the functional significance of the stilbene disulfonate binding site in mouse band 3 by site-directed mutagenesis
    • Passow, H., P.G. Wood, S. Lepke, H. Müller, and M. Sovak. 1992. Exploration of the functional significance of the stilbene disulfonate binding site in mouse band 3 by site-directed mutagenesis. Biophys. J. 62:98-100.
    • (1992) Biophys. J. , vol.62 , pp. 98-100
    • Passow, H.1    Wood, P.G.2    Lepke, S.3    Müller, H.4    Sovak, M.5
  • 73
    • 0027996879 scopus 로고
    • Molecular physiology of voltage-gated chloride channels
    • Pusch, M., and T.J. Jentsch. 1994. Molecular physiology of voltage-gated chloride channels. Physiol. Rev. 74:813-827.
    • (1994) Physiol. Rev. , vol.74 , pp. 813-827
    • Pusch, M.1    Jentsch, T.J.2
  • 74
    • 0029918160 scopus 로고    scopus 로고
    • Distribution of chloride permeabilities in normal human red cells
    • Rattos, J.E., R.M. Bookchin, and V.L. Lew. 1996. Distribution of chloride permeabilities in normal human red cells. J. Physiol. (Lond.). 491:773-777.
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 773-777
    • Rattos, J.E.1    Bookchin, R.M.2    Lew, V.L.3
  • 75
    • 0018715095 scopus 로고
    • Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer
    • Rao, A., P. Martin, R.A.F. Reithmeier, and L.C. Cantley. 1979. Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer. Biochemistry. 18:4505-4516.
    • (1979) Biochemistry , vol.18 , pp. 4505-4516
    • Rao, A.1    Martin, P.2    Reithmeier, R.A.F.3    Cantley, L.C.4
  • 76
    • 0027176416 scopus 로고
    • The erythrocyte anion transporter (band 3)
    • Reithmeier, R.A.F. 1993. The erythrocyte anion transporter (band 3). Curr. Opin. Struct. Biol. 3:515-523.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 515-523
    • Reithmeier, R.A.F.1
  • 77
    • 0024998501 scopus 로고
    • Double-barreled chloride channels of collecting duct basolateral membrane
    • Sansom, S.C., B.-Q. La, and S.L. Carosi. 1990. Double-barreled chloride channels of collecting duct basolateral membrane. Am. J. Physiol. 259:F46-F52.
    • (1990) Am. J. Physiol. , vol.259
    • Sansom, S.C.1    La, B.-Q.2    Carosi, S.L.3
  • 78
    • 34250386678 scopus 로고
    • Kinetic characteristics of the sulfate self-exchange in human red blood cells and red blood cell ghosts
    • Schnell, K.F., S. Gerhardt, and A. Schöppe-Fredenburg. 1977. Kinetic characteristics of the sulfate self-exchange in human red blood cells and red blood cell ghosts. J. Membr. Biol. 30:319-350.
    • (1977) J. Membr. Biol. , vol.30 , pp. 319-350
    • Schnell, K.F.1    Gerhardt, S.2    Schöppe-Fredenburg, A.3
  • 79
    • 0024459225 scopus 로고
    • Recording channel currents from human red cells
    • Schwarz, W., R. Grygorczyk, and D. Hof. 1989. Recording channel currents from human red cells. Methods Enzymol. 173: 112-121.
    • (1989) Methods Enzymol. , vol.173 , pp. 112-121
    • Schwarz, W.1    Grygorczyk, R.2    Hof, D.3
  • 80
    • 15444351876 scopus 로고
    • The rate theory of transport
    • Allen and Unwin, Boston, MA. Ch. 13
    • Silver, B.L. 1985. The rate theory of transport. In The Physical Chemistry of Membranes. Allen and Unwin, Boston, MA. Ch. 13 277-290.
    • (1985) The Physical Chemistry of Membranes , pp. 277-290
    • Silver, B.L.1
  • 81
    • 0010522476 scopus 로고
    • The transport of potassium through lipid bilayer membranes by the neutral carriers valinomycin and monactin. Experimental studies to a previously proposed model
    • Stark, G., and R. Benz. 1971. The transport of potassium through lipid bilayer membranes by the neutral carriers valinomycin and monactin. Experimental studies to a previously proposed model. J. Membr. Biol. 5:133-153.
    • (1971) J. Membr. Biol. , vol.5 , pp. 133-153
    • Stark, G.1    Benz, R.2
  • 82
    • 0024264841 scopus 로고
    • The complete amino acid sequence of the human erythrocyte membrane anion transport protein deduced from the cDNA sequence
    • Tanner, M.J.A., P.G. Martin, and S. High. 1988. The complete amino acid sequence of the human erythrocyte membrane anion transport protein deduced from the cDNA sequence. Biochem. J. 256:703-712.
    • (1988) Biochem. J. , vol.256 , pp. 703-712
    • Tanner, M.J.A.1    Martin, P.G.2    High, S.3
  • 83
    • 0026522116 scopus 로고
    • A chloride channel widely expressed in epithelial and non-epithelial cells
    • Thiemann, A., S. Gründer, M. Pusch, and T.J. Jentsch. 1992. A chloride channel widely expressed in epithelial and non-epithelial cells. Nature (Lond.). 356:57-60.
    • (1992) Nature (Lond.) , vol.356 , pp. 57-60
    • Thiemann, A.1    Gründer, S.2    Pusch, M.3    Jentsch, T.J.4
  • 84
    • 0027266988 scopus 로고
    • Two-dimensional structure of the membrane domain of human Band 3, the anion transport protein of the erythrocyte membrane
    • Wang, D.N., W. Kühlbrandt, V.E. Sarabia, and R.A.F. Reithmeier. 1993. Two-dimensional structure of the membrane domain of human Band 3, the anion transport protein of the erythrocyte membrane. EMBO (Eur. Mol. Biol Organ.) J. 12:2233-2239.
    • (1993) EMBO (Eur. Mol. Biol Organ.) J. , vol.12 , pp. 2233-2239
    • Wang, D.N.1    Kühlbrandt, W.2    Sarabia, V.E.3    Reithmeier, R.A.F.4
  • 85
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3
    • Wang, D.N., V.E. Sarabia, R.A.F. Reithmeier, and W. Kühlbrandt. 1994. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. EMBO (Eur. Mol. Biol. Organ.) J. 13:3230-3235.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.F.3    Kühlbrandt, W.4
  • 86
    • 0018801493 scopus 로고
    • A voltage-gated anion channel from the electric organ of Torpedo californica
    • White, M.M., and C. Miller. 1979. A voltage-gated anion channel from the electric organ of Torpedo californica. J. Biol. Chem. 254: 10161-10166.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10161-10166
    • White, M.M.1    Miller, C.2
  • 87
    • 0020038973 scopus 로고
    • Titration of transport and modifier sites in the red cell anion transport system
    • Wieth, J.O., and P.J. Bjerrum. 1982. Titration of transport and modifier sites in the red cell anion transport system. J. Gen. Physiol. 79:253-282.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 253-282
    • Wieth, J.O.1    Bjerrum, P.J.2
  • 88
    • 0020082387 scopus 로고
    • Irreversible inactivation of red cell chloride exchange with phenylglyoxal, an arginine-specific reagent
    • Wieth, J.O., P.J. Bjerrum, and C.L. Borders, Jr. 1982. Irreversible inactivation of red cell chloride exchange with phenylglyoxal, an arginine-specific reagent. J. Gen. Physiol. 79:283-312.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 283-312
    • Wieth, J.O.1    Bjerrum, P.J.2    Borders Jr., C.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.