메뉴 건너뛰기




Volumn 88, Issue 4, 2005, Pages 2681-2691

Evidence for a second binding/transport site for chloride in erythrocyte anion transporter AE1 modified at glutamate 681

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; ERYTHROCYTE BAND 3 PROTEIN; GLUTAMIC ACID; SULFATE;

EID: 22144435862     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.056812     Document Type: Article
Times cited : (28)

References (51)
  • 3
    • 0034663190 scopus 로고    scopus 로고
    • Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: Identification of primary and secondary phosphorylation sites
    • Brunati, A. M., L. Bordin, G. Clari, P. James, M. Quadroni, E. Baritono, L. A. Pinna, and A. Donella-Deana. 2000. Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites. Blood. 96:1550-1557.
    • (2000) Blood , vol.96 , pp. 1550-1557
    • Brunati, A.M.1    Bordin, L.2    Clari, G.3    James, P.4    Quadroni, M.5    Baritono, E.6    Pinna, L.A.7    Donella-Deana, A.8
  • 4
    • 0021685638 scopus 로고
    • Organic phosphates modulate anion self-exchange across the human erythrocyte membrane
    • Bursaux, E., M. Hilly, A. Bluze, and C. Poyart. 1984. Organic phosphates modulate anion self-exchange across the human erythrocyte membrane. Biochim. Biophys. Acta. 777:253-260.
    • (1984) Biochim. Biophys. Acta. , vol.777 , pp. 253-260
    • Bursaux, E.1    Hilly, M.2    Bluze, A.3    Poyart, C.4
  • 5
    • 0015962082 scopus 로고
    • Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation
    • Cabantchik, Z. I., and A. Rothstein. 1974. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. J. Membr. Biol. 15:207-226.
    • (1974) J. Membr. Biol. , vol.15 , pp. 207-226
    • Cabantchik, Z.I.1    Rothstein, A.2
  • 6
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromotography
    • Casey, J. R., and R. A. F. Reithmeier. 1991. Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromotography. J. Biol. Chem. 266:15726-15737.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 8
    • 0017287121 scopus 로고
    • Effects of halides and bicarbonate on chloride transport in human red blood cells
    • Dalmark, M. 1976. Effects of halides and bicarbonate on chloride transport in human red blood cells. J. Gen. Physiol. 67:223-234.
    • (1976) J. Gen. Physiol. , vol.67 , pp. 223-234
    • Dalmark, M.1
  • 9
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler, R., E. B. Campbell, M. Cadene, B. T. Chait, and R. MacKinnon. 2002. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature. 415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 10
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., E. B. Campbell, and R. MacKinnon. 2003. Gating the selectivity filter in ClC chloride channels. Science. 300:108-112.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 11
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., T. L. Steck, and D. F. H. Wallach. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 10:2606-2616.
    • (1971) Biochemistry , vol.10 , pp. 2606-2616
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 12
    • 0021686963 scopus 로고
    • Relative contributions of the slippage and tunneling mechanisms to anion net efflux from human erythrocytes
    • Fröhlich, O. 1984. Relative contributions of the slippage and tunneling mechanisms to anion net efflux from human erythrocytes. J. Gen. Physiol. 84:877-893.
    • (1984) J. Gen. Physiol. , vol.84 , pp. 877-893
    • Fröhlich, O.1
  • 13
    • 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
  • 14
    • 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. Liebson, 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    Liebson, C.2    Gunn, R.B.3
  • 15
    • 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
  • 16
    • 0018638065 scopus 로고
    • Asymmetry in the mechanism for anion exchange in human red blood cell membranes
    • Gunn, R., and O. Fröhlich. 1979. Asymmetry in the mechanism for anion exchange in human red blood cell membranes. J. Gen. Physiol. 74:351-374.
    • (1979) J. Gen. Physiol. , vol.74 , pp. 351-374
    • Gunn, R.1    Fröhlich, O.2
  • 18
    • 78651026696 scopus 로고
    • The effect of sodium ions on the electrical activity of the giant axon of the squid
    • Hodgkin, A. L., and B. Katz. 1949. The effect of sodium 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0017903097 scopus 로고
    • 2-independent pH equilibration in human red blood cells
    • 2-independent pH equilibration in human red blood cells. J. Membr. Biol. 40:365-391.
    • (1978) J. Membr. Biol. , vol.40 , pp. 365-391
    • Jennings, M.L.1
  • 23
    • 0001182903 scopus 로고
    • Apparent "recruitment" of sulfate transport sites by the Cl gradient across the human erythrocyte membrane
    • U. V. Lassen, H. H. Ussing, and J. O. Wieth, editors. Munksgaard, Copenhagen
    • Jennings, M. L. 1980. Apparent "recruitment" of sulfate transport sites by the Cl gradient across the human erythrocyte membrane. In Membrane Transport in Erythrocytes. U. V. Lassen, H. H. Ussing, and J. O. Wieth, editors. Munksgaard, Copenhagen. 450-463.
    • (1980) Membrane Transport in Erythrocytes , pp. 450-463
    • Jennings, M.L.1
  • 24
    • 0024949168 scopus 로고
    • Characteristics of the binding site for extracellular anions in human red blood cell band 3
    • Jennings, M. L. 1989. Characteristics of the binding site for extracellular anions in human red blood cell band 3. Ann. N. Y. Acad. Sci. 574:84-95.
    • (1989) Ann. N. Y. Acad. Sci. , vol.574 , pp. 84-95
    • Jennings, M.L.1
  • 25
    • 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
  • 26
    • 0030030319 scopus 로고    scopus 로고
    • Characterization of oxalate transport by the human erythrocyte band 3 protein
    • Jennings, M. L., and M. F. Adame. 1996. Characterization of oxalate transport by the human erythrocyte band 3 protein. J. Gen. Physiol. 107:145-159.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 145-159
    • Jennings, M.L.1    Adame, M.F.2
  • 27
    • 0021251488 scopus 로고
    • Peptides of human erythrocyte band 3 protein produced by extracellular papain cleavage
    • Jennings, M. L., M. Adams-Lackey, and G. H. Denney. 1984. Peptides of human erythrocyte band 3 protein produced by extracellular papain cleavage. J. Biol. Chem. 259:4652-4660.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4652-4660
    • Jennings, M.L.1    Adams-Lackey, M.2    Denney, G.H.3
  • 28
    • 0025245753 scopus 로고
    • Effects of membrane potential on electrically silent transport
    • Jennings, M. L., M. Allen, and R. K. Schulz. 1990. Effects of membrane potential on electrically silent transport. J. Gen. Physiol. 96:991-1012.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 991-1012
    • Jennings, M.L.1    Allen, M.2    Schulz, R.K.3
  • 29
    • 0023715210 scopus 로고
    • Modification of a carboxyl group that appears to cross the permeability barrier in the red blood cell anion transporter
    • Jennings, M. L., and S. Al-Rhaiyel. 1988. Modification of a carboxyl group that appears to cross the permeability barrier in the red blood cell anion transporter. J. Gen. Physiol. 92:161-178.
    • (1988) J. Gen. Physiol. , vol.92 , pp. 161-178
    • Jennings, M.L.1    Al-Rhaiyel, S.2
  • 30
    • 0023203804 scopus 로고
    • Chemical modification of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein
    • Jennings, M. L., and M. P. Anderson. 1987. Chemical modification of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein. J. Biol. Chem. 262:1691-1697.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1691-1697
    • Jennings, M.L.1    Anderson, M.P.2
  • 31
    • 0018746219 scopus 로고
    • Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano-dihydrostilbene-2,2′-disulfonate
    • Jennings, M. L., and H. Passow. 1979. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano-dihydrostilbene-2, 2′-disulfonate. Biochim. Biophys. Acta. 554:498-519.
    • (1979) Biochim. Biophys. Acta. , vol.554 , pp. 498-519
    • Jennings, M.L.1    Passow, H.2
  • 32
    • 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
  • 33
    • 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
  • 34
    • 0017328329 scopus 로고
    • The relationship between 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 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
  • 35
    • 0036678036 scopus 로고    scopus 로고
    • Substrate-dependent reversal of anion transport site orientation in the human red blood cell anion-exchange protein, AE1
    • Knauf, P. A., F.-Y. Law, T. Leung, A. U. Gehret, and M. L. Perez. 2002. Substrate-dependent reversal of anion transport site orientation in the human red blood cell anion-exchange protein, AE1. Proc. Natl. Acad. Sci. USA. 99:10861-10864.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 10861-10864
    • Knauf, P.A.1    Law, F.-Y.2    Leung, T.3    Gehret, A.U.4    Perez, M.L.5
  • 36
    • 0022452951 scopus 로고
    • Location of the chloride self-inhibitory site of the human erythrocyte anion exchange system
    • Knauf, P. A. and N. A. Mann. 1986. Location of the chloride self-inhibitory site of the human erythrocyte anion exchange system. Am. J. Physiol. 251:C1-C9.
    • (1986) Am. J. Physiol. , vol.251
    • Knauf, P.A.1    Mann, N.A.2
  • 37
    • 0018422046 scopus 로고
    • A comparison of the inhibitory potency of reversibly action inhibitors of anion transport on chloride and sulfate movements across the human red cell membrane
    • Ku, C.-P., M. L. Jennings, and H. Passow. 1979. A comparison of the inhibitory potency of reversibly action inhibitors of anion transport on chloride and sulfate movements across the human red 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
  • 38
    • 2342605185 scopus 로고    scopus 로고
    • The band 3 protein: Anion exchanger and anion-proton cotransporter
    • I. Bernhardt and J. C. Ellory, editors. Springer, Heidelberg
    • Lepke, S., J. Heberle, and H. Passow. 2003. The band 3 protein: anion exchanger and anion-proton cotransporter. In Red Cell Membrane Transport in Health and Disease. I. Bernhardt and J. C. Ellory, editors. Springer, Heidelberg, 221-252.
    • (2003) Red Cell Membrane Transport in Health and Disease , pp. 221-252
    • Lepke, S.1    Heberle, J.2    Passow, H.3
  • 40
    • 0020075082 scopus 로고
    • Proton-sulfate cotransport: Mechanism of hydrogen and sulfate addition to the chloride transporter of human red blood cells
    • Milanick, M. A., and R. B. Gunn. 1982. Proton-sulfate cotransport: mechanism of hydrogen 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 0030279607 scopus 로고    scopus 로고
    • Allosteric effects in stilbenedisulfonate binding to band 3 protein (AE1)
    • Salhany, J. M. 1996. Allosteric effects in stilbenedisulfonate binding to band 3 protein (AE1). Mol. Cell. Biol. 42:1065-1096.
    • (1996) Mol. Cell. Biol. , vol.42 , pp. 1065-1096
    • Salhany, J.M.1
  • 44
    • 2342448651 scopus 로고    scopus 로고
    • Slow transitions between two conformational states of band 3 (AE1) modulate divalent anion transport and DBDS binding to a second site on band 3 which is activated by lowering the pH (pK ∼5.0)
    • Salhany, J. M. 2004. Slow transitions between two conformational states of band 3 (AE1) modulate divalent anion transport and DBDS binding to a second site on band 3 which is activated by lowering the pH (pK ∼5.0). Blood Cells Mol. Dis. 32:372-378.
    • (2004) Blood Cells Mol. Dis. , vol.32 , pp. 372-378
    • Salhany, J.M.1
  • 45
    • 0026761313 scopus 로고
    • Transient-state kinetic evidence for intersubunit allosteric hysteresis during band 3 anion exchange
    • Salhany, J. M., and K. A. Cordes. 1992. Transient-state kinetic evidence for intersubunit allosteric hysteresis during band 3 anion exchange. Biochemistry. 31:7301-7310.
    • (1992) Biochemistry , vol.31 , pp. 7301-7310
    • Salhany, J.M.1    Cordes, K.A.2
  • 46
    • 0020674639 scopus 로고
    • Kinetics and mechanism of erycthrocyte anion exchange
    • Salhany, J. M., and P. B. Rauenbuehler. 1983. Kinetics and mechanism of erycthrocyte anion exchange. J. Biol. Chem. 258:245-249.
    • (1983) J. Biol. Chem. , vol.258 , pp. 245-249
    • Salhany, J.M.1    Rauenbuehler, P.B.2
  • 47
    • 0037452558 scopus 로고    scopus 로고
    • The carboxyl side chain of glutamate 681 interacts with a chloride binding modifier site that allosterically modulates the dimeric conformational state of band 3 (AE1). Implications for the mechanism of anion/proton cotransport
    • Salhany, J. M., R. L. Sloan, and K. S. Cordes. 2003. The carboxyl side chain of glutamate 681 interacts with a chloride binding modifier site that allosterically modulates the dimeric conformational state of band 3 (AE1). Implications for the mechanism of anion/proton cotransport. Biochemistry. 42:1589-1602.
    • (2003) Biochemistry. , vol.42 , pp. 1589-1602
    • Salhany, J.M.1    Sloan, R.L.2    Cordes, K.S.3
  • 48
    • 0015764378 scopus 로고
    • Preparation and properties of human erythrocyte ghosts
    • Schwoch, G., and H. Passow. 1973. Preparation and properties of human erythrocyte ghosts. Mol. Cell. Biochem. 2:197-218.
    • (1973) Mol. Cell. Biochem. , vol.2 , pp. 197-218
    • Schwoch, G.1    Passow, H.2
  • 50
    • 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. Kuhlbrandt. 1994. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger. Band 3. EMBO J. 13:3230-3235.
    • (1994) EMBO J. , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.F.3    Kuhlbrandt, W.4
  • 51
    • 0020347505 scopus 로고
    • Chloride-bicarbonate exchange in red blood cells: Physiology of transport and chemical modification of binding sites
    • Wieth, J. O., O. S. Anderson, J. Brahm, P. J. Bjerrum, and C. L. Borders, Jr. 1982. Chloride-bicarbonate exchange in red blood cells: physiology of transport and chemical modification of binding sites. Phil. Trans. R. Soc. Lond. B. 299:383-399.
    • (1982) Phil. Trans. R. Soc. Lond. B , vol.299 , pp. 383-399
    • Wieth, J.O.1    Anderson, O.S.2    Brahm, J.3    Bjerrum, P.J.4    Borders Jr., C.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.