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Volumn 107, Issue 2, 1996, Pages 293-306

Effects of external pH on binding of external sulfate, 4,4′-dinitro-stilbene-2,2′-disulfonate (DNDS), and chloride to the band 3 anion exchange protein

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DINITRO 2,2' STILBENEDISULFONIC ACID; ANTIPORTER;

EID: 0029968022     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.107.2.293     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0028265902 scopus 로고
    • Influence of stilbene disulfonates on the accessibility of the substrate-binding site for anions in the band 3 protein (AEB1)
    • Aranibar, X., C. Ostermeier, B. Legrum, H. Rüterjans, and H. Passow. 1994. Influence of stilbene disulfonates on the accessibility of the substrate-binding site for anions in the band 3 protein (AEB1). Renal Physiol. Biochem. 17:187-189.
    • (1994) Renal Physiol. Biochem. , vol.17 , pp. 187-189
    • Aranibar, X.1    Ostermeier, C.2    Legrum, B.3    Rüterjans, H.4    Passow, H.5
  • 2
    • 0026657905 scopus 로고
    • The human erythrocyte anion transport protein, band 3. Characterization of exofacial alkaline titratable groups involved in anion binding/translocation
    • Bjerrum, P. J. 1992. The human erythrocyte anion transport protein, band 3. Characterization of exofacial alkaline titratable groups involved in anion binding/translocation. J. Gen. Physiol. 100:301-339.
    • (1992) J. Gen. Physiol. , vol.100 , pp. 301-339
    • Bjerrum, P.J.1
  • 3
    • 0020063756 scopus 로고
    • The external anion binding site of the human erythrocyte anion transporter: DNDS binding and competition with chloride
    • Fröhlich, O. 1982. The external anion binding site of the human erythrocyte anion transporter: DNDS binding and competition with chloride. J. Membr. Biol. 65:111-125.
    • (1982) J. Membr. Biol. , vol.65 , pp. 111-125
    • Fröhlich, O.1
  • 4
    • 0022552582 scopus 로고
    • Erythrocyte anion transport: The kinetics of a single-site obligatory exchange system
    • Fröhlich, O., and R. B. Gunn. 1986. Erythrocyte anion transport: the kinetics of a single-site obligatory exchange system. Biochim. Biophys. Acta 864:169-194.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 169-194
    • Fröhlich, O.1    Gunn, R.B.2
  • 5
    • 0023140587 scopus 로고
    • Interactions of inhibitors on anion transporter of human erythrocyte
    • Cell Physiol.
    • Fröhlich, O., and R. B. Gunn. 1987. Interactions of inhibitors on anion transporter of human erythrocyte. Am. J. Physiol. (Cell Physiol.) 252:C153-C162.
    • (1987) Am. J. Physiol. , vol.252
    • Fröhlich, O.1    Gunn, R.B.2
  • 6
    • 0020660721 scopus 로고
    • Chloride net efflux from intact erythrocytes under slippage conditions. Evidence for a positive charge on the anion binding/transport site
    • Fröhlich, O., C. Leibson. and R. B. Gunn. 1983. Chloride net efflux from intact erythrocytes under slippage conditions. Evidence for a positive charge on the anion binding/transport site. 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
  • 8
    • 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
  • 9
    • 0024435961 scopus 로고
    • Methods and analysis of erythrocyte anion fluxes
    • S. Fleischer and B. Fleischer, editors. Academic Press, Inc., San Diego, California
    • Gunn, R. B., and O. Fröhlich. 1989. Methods and analysis of erythrocyte anion fluxes. in Methods in Enzymology, Vol. 173. S. Fleischer and B. Fleischer, editors. Academic Press, Inc., San Diego, California. 54-80.
    • (1989) Methods in Enzymology , vol.173 , pp. 54-80
    • Gunn, R.B.1    Fröhlich, O.2
  • 10
    • 0022371098 scopus 로고
    • Functions of extracellular lysine residues in the human erythrocyte anion transport protein
    • Jennings, M. L., R. Monaghan, S. M. Douglas, and J. S. Nicknish. 1985. Functions of extracellular lysine residues in the human erythrocyte anion transport protein. J. Gen. Physiol. 86:653-669.
    • (1985) J. Gen. Physiol. , vol.86 , pp. 653-669
    • Jennings, M.L.1    Monaghan, R.2    Douglas, S.M.3    Nicknish, J.S.4
  • 11
    • 0023918104 scopus 로고
    • Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein
    • Kawano, Y., K. Okubo, F. Tokunaga, T. Miyata, S. Iwanaga, and N. Hamasaki. 1988. Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein. J. Biol. Chem. 263:8232-8238.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8232-8238
    • Kawano, Y.1    Okubo, K.2    Tokunaga, F.3    Miyata, T.4    Iwanaga, S.5    Hamasaki, N.6
  • 12
    • 0024428274 scopus 로고
    • Functional asymmetry of the anion exchange protein, capnophorin: Effects on substrate and inhibitor binding
    • S. Fleischer and B. Fleischer, editors. Academic Press, New York
    • Knauf, P. A., and J. Brahm. 1989. Functional asymmetry of the anion exchange protein, capnophorin: effects on substrate and inhibitor binding. In Methods in Enzymology, Vol. 173. S. Fleischer and B. Fleischer, editors. Academic Press, New York. 432-453.
    • (1989) Methods in Enzymology , vol.173 , pp. 432-453
    • Knauf, P.A.1    Brahm, J.2
  • 13
    • 0007959905 scopus 로고
    • Mechanisms of substrate binding, inhibitor binding, and ion translocation in band 3 and band 3-related proteins
    • E. Bamberg and H. Passow, editors. Elsevier, Amsterdam
    • Knauf, P. A., D. Restrepo, S. J. Lin, N. M. Raha, L. J. Spinelli, F.-Y. Law, B. Cronise, R. B. Snyder, and L. Romanow. 1992. Mechanisms of substrate binding, inhibitor binding, and ion translocation in band 3 and band 3-related proteins. In Progress in Cell Research, Vol. 2. E. Bamberg and H. Passow, editors. Elsevier, Amsterdam. 35-44.
    • (1992) Progress in Cell Research , vol.2 , pp. 35-44
    • Knauf, P.A.1    Restrepo, D.2    Lin, S.J.3    Raha, N.M.4    Spinelli, L.J.5    Law, F.-Y.6    Cronise, B.7    Snyder, R.B.8    Romanow, L.9
  • 14
    • 0007911305 scopus 로고
    • DNDS (4,4′-dinitro-stilbene-2.2′-disulfonate) does not act as a purely competitive inhibitor of red blood cell band 3-mediated anion exchange
    • Abstr.
    • Knauf, P. A., E. A. Ries, L. A. Romanow, S. Bahar, and E. S. Szekeres. 1993a. DNDS (4,4′-dinitro-stilbene-2.2′-disulfonate) does not act as a purely competitive inhibitor of red blood cell band 3-mediated anion exchange. Biophys. J. 64:A307. (Abstr.)
    • (1993) Biophys. J. , vol.64
    • Knauf, P.A.1    Ries, E.A.2    Romanow, L.A.3    Bahar, S.4    Szekeres, E.S.5
  • 15
    • 0018217047 scopus 로고
    • Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitrophenyl)-2-ammoethylsulfonate (NAP-taurine) at the inside and outside of the membrane
    • Knauf, P. A., S. Ship, L. Breuer, L. McCulloch, and A. Rothstein. 1978. Asymmetry of the red cell anion exchange system. Different mechanisms of reversible inhibition by N-(4-azido-2-nitrophenyl)-2-ammoethylsulfonate (NAP-taurine) at the inside and outside of the membrane. J. Gen. Physiol 72:607-630.
    • (1978) J. Gen. Physiol , vol.72 , pp. 607-630
    • Knauf, P.A.1    Ship, S.2    Breuer, L.3    McCulloch, L.4    Rothstein, A.5
  • 16
    • 0028817440 scopus 로고
    • NIP- and NAP-taunne bind to external modifier site of AE1 (band 3). at which iodide inhibits anion exchange
    • Knauf, P. A., and L. J. Spinelli. 1995. NIP- and NAP-taunne bind to external modifier site of AE1 (band 3). at which iodide inhibits anion exchange. Am. J. Physiol. (Cell Physiol ) 269:CA10-C416.
    • (1995) Am. J. Physiol. (Cell Physiol ) , vol.269
    • Knauf, P.A.1    Spinelli, L.J.2
  • 17
    • 0024452506 scopus 로고
    • Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein
    • Knauf, P. A., L. J. Spinelli, and N. A. Mann. 1989. Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein. Am. J. Phisiol. (Cell Physiol.) 257:C277-C289.
    • (1989) Am. J. Phisiol. (Cell Physiol.) , vol.257
    • Knauf, P.A.1    Spinelli, L.J.2    Mann, N.A.3
  • 19
    • 0018422046 scopus 로고
    • A comparison of the inhibitory potency of reversibly acting inhibitors of anion transport on chloride and sulfate movements across the human red blood cell membrane
    • Ku, C. P., M. L. Jennings, and H. Passow. 1979. A comparison of the inhibitory potency of reversibly acting inhibitors of anion transport on chloride and sulfate movements across the human red blood cell membrane. Biochim. Biophys. Acta. 553:132-141.
    • (1979) Biochim. Biophys. Acta , vol.553 , pp. 132-141
    • Ku, C.P.1    Jennings, M.L.2    Passow, H.3
  • 20
    • 0028983352 scopus 로고
    • 35Cl Nuclear magnetic resonance line broadening shows that eosin-5-maleimide does not block the external anion access channel of band 3
    • 35Cl Nuclear magnetic resonance line broadening shows that eosin-5-maleimide does not block the external anion access channel of band 3. Biophys. J. 69:399-408.
    • (1995) Biophys. J. , vol.69 , pp. 399-408
    • Liu, D.1    Kennedy, S.D.2    Knauf, P.A.3
  • 22
    • 0029915373 scopus 로고    scopus 로고
    • Effects of external pH on substrate binding, and on the inward chloride translocation rate-constant of band 3
    • Liu, S. J., Y. Law, and P. A. Knauf. 1996. Effects of external pH on substrate binding, and on the inward chloride translocation rate-constant of band 3. J. Gen. Physiol. 107:271-291.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 271-291
    • Liu, S.J.1    Law, Y.2    Knauf, P.A.3
  • 23
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)
    • Lux, S. E., K. M. John, R. 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.R.3    Lodish, H.F.4
  • 24
    • 0020075082 scopus 로고
    • - and sulfate addition to the chloride transporter of human red blood cells
    • - and sulfate addition to the chloride transporter of human red blood cells. J. Gen. Physiol. 79:87-113.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 87-113
    • Milanick, M.A.1    Gunn, R.B.2
  • 25
    • 0022494334 scopus 로고
    • Proton inhibition of chloride exchange: Asynchrony of band 3 proton and anion transport sites?
    • Milanick, M. A., and R. B. Gunn. 1986. Proton inhibition of chloride exchange: asynchrony of band 3 proton and anion transport sites? Am. J Physiol. (Cell Physiol.)250:C955-C969.
    • (1986) Am. J Physiol. (Cell Physiol.) , vol.250
    • Milanick, M.A.1    Gunn, R.B.2
  • 26
    • 0028006541 scopus 로고
    • 2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule
    • 2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule. J. Biol. Chem. 269:1918-1926.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1918-1926
    • Okubo, K.1    Rang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 27
    • 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. 103:61-223.
    • (1986) Rev. Physiol. Biochem. Pharmacol. , vol.103 , pp. 61-223
    • Passow, H.1
  • 28
    • 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. Schoppe-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    Schoppe-Fredenburg, A.3
  • 29
    • 0017801444 scopus 로고
    • - transport site of human red blood cells by a kinetic analysis of the inhibitory effects of a chemical probe
    • - transport site of human red blood cells by a kinetic analysis of the inhibitory effects of a chemical probe. Biochem. Biophys. Acta. 508:357-363.
    • (1978) Biochem. Biophys. Acta , vol.508 , pp. 357-363
    • Shami, Y.1    Rothstein, A.2    Knauf, P.A.3
  • 30
    • 0020510110 scopus 로고
    • Cross-linking and chymotryptic digestion of the extracytoplasmic domain of the anion exchange channel in intact human erythrocytes
    • Staros, J. V., and B. P. Kakkad. 1983. Cross-linking and chymotryptic digestion of the extracytoplasmic domain of the anion exchange channel in intact human erythrocytes. J. Membr. Biol. 74:247-254.
    • (1983) J. Membr. Biol. , vol.74 , pp. 247-254
    • Staros, J.V.1    Kakkad, B.P.2
  • 31
    • 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. 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.2    High, S.3
  • 32
    • 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
  • 33
    • 0343879900 scopus 로고
    • Transport and modifier sites in capnophorin, the anion transport protein of the erythrocyte membrane
    • E. Quagliariello and F. Palmieri, editors. Elsevier Science Publishers B.V.
    • Wieth, J. O., and P. J. Bjerrum. 1983. Transport and modifier sites in capnophorin, the anion transport protein of the erythrocyte membrane. In Structure and Function of Membrane Proteins. E. Quagliariello and F. Palmieri, editors. Elsevier Science Publishers B.V. 95-106.
    • (1983) Structure and Function of Membrane Proteins , pp. 95-106
    • Wieth, J.O.1    Bjerrum, P.J.2
  • 34
    • 0000119277 scopus 로고
    • The anion exchange proteins: Homology and secondary structure
    • E. Bamberg and H. Passow, editors. Elsevier Science Publishers, Amsterdam
    • Wood, P. G. 1992. The anion exchange proteins: homology and secondary structure. In Progress in Cell Science, Vol 2. E. Bamberg and H. Passow, editors. Elsevier Science Publishers, Amsterdam. 325-352.
    • (1992) Progress in Cell Science , vol.2 , pp. 325-352
    • Wood, P.G.1
  • 35
    • 0026529671 scopus 로고
    • Role of Lys 558 and Lys 869 in substrate and inhibitor binding to the murine band 3 protein: A study of the effects of site-directed mutagenesis of the band 3 protein expressed in the oocytes of Xenopus laevis
    • Wood, P. G., H. Müller, M. Sovak, and H. Passow. 1992. Role of Lys 558 and Lys 869 in substrate and inhibitor binding to the murine band 3 protein: A study of the effects of site-directed mutagenesis of the band 3 protein expressed in the oocytes of Xenopus laevis. J. Membr. Biol. 127:139-148.
    • (1992) J. Membr. Biol. , vol.127 , pp. 139-148
    • Wood, P.G.1    Müller, H.2    Sovak, M.3    Passow, H.4


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