메뉴 건너뛰기




Volumn , Issue , 2005, Pages 119-176

Molecular biology of renal acid-base transporters

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33748059671     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (364)
  • 1
    • 0023140106 scopus 로고
    • Evidence that parallel Na+-H+ and antiporters transport NaCl in the proximal tubule
    • Baum M. Evidence that parallel Na+-H+ and antiporters transport NaCl in the proximal tubule. Am J Physiol 1987; 252: F338-F345.
    • (1987) Am J Physiol , vol.252 , pp. F338-F345
    • Baum, M.1
  • 2
    • 0028365512 scopus 로고
    • Mechanism of apical and basolateral Na(+)-independent Cl~/base exchange in the rabbit superficial proximal straight tubule
    • Kurtz I, Nagami G, Yanagawa N, Li L, Emmons C, Lee I. Mechanism of apical and basolateral Na(+)-independent Cl~/base exchange in the rabbit superficial proximal straight tubule. J Clin Invest 1994; 94:173-183.
    • (1994) J Clin Invest , vol.94 , pp. 173-183
    • Kurtz, I.1    Nagami, G.2    Yanagawa, N.3    Li, L.4    Emmons, C.5    Lee, I.6
  • 3
    • 0022268406 scopus 로고
    • An early soda water ocean
    • Kempe S, Degens ET. An early soda water ocean? Chem Geol 1985; 53: 95-104.
    • (1985) Chem Geol , vol.53 , pp. 95-104
    • Kempe, S.1    Degens, E.T.2
  • 4
    • 0031034881 scopus 로고    scopus 로고
    • The reason for as well as the consequence of the Cambrian explosion in animal evolution
    • Ohno S. The reason for as well as the consequence of the Cambrian explosion in animal evolution. J Mol Evol 1997; 44:S23-S27.
    • (1997) J Mol Evol , vol.44 , pp. S23-S27
    • Ohno, S.1
  • 6
    • 0033823229 scopus 로고    scopus 로고
    • Prokaryotic carbonic anhydrases
    • Smith KS, Ferry JG. Prokaryotic carbonic anhydrases. FEMS Microbio Rev 2000; 24:335-366.
    • (2000) FEMS Microbio Rev , vol.24 , pp. 335-366
    • Smith, K.S.1    Ferry, J.G.2
  • 7
    • 0031452168 scopus 로고    scopus 로고
    • Structure, function and regulation of the vacuolar (H+)-ATPase
    • Stevens TH, Forgac M. Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 1997; 13:779-808.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 779-808
    • Stevens, T.H.1    Forgac, M.2
  • 8
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague MJ, Urbe S, Aniento F, Gruenberg. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J Biol Chem 1994; 269: 21-24.
    • (1994) J Biol Chem , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg4
  • 9
    • 0033983475 scopus 로고    scopus 로고
    • Luminal acidification of diverse organelles by V-ATPase in animal cells
    • Futai M, Oka T, Sun-Wada G, Moriyama Y, Kanazawa H, Wada Y. Luminal acidification of diverse organelles by V-ATPase in animal cells. J Exp Biol 2000; 203:107-116.
    • (2000) J Exp Biol , vol.203 , pp. 107-116
    • Futai, M.1    Oka, T.2    Sun-Wada, G.3    Moriyama, Y.4    Kanazawa, H.5    Wada, Y.6
  • 10
    • 0027422246 scopus 로고
    • Relative roles of Na+/H+ exchange and vacuolar-type H+ ATPases in regulating cytoplasmic pH and function in murine peritoneal macrophages
    • Swallow CJ, Grinstein S, Sudsbury RA, Rotstein OD. Relative roles of Na+/H+ exchange and vacuolar-type H+ ATPases in regulating cytoplasmic pH and function in murine peritoneal macrophages. J Cell Physiol 1993; 157:453-460.
    • (1993) J Cell Physiol , vol.157 , pp. 453-460
    • Swallow, C.J.1    Grinstein, S.2    Sudsbury, R.A.3    Rotstein, O.D.4
  • 11
    • 0025773968 scopus 로고
    • A vacuolar-type protein pump energizes K/H antiport in an animal plasma membrane
    • Wieczorek H, Putzenlechner M, Zeiske W, Klein U. A vacuolar-type protein pump energizes K/H antiport in an animal plasma membrane. J Biol Chem 1991; 266:15,340-15,347.
    • (1991) J Biol Chem , vol.266 , pp. 15340-15347
    • Wieczorek, H.1    Putzenlechner, M.2    Zeiske, W.3    Klein, U.4
  • 12
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar protein pump
    • Blair HC, Teitelbaum SL, Ghiselli R, Gluck S. Osteoclastic bone resorption by a polarized vacuolar protein pump. Science 1989; 245:855-857.
    • (1989) Science , vol.245 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 14
    • 0020059738 scopus 로고
    • An ATP-driven proton pump in brush border membranes from rat renal cortex
    • Kinne-Safran E, Beauwens R, Kinne R. An ATP-driven proton pump in brush border membranes from rat renal cortex. J Memb Biol 1982; 64:67-76.
    • (1982) J Memb Biol , vol.64 , pp. 67-76
    • Kinne-Safran, E.1    Beauwens, R.2    Kinne, R.3
  • 15
    • 0024240241 scopus 로고
    • Localization of a proton pumping ATPase in rat kidney
    • Brown D, Hirsch S, Gluck S. Localization of a proton pumping ATPase in rat kidney. J Clin Invest 1988; 82:2114-2126.
    • (1988) J Clin Invest , vol.82 , pp. 2114-2126
    • Brown, D.1    Hirsch, S.2    Gluck, S.3
  • 16
    • 0023575996 scopus 로고
    • Role of the Na+/H+ antiporter in rat proximal tubule bicarbonate absorption
    • Preisig PA, Ives HE, Cragoe EJ Jr, Alpern RJ, Rector FC Jr. Role of the Na+/H+ antiporter in rat proximal tubule bicarbonate absorption. J Clin Invest 1987; 80:970-978.
    • (1987) J Clin Invest , vol.80 , pp. 970-978
    • Preisig, P.A.1    Ives, H.E.2    Cragoe, E.J.3    Alpern, R.J.4    Rector, F.C.5
  • 17
    • 0023856320 scopus 로고
    • An H+-ATPase in opposite membranes domains in a kidney epithelial cell subpopulations
    • Brown D, Hirsch S, Gluck S. An H+-ATPase in opposite membranes domains in a kidney epithelial cell subpopulations. Nature 1988; 331:622-624.
    • (1988) Nature , vol.331 , pp. 622-624
    • Brown, D.1    Hirsch, S.2    Gluck, S.3
  • 18
    • 1042286852 scopus 로고
    • Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase
    • Alper SL, Natale J, Gluck S, Lodish HF, Brown D. Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase. Proc Natl Acad Sci USA 1989; 86:5429-5433.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5429-5433
    • Alper, S.L.1    Natale, J.2    Gluck, S.3    Lodish, H.F.4    Brown, D.5
  • 19
    • 0025070282 scopus 로고
    • Regulation of intracellular pH in the rabbit cortical collecting tubule
    • Weiner ID, Hamm LL. Regulation of intracellular pH in the rabbit cortical collecting tubule. J Clin Invest 1990; 85:274-281.
    • (1990) J Clin Invest , vol.85 , pp. 274-281
    • Weiner, I.D.1    Hamm, L.L.2
  • 20
    • 0028011904 scopus 로고
    • Functional characterization of three intercalated cell subtypes in the rabbit collecting duct
    • Emmons C, Kurtz I. Functional characterization of three intercalated cell subtypes in the rabbit collecting duct. J Clin Invest 1994; 93:417-423.
    • (1994) J Clin Invest , vol.93 , pp. 417-423
    • Emmons, C.1    Kurtz, I.2
  • 21
    • 0022399724 scopus 로고
    • Monoclonal antibody to Na-K-ATPase: Immunolocalization along nephron segments
    • Kashgarian M, Biemesderfer D, Caplan M, Forbush B. Monoclonal antibody to Na-K-ATPase: immunolocalization along nephron segments. Kidney Int 1985; 28:899-913.
    • (1985) Kidney Int , vol.28 , pp. 899-913
    • Kashgarian, M.1    Biemesderfer, D.2    Caplan, M.3    Forbush, B.4
  • 22
    • 0023236527 scopus 로고
    • Electrophysiologic identification of principal and intercalated cells in the rabbit outer medullary collecting duct
    • Koeppen BM. Electrophysiologic identification of principal and intercalated cells in the rabbit outer medullary collecting duct. Pflügers Arch 1987; 409:138-141.
    • (1987) Pflügers Arch , vol.409 , pp. 138-141
    • Koeppen, B.M.1
  • 24
    • 0031445914 scopus 로고    scopus 로고
    • Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis
    • Boekema EJ, Ubbink-Kok T, Lolkema JS, Brisson A, Konings WN. Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis. Proc Natl Acad Sci USA 1997; 94: 14, 291-14,293.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14291-14293
    • Boekema, E.J.1    Ubbink-Kok, T.2    Lolkema, J.S.3    Brisson, A.4    Konings, W.N.5
  • 25
    • 2642707545 scopus 로고    scopus 로고
    • ATP synthase's second stalk comes into focus
    • Wilkens S, Capaldi RA. ATP synthase's second stalk comes into focus. Nature 1998; 393:29.
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 26
    • 0025907484 scopus 로고
    • Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump
    • Perin MS, Fried VA, Stone DK, Xie XS, Sudhof TC. Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump. J Biol Chem 1991; 266:3877-3881.
    • (1991) J Biol Chem , vol.266 , pp. 3877-3881
    • Perin, M.S.1    Fried, V.A.2    Stone, D.K.3    Xie, X.S.4    Sudhof, T.C.5
  • 27
    • 0032549629 scopus 로고    scopus 로고
    • Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase
    • Leng XH, Manolson MF, Forgac M. Function of the COOH-terminal domain of Vph1p in activity and assembly of the yeast V-ATPase. J Biol Chem 1998; 273:6717-6723.
    • (1998) J Biol Chem , vol.273 , pp. 6717-6723
    • Leng, X.H.1    Manolson, M.F.2    Forgac, M.3
  • 28
    • 0027970177 scopus 로고
    • A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit
    • Vik SB, Antonio BJ. A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit. J Biol Chem 1994; 269:30,364-30,369.
    • (1994) J Biol Chem , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 29
    • 0027978351 scopus 로고
    • Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase
    • Zhang J, Feng Y, Forgac M. Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. J Biol Chem 1994; 269:23,518-23,523.
    • (1994) J Biol Chem , vol.269 , pp. 23518-23523
    • Zhang, J.1    Feng, Y.2    Forgac, M.3
  • 30
    • 0028989609 scopus 로고
    • The F0 complex of the Escherichia coli ATP synthase. Investigation by electron spectroscopic imaging and immunoelectron microscopy
    • Birkenhager R, Hoppert M, Deckers-Hebestreit G, Mayer F, Altendorf K. The F0 complex of the Escherichia coli ATP synthase. Investigation by electron spectroscopic imaging and immunoelectron microscopy. Eur J Biochem 1995; 230:58-67.
    • (1995) Eur J Biochem , vol.230 , pp. 58-67
    • Birkenhager, R.1    Hoppert, M.2    Deckers-Hebestreit, G.3    Mayer, F.4    Altendorf, K.5
  • 32
    • 0030898875 scopus 로고    scopus 로고
    • Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: Glimpses of interacting parts in a dynamic molecular machine
    • Fillingame RH. Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine. J Exp Biol 1997; 200:217-224.
    • (1997) J Exp Biol , vol.200 , pp. 217-224
    • Fillingame, R.H.1
  • 33
    • 0029019213 scopus 로고
    • Inhibition and labeling of the coated vesicle V-ATPase by 2-azido-[32P]ATP
    • Zhang J, Vasilyeva E, Feng Y, Forgac M. Inhibition and labeling of the coated vesicle V-ATPase by 2-azido-[32P]ATP. J Biol Chem 1995; 270:15,494-15,500.
    • (1995) J Biol Chem , vol.270 , pp. 15494-15500
    • Zhang, J.1    Vasilyeva, E.2    Feng, Y.3    Forgac, M.4
  • 34
    • 0029782419 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase
    • Liu J, Kane PM. Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase. Biochemistry 1996; 35:10,938-10,948.
    • (1996) Biochemistry , vol.35 , pp. 10938-10948
    • Liu, J.1    Kane, P.M.2
  • 35
    • 0028319319 scopus 로고
    • Inhibition of vacuolar H(+)-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A
    • Feng Y, Forgac M. Inhibition of vacuolar H(+)-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A. J Biol Chem 1994; 269:13,224-13,230.
    • (1994) J Biol Chem , vol.269 , pp. 13224-13230
    • Feng, Y.1    Forgac, M.2
  • 36
    • 0030028171 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the yeast V-ATPase B subunit (Vma2p)
    • Liu Q, Kane PM, Newman PR, Forgac M. Site-directed mutagenesis of the yeast V-ATPase B subunit (Vma2p). J Biol Chem 1996; 271:2018-2022.
    • (1996) J Biol Chem , vol.271 , pp. 2018-2022
    • Liu, Q.1    Kane, P.M.2    Newman, P.R.3    Forgac, M.4
  • 37
    • 0026554164 scopus 로고
    • Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells
    • Nelson RD, Guo XL, Masood K, Brown D, Kalkbrenner M, Gluck S. Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells. Proc Natl Acad Sci USA 1992; 89:3541-3545.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3541-3545
    • Nelson, R.D.1    Guo, X.L.2    Masood, K.3    Brown, D.4    Kalkbrenner, M.5    Gluck, S.6
  • 38
    • 0027317398 scopus 로고
    • VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae
    • Ho MN, Hirata R, Umemoto N, Ohya Y, Takatsuki A, Stevens TH, Anraku Y. VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae. J Biol Chem 1993; 268:18,286-18,292.
    • (1993) J Biol Chem , vol.268 , pp. 18286-18292
    • Ho, M.N.1    Hirata, R.2    Umemoto, N.3    Ohya, Y.4    Takatsuki, A.5    Stevens, T.H.6    Anraku, Y.7
  • 39
    • 0027991080 scopus 로고
    • Enzymatic and functional evidence for adaptation of the vacuolar H(+)-ATPase in proximal tubule apical membranes from rats with chronic metabolic acidosis
    • Chambrey R, Paillard M, Podevin RA. Enzymatic and functional evidence for adaptation of the vacuolar H(+)-ATPase in proximal tubule apical membranes from rats with chronic metabolic acidosis. J Biol Chem 1994; 269:3243-3250.
    • (1994) J Biol Chem , vol.269 , pp. 3243-3250
    • Chambrey, R.1    Paillard, M.2    Podevin, R.A.3
  • 40
    • 0030044062 scopus 로고    scopus 로고
    • Adaptation of rabbit cortical collecting duct HCO^ transport to metabolic acidosis in vitro
    • Tsuruoka S, Schwartz GJ. Adaptation of rabbit cortical collecting duct HCO^ transport to metabolic acidosis in vitro. J Clin Invest 1996; 97:1076-1084.
    • (1996) J Clin Invest , vol.97 , pp. 1076-1084
    • Tsuruoka, S.1    Schwartz, G.J.2
  • 41
    • 0025738533 scopus 로고
    • Expression and distribution of renal vacuolar proton-translocating ATPase in response to chronic acid and alkali loads in the rat
    • Bastani B, Purcell H, Hemken P, Trigg D, Gluck S. Expression and distribution of renal vacuolar proton-translocating ATPase in response to chronic acid and alkali loads in the rat. J Clin Invest 1991; 88:126-136.
    • (1991) J Clin Invest , vol.88 , pp. 126-136
    • Bastani, B.1    Purcell, H.2    Hemken, P.3    Trigg, D.4    Gluck, S.5
  • 42
    • 0031047916 scopus 로고    scopus 로고
    • Regulation of AE1 anion exchanger and H+-ATPase in rat cortex by acute metabolic acidosis and alkalosis
    • Sabolic I, Brown D, Gluck SL, Alper SL. Regulation of AE1 anion exchanger and H+-ATPase in rat cortex by acute metabolic acidosis and alkalosis. Kidney Int 1997; 51:125-137.
    • (1997) Kidney Int , vol.51 , pp. 125-137
    • Sabolic, I.1    Brown, D.2    Gluck, S.L.3    Alper, S.L.4
  • 43
    • 0026781858 scopus 로고
    • A novel mechanism for regulation of vacuolar acidification
    • Feng Y, Forgac M. A novel mechanism for regulation of vacuolar acidification. J Biol Chem 1992; 267:19,769-19,772.
    • (1992) J Biol Chem , vol.267 , pp. 19769-19772
    • Feng, Y.1    Forgac, M.2
  • 44
    • 0028906608 scopus 로고
    • The vacuolar ATPase: Sulfite stabilization and the mechanism of nitrate inactivation
    • Dschida WJ, Bowman BJ. The vacuolar ATPase: sulfite stabilization and the mechanism of nitrate inactivation. J Biol Chem 1995; 270:1557-1563.
    • (1995) J Biol Chem , vol.270 , pp. 1557-1563
    • Dschida, W.J.1    Bowman, B.J.2
  • 45
    • 0030834977 scopus 로고    scopus 로고
    • Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo
    • Oluwatosin YE, Kane PM. Mutations in the CYS4 gene provide evidence for regulation of the yeast vacuolar H+-ATPase by oxidation and reduction in vivo. J Biol Chem 1997; 272:28,149-28,157.
    • (1997) J Biol Chem , vol.272 , pp. 28149-28157
    • Oluwatosin, Y.E.1    Kane, P.M.2
  • 46
    • 0025719132 scopus 로고
    • Role of lipid peroxidation on renal dysfunction associated with glutathione depletion: Effects of vitamin E
    • Torres AM, Ochoa JE, Elias MM. Role of lipid peroxidation on renal dysfunction associated with glutathione depletion: effects of vitamin E. Toxicology 1991; 70:163-172.
    • (1991) Toxicology , vol.70 , pp. 163-172
    • Torres, A.M.1    Ochoa, J.E.2    Elias, M.M.3
  • 47
    • 0034629251 scopus 로고    scopus 로고
    • Regulation of V-ATPases by reversible disassembly
    • Kane PM. Regulation of V-ATPases by reversible disassembly. FEBS Lett 2000; 469:137-141.
    • (2000) FEBS Lett , vol.469 , pp. 137-141
    • Kane, P.M.1
  • 48
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner JP, Dow JA, Earley FG, Klein U, Jager D, Wieczorek H. Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J Biol Chem 1995; 270:5649-5653.
    • (1995) J Biol Chem , vol.270 , pp. 5649-5653
    • Sumner, J.P.1    Dow, J.A.2    Earley, F.G.3    Klein, U.4    Jager, D.5    Wieczorek, H.6
  • 49
    • 0026612693 scopus 로고
    • Characterization of the Vo domain of the coated vesicle H+-ATPase
    • Zhang J, Myers M, Forgac M. Characterization of the Vo domain of the coated vesicle H+-ATPase. J Biol Chem 1992; 267:9773-9778.
    • (1992) J Biol Chem , vol.267 , pp. 9773-9778
    • Zhang, J.1    Myers, M.2    Forgac, M.3
  • 50
    • 0027184120 scopus 로고
    • Assembly of the peripheral domain of the bovine vascuolar H-ATPase
    • Myers M, Forgac M. Assembly of the peripheral domain of the bovine vascuolar H-ATPase. J Cell Physiol 1993; 156:35-12.
    • (1993) J Cell Physiol , vol.156 , pp. 35-12
    • Myers, M.1    Forgac, M.2
  • 51
    • 0032508554 scopus 로고    scopus 로고
    • Interaction of the clathrin-coated vesicle V-ATPase with ADP and sodium azide
    • Vasilyeva E, Forgac M. Interaction of the clathrin-coated vesicle V-ATPase with ADP and sodium azide. J Biol Chem 1998; 273:23,823-23,829.
    • (1998) J Biol Chem , vol.273 , pp. 23823-23829
    • Vasilyeva, E.1    Forgac, M.2
  • 52
    • 0032407699 scopus 로고    scopus 로고
    • Structure, function and regulation of the vacuolar (H+)-ATPases
    • Forgac M. Structure, function and regulation of the vacuolar (H+)-ATPases. FEBS Lett 1998; 440:258-326.
    • (1998) FEBS Lett , vol.440 , pp. 258-326
    • Forgac, M.1
  • 53
    • 0039785861 scopus 로고    scopus 로고
    • Purification and reconstitution of the vacuolar H+-ATPases from lemon fruits and epicotyls
    • Muller ML, Irkens-Kiesecker U, Kramer D, Taiz L. Purification and reconstitution of the vacuolar H+-ATPases from lemon fruits and epicotyls. J Biol Chem 1997; 272:12,762-12,770.
    • (1997) J Biol Chem , vol.272 , pp. 12762-12770
    • Muller, M.L.1    Irkens-Kiesecker, U.2    Kramer, D.3    Taiz, L.4
  • 54
    • 0026630120 scopus 로고
    • Identification and partial purification of a cytosolic activator of vacuolar H+-ATPase from mammalian kidney
    • Zhang K, Wang ZQ, Gluck S. Identification and partial purification of a cytosolic activator of vacuolar H+-ATPase from mammalian kidney. J Biol Chem 1992; 267:9701-9705.
    • (1992) J Biol Chem , vol.267 , pp. 9701-9705
    • Zhang, K.1    Wang, Z.Q.2    Gluck, S.3
  • 55
    • 0027424405 scopus 로고
    • Isolation of a protein activator of the clathrin-coated vesicle proton pump
    • Xie XS, Crider BP, Stone DK. Isolation of a protein activator of the clathrin-coated vesicle proton pump. J Biol Chem 1993; 268:25,063-25,067.
    • (1993) J Biol Chem , vol.268 , pp. 25063-25067
    • Xie, X.S.1    Crider, B.P.2    Stone, D.K.3
  • 56
    • 0026720014 scopus 로고
    • A cytosolic inhibitor of vacuolar H+-ATPase from mammalian kidney
    • Zhang K, Wang ZQ, Gluck S. A cytosolic inhibitor of vacuolar H+-ATPase from mammalian kidney. J Biol Chem 1992; 267:14,539-14,542.
    • (1992) J Biol Chem , vol.267 , pp. 14539-14542
    • Zhang, K.1    Wang, Z.Q.2    Gluck, S.3
  • 57
    • 0022412843 scopus 로고
    • Plasticity of functional epithelial polarity
    • Schwartz GJ, Barasch J, Al-Awqati Q. Plasticity of functional epithelial polarity. Nature 1985; 318:368-371.
    • (1985) Nature , vol.318 , pp. 368-371
    • Schwartz, G.J.1    Barasch, J.2    Al-Awqati, Q.3
  • 58
    • 0028350154 scopus 로고
    • An induced extracellular matrix protein reverses the polarity of band 3 in intercalated cells
    • van Adelsberg J, Edwards JC, Takito J, Kiss B, Al-Awqati Q. An induced extracellular matrix protein reverses the polarity of band 3 in intercalated cells. Cell 1994; 76:1053-1061.
    • (1994) Cell , vol.76 , pp. 1053-1061
    • van Adelsberg, J.1    Edwards, J.C.2    Takito, J.3    Kiss, B.4    Al-Awqati, Q.5
  • 59
    • 0029852842 scopus 로고    scopus 로고
    • Hensin, a new collecting duct protein involved in the in vitro plasticity of intercalated cell polarity
    • Takito J, Hikita C, Al-Awqati Q. Hensin, a new collecting duct protein involved in the in vitro plasticity of intercalated cell polarity. J Clin Invest 1996; 98:2324-2331.
    • (1996) J Clin Invest , vol.98 , pp. 2324-2331
    • Takito, J.1    Hikita, C.2    Al-Awqati, Q.3
  • 60
    • 0033580991 scopus 로고    scopus 로고
    • Only multimeric hensin located in the extracellular matrix can induce apical endocytosis and reverse the polarity of intercalated cells
    • Hikita C, Takito J, Vijayakumar S, Al-Awqati Q. Only multimeric hensin located in the extracellular matrix can induce apical endocytosis and reverse the polarity of intercalated cells. J Biol Chem 1999; 274:17,671-17,676.
    • (1999) J Biol Chem , vol.274 , pp. 17671-17676
    • Hikita, C.1    Takito, J.2    Vijayakumar, S.3    Al-Awqati, Q.4
  • 61
    • 0033535322 scopus 로고    scopus 로고
    • Hensin remodels the apical cytoskeleton and induces columnarization of intercalated epithelial cells: Processes that resemble terminal differentiation
    • Vijayakumar S, Takito J, Hikita C, Al-Awqati Q. Hensin remodels the apical cytoskeleton and induces columnarization of intercalated epithelial cells: processes that resemble terminal differentiation. J Cell Biol 1999; 144:1057-1067.
    • (1999) J Cell Biol , vol.144 , pp. 1057-1067
    • Vijayakumar, S.1    Takito, J.2    Hikita, C.3    Al-Awqati, Q.4
  • 62
    • 0027336797 scopus 로고
    • The apical Cl/HCO3 exchanger of beta-intercalated cells
    • van Adelsberg J, Edwards JC, Al-Alwati Q. The apical Cl/HCO3 exchanger of beta-intercalated cells. J Biol Chem 1993; 268:11,283-11,289.
    • (1993) J Biol Chem , vol.268 , pp. 11283-11289
    • van Adelsberg, J.1    Edwards, J.C.2    Al-Alwati, Q.3
  • 64
    • 0024541542 scopus 로고
    • Membrane recycling and epithelial cell function
    • Brown D. Membrane recycling and epithelial cell function. Am J Physiol 1989; 256:F1-F12.
    • (1989) Am J Physiol , vol.256 , pp. F1-F12
    • Brown, D.1
  • 65
    • 0027748886 scopus 로고
    • Endosomal pathways for water channel and proton pump recylcing in kidney epithelial cells
    • Brown D, Sabolic I. Endosomal pathways for water channel and proton pump recylcing in kidney epithelial cells. J Cell Sci 1993; 17(suppl):49-59.
    • (1993) J Cell Sci , vol.17 , pp. 49-59
    • Brown, D.1    Sabolic, I.2
  • 66
    • 0033981348 scopus 로고    scopus 로고
    • H+-V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: Vesicle recycling and transcytotic pathways
    • Brown D, Breton S. H+-V-ATPase-dependent luminal acidification in the kidney collecting duct and the epididymis/vas deferens: vesicle recycling and transcytotic pathways. J Exp Biol 2000; 203:137-145.
    • (2000) J Exp Biol , vol.203 , pp. 137-145
    • Brown, D.1    Breton, S.2
  • 67
    • 0026905017 scopus 로고
    • Absence of H(+)-ATPase in cortical collecting tubules of a patient with Sjogren's syndrome and distal renal tubular acidosis
    • Cohen EP, Bastani B, Cohen MR, Kolner S, Hemken P, Gluck SL. Absence of H(+)-ATPase in cortical collecting tubules of a patient with Sjogren's syndrome and distal renal tubular acidosis. J Am Soc Nephrol 1992; 3:264-271.
    • (1992) J Am Soc Nephrol , vol.3 , pp. 264-271
    • Cohen, E.P.1    Bastani, B.2    Cohen, M.R.3    Kolner, S.4    Hemken, P.5    Gluck, S.L.6
  • 68
    • 0027986814 scopus 로고
    • Renal tubular acidosis with antibody directed to renal collecting duct cells
    • Konoshi K, Hayashi M, Saruta T. Renal tubular acidosis with antibody directed to renal collecting duct cells. N Eng J Med 1994; 331:1494-1593.
    • (1994) N Eng J Med , vol.331 , pp. 1494-1593
    • Konoshi, K.1    Hayashi, M.2    Saruta, T.3
  • 69
    • 0030881937 scopus 로고    scopus 로고
    • Preservation of intercalated cell H(+)-ATPase in two patients with lupus nephritis and hyperkalemic distal renal tubular acidosis
    • Bastani B, Underhill D, Chu N, Nelson RD, Haragsim L, Gluck S. Preservation of intercalated cell H(+)-ATPase in two patients with lupus nephritis and hyperkalemic distal renal tubular acidosis. J Am Soc Nephrol 1997; 7: 1109-1117.
    • (1997) J Am Soc Nephrol , vol.7 , pp. 1109-1117
    • Bastani, B.1    Underhill, D.2    Chu, N.3    Nelson, R.D.4    Haragsim, L.5    Gluck, S.6
  • 70
    • 0032726897 scopus 로고    scopus 로고
    • Targeted disruption of the gene encoding the proteolipid subunit of mouse vacuolar H(+)-ATPase leads to early embryonic lethality
    • Inoue H, Noumi T, Nagata M, Murakami H, Kanazawa H. Targeted disruption of the gene encoding the proteolipid subunit of mouse vacuolar H(+)-ATPase leads to early embryonic lethality. Biochim Biophys Acta 1999; 1413:130-138.
    • (1999) Biochim Biophys Acta , vol.1413 , pp. 130-138
    • Inoue, H.1    Noumi, T.2    Nagata, M.3    Murakami, H.4    Kanazawa, H.5
  • 71
    • 0032748995 scopus 로고    scopus 로고
    • Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification
    • Li YP, Chen W, Liang Y, Li E, Stashenko P. Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification. Nat Genet 1999; 23:447-451.
    • (1999) Nat Genet , vol.23 , pp. 447-451
    • Li, Y.P.1    Chen, W.2    Liang, Y.3    Li, E.4    Stashenko, P.5
  • 76
    • 0008959136 scopus 로고    scopus 로고
    • Sarco/endoplasmic reticulum Ca2+ (SERCA)-pumps: Link to heart beats and calcium waves
    • Misquitta CM, Mack DP, Grover AK. Sarco/endoplasmic reticulum Ca2+ (SERCA)-pumps: link to heart beats and calcium waves. Cell Calcium 1999; 25:277-290.
    • (1999) Cell Calcium , vol.25 , pp. 277-290
    • Misquitta, C.M.1    Mack, D.P.2    Grover, A.K.3
  • 77
    • 0030467311 scopus 로고    scopus 로고
    • The plasma membrane calcium pump: Recent developments and future perspectives
    • Carafoli E, Garcia-Martin E, Guerini D. The plasma membrane calcium pump: recent developments and future perspectives. Experientia 1996; 52:1091-1100.
    • (1996) Experientia , vol.52 , pp. 1091-1100
    • Carafoli, E.1    Garcia-Martin, E.2    Guerini, D.3
  • 78
    • 0032146635 scopus 로고    scopus 로고
    • Gastric H+/K+-ATPase: Targeting signals in the regulation of physiologic function
    • Caplan MJ. Gastric H+/K+-ATPase: targeting signals in the regulation of physiologic function. Curr Opin Cell Biol 1998; 10:468-473.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 468-473
    • Caplan, M.J.1
  • 79
    • 0027522993 scopus 로고
    • Renal tubule of dogfish, Scylior-hinus caniculus: A comprehensive study of structure with emphasis on intramembrane particles and immunoreactivity for H(+)-K(+)-adenosine triphosphatase
    • Hentschel H, Mahler S, Herter P, Elger M. Renal tubule of dogfish, Scylior-hinus caniculus: a comprehensive study of structure with emphasis on intramembrane particles and immunoreactivity for H(+)-K(+)-adenosine triphosphatase. Anat Rec 1993; 235:511-532.
    • (1993) Anat Rec , vol.235 , pp. 511-532
    • Hentschel, H.1    Mahler, S.2    Herter, P.3    Elger, M.4
  • 80
    • 0028131858 scopus 로고
    • Physiological and immunocytochemical evidence for a putative H-K-ATPase in elas-mobranch renal acid secretion
    • Swenson ER, Fine AD, Maren TH, Reale E, Lacy ER, Smolka AJ. Physiological and immunocytochemical evidence for a putative H-K-ATPase in elas-mobranch renal acid secretion. Am J Physiol 1994; 267:F639-F645.
    • (1994) Am J Physiol , vol.267 , pp. F639-F645
    • Swenson, E.R.1    Fine, A.D.2    Maren, T.H.3    Reale, E.4    Lacy, E.R.5    Smolka, A.J.6
  • 81
    • 0024356509 scopus 로고
    • Active protein secretion and potassium absorption in the rabbit outer medullary collecting duct: Functional evidence for proton, potassium activated adenosine triphosphatase
    • Wingo CS. Active protein secretion and potassium absorption in the rabbit outer medullary collecting duct: functional evidence for proton, potassium activated adenosine triphosphatase. J Clin Invest 1989; 84:361-365.
    • (1989) J Clin Invest , vol.84 , pp. 361-365
    • Wingo, C.S.1
  • 82
    • 0026465110 scopus 로고
    • Rubidium absorption and proton secretion by rabbit outer medullary collecting duct via H+/K+-ATPase
    • Wingo CS, Armitage FE. Rubidium absorption and proton secretion by rabbit outer medullary collecting duct via H+/K+-ATPase. Am J Physiol 1992; 263:F849-F857.
    • (1992) Am J Physiol , vol.263 , pp. F849-F857
    • Wingo, C.S.1    Armitage, F.E.2
  • 83
    • 0027474515 scopus 로고
    • Functional identification of H+/K+-ATPase in intercalated cells of cortical collecting tubule
    • Silver RB, Frindt G. Functional identification of H+/K+-ATPase in intercalated cells of cortical collecting tubule. Am J Physiol 1993; 264: F259-F266.
    • (1993) Am J Physiol , vol.264 , pp. F259-F266
    • Silver, R.B.1    Frindt, G.2
  • 84
    • 0029853573 scopus 로고    scopus 로고
    • H+/K+-ATPase mediates net acid secretion in rat terminal inner medullary collecting duct
    • Wall SM, Truong AV, DuBose TD. H+/K+-ATPase mediates net acid secretion in rat terminal inner medullary collecting duct. Am J Physiol 1996; 271:F1037-F1044.
    • (1996) Am J Physiol , vol.271 , pp. F1037-F1044
    • Wall, S.M.1    Truong, A.V.2    DuBose, T.D.3
  • 85
    • 0029865691 scopus 로고    scopus 로고
    • H+/K+-ATPase in rabbit cortical collecting duct B-type intercalated cell
    • Weiner ID, Milton AE. H+/K+-ATPase in rabbit cortical collecting duct B-type intercalated cell. Am J Physiol 1996; 270:F450-F458.
    • (1996) Am J Physiol , vol.270 , pp. F450-F458
    • Weiner, I.D.1    Milton, A.E.2
  • 86
    • 0024450973 scopus 로고
    • Sodium ions as substitutes for protons in the gastric H,K-ATPase
    • Polvani C, Sachs G, Blostein R. Sodium ions as substitutes for protons in the gastric H,K-ATPase. J Biol Chem 1989; 264:17,854-17,859.
    • (1989) J Biol Chem , vol.264 , pp. 17854-17859
    • Polvani, C.1    Sachs, G.2    Blostein, R.3
  • 87
    • 0025200972 scopus 로고
    • Conformational transitions of the H,K-ATPase studied with sodium ions as surrogates for protons
    • Rabon EC, Bassilian S, Sachs G, Karlish SJ. Conformational transitions of the H,K-ATPase studied with sodium ions as surrogates for protons. J Biol Chem 1990; 265:19,594-19,599.
    • (1990) J Biol Chem , vol.265 , pp. 19594-19599
    • Rabon, E.C.1    Bassilian, S.2    Sachs, G.3    Karlish, S.J.4
  • 88
    • 0032561182 scopus 로고    scopus 로고
    • ATP1AL1, a member of the non-gastric H,K-ATPase family, functions as a sodium pump
    • Grishin AV, Caplan MJ. ATP1AL1, a member of the non-gastric H,K-ATPase family, functions as a sodium pump. J Biol Chem 1998; 273:27,772-27,778.
    • (1998) J Biol Chem , vol.273 , pp. 27772-27778
    • Grishin, A.V.1    Caplan, M.J.2
  • 90
    • 0023796964 scopus 로고
    • Protons as substitutes for sodium and potassium in the sodium pump reaction
    • Polvani C, Blostein R. Protons as substitutes for sodium and potassium in the sodium pump reaction. J Biol Chem 1988; 263:16,757-16,763.
    • (1988) J Biol Chem , vol.263 , pp. 16757-16763
    • Polvani, C.1    Blostein, R.2
  • 91
    • 0033000386 scopus 로고    scopus 로고
    • H-K-ATPases: Regulation and role in pathophysio-logic states
    • Silver RN, Soleimani M. H-K-ATPases: regulation and role in pathophysio-logic states. Am J Physiol 1999; 276:F799-F811.
    • (1999) Am J Physiol , vol.276 , pp. F799-F811
    • Silver, R.N.1    Soleimani, M.2
  • 92
    • 0025009959 scopus 로고
    • H-K-ATPase immunoreactivity in cortical and outer medullary collecting duct
    • Wingo CS, Madsen KM, Smolka A, Tisher CC. H-K-ATPase immunoreactivity in cortical and outer medullary collecting duct. Kidney Int 1990; 38:985-990.
    • (1990) Kidney Int , vol.38 , pp. 985-990
    • Wingo, C.S.1    Madsen, K.M.2    Smolka, A.3    Tisher, C.C.4
  • 93
    • 0029079008 scopus 로고
    • Colocalization of H-ATPase and K-K-ATPase immunoreactivity in the rat kidney
    • Bastani B. Colocalization of H-ATPase and K-K-ATPase immunoreactivity in the rat kidney. J Am Soc Nephrol 1995; 5:1476-1482.
    • (1995) J Am Soc Nephrol , vol.5 , pp. 1476-1482
    • Bastani, B.1
  • 94
    • 0028813319 scopus 로고
    • Expression and cellular localization of mRNA encoding the "gastric" isoform of H(+)-K(+)-ATPase alpha-subunit in rat kidney
    • Ahn KY, Kone BC. Expression and cellular localization of mRNA encoding the "gastric" isoform of H(+)-K(+)-ATPase alpha-subunit in rat kidney. Am J Physiol 1995; 268:F99-F109.
    • (1995) Am J Physiol , vol.268 , pp. F99-F109
    • Ahn, K.Y.1    Kone, B.C.2
  • 95
    • 0028968196 scopus 로고
    • Expression of gastric and colonic H(+)-K(+)-ATPase in the rat kidney
    • Kraut JA, Starr F, Sachs G, Reuben M. Expression of gastric and colonic H(+)-K(+)-ATPase in the rat kidney. Am J Physiol 1995; 268:F581-F587.
    • (1995) Am J Physiol , vol.268 , pp. F581-F587
    • Kraut, J.A.1    Starr, F.2    Sachs, G.3    Reuben, M.4
  • 96
    • 0033830188 scopus 로고    scopus 로고
    • Differential localization of human nongastric H(+)-K(+)-ATPase ATP1AL1 in polarized renal epithelial cells
    • Reinhardt J, Grishin AV, Oberleithner H, Caplan MJ. Differential localization of human nongastric H(+)-K(+)-ATPase ATP1AL1 in polarized renal epithelial cells. Am J Physiol 2000; 279:F417-F425.
    • (2000) Am J Physiol , vol.279 , pp. F417-F425
    • Reinhardt, J.1    Grishin, A.V.2    Oberleithner, H.3    Caplan, M.J.4
  • 97
    • 0031021581 scopus 로고    scopus 로고
    • Re-evaluation of the expression of the gastric H,K-ATPase alpha subunit along the rat nephron
    • Cheval L, Elalouf JM, Doucet A. Re-evaluation of the expression of the gastric H,K-ATPase alpha subunit along the rat nephron. Pflugers Arch 1997; 433:539-541.
    • (1997) Pflugers Arch , vol.433 , pp. 539-541
    • Cheval, L.1    Elalouf, J.M.2    Doucet, A.3
  • 98
    • 0030733798 scopus 로고    scopus 로고
    • Characterization and regulation of H-K-ATPase in intercalated cells of rabbit cortical collecting duct
    • Silver RB, Frindt G, Mennitt P, Satlin L. Characterization and regulation of H-K-ATPase in intercalated cells of rabbit cortical collecting duct. J Exp Zool 1997; 279:443-455.
    • (1997) J Exp Zool , vol.279 , pp. 443-455
    • Silver, R.B.1    Frindt, G.2    Mennitt, P.3    Satlin, L.4
  • 99
    • 0026766656 scopus 로고
    • Isolation and characterization of a cDNA encoding the putative distal colon H-K-ATPase
    • Crowson MS, Shull GE. Isolation and characterization of a cDNA encoding the putative distal colon H-K-ATPase. J Biol Chem 1992; 2267:13,740-13,748.
    • (1992) J Biol Chem , vol.2267 , pp. 13740-13748
    • Crowson, M.S.1    Shull, G.E.2
  • 101
    • 0029736657 scopus 로고    scopus 로고
    • Chronic hypokalemia enhances expression of the H(+)-K(+)-ATPase alpha 2-subunit gene in renal medulla
    • Ahn KY, Park KY, Kim KK, Kone BC. Chronic hypokalemia enhances expression of the H(+)-K(+)-ATPase alpha 2-subunit gene in renal medulla. Am J Physiol 1996; 271:F314-F321.
    • (1996) Am J Physiol , vol.271 , pp. F314-F321
    • Ahn, K.Y.1    Park, K.Y.2    Kim, K.K.3    Kone, B.C.4
  • 102
    • 0029865691 scopus 로고    scopus 로고
    • H-K-ATPase in rabbit cortical collecting duct B-type intercalated
    • Weiner ID, Milton AE. H-K-ATPase in rabbit cortical collecting duct B-type intercalated. Am J Physiol 1996; 270:F518-F530.
    • (1996) Am J Physiol , vol.270 , pp. F518-F530
    • Weiner, I.D.1    Milton, A.E.2
  • 105
    • 0033067063 scopus 로고    scopus 로고
    • The nongastric H+/K+-ATPase's: Molecular and functional properties
    • Jaisser F, Beggah AT. The nongastric H+/K+-ATPase's: molecular and functional properties. Am J Physiol 1999; 276:F812-F824.
    • (1999) Am J Physiol , vol.276 , pp. F812-F824
    • Jaisser, F.1    Beggah, A.T.2
  • 106
    • 0033058242 scopus 로고    scopus 로고
    • H-K-ATPase in the RCCT-28A rabbit cortical collecting duct cell line
    • Campbell WG, Weiner ID, Wingo CS, Cain BD. H-K-ATPase in the RCCT-28A rabbit cortical collecting duct cell line. Am J Physiol 1999; 276:F237-F245.
    • (1999) Am J Physiol , vol.276 , pp. F237-F245
    • Campbell, W.G.1    Weiner, I.D.2    Wingo, C.S.3    Cain, B.D.4
  • 107
    • 0032579251 scopus 로고    scopus 로고
    • A novel N-terminal splice variant of the rat H+-K+-ATPase alpha2 subunit: Cloning, functional expression, and renal adaptive response to chronic hypokalemia
    • Kone BC, Higham SC. A novel N-terminal splice variant of the rat H+-K+-ATPase alpha2 subunit: cloning, functional expression, and renal adaptive response to chronic hypokalemia. J Biol Chem 1998; 273:2543-2552.
    • (1998) J Biol Chem , vol.273 , pp. 2543-2552
    • Kone, B.C.1    Higham, S.C.2
  • 110
    • 0032130345 scopus 로고    scopus 로고
    • Symposium on ion motive ATPase
    • Sachs G. Symposium on ion motive ATPase. Acta Physiol Scand 1998; 643(supp):5-6.
    • (1998) Acta Physiol Scand , vol.643 , pp. 5-6
    • Sachs, G.1
  • 111
    • 0033950349 scopus 로고    scopus 로고
    • Analysis of the membrane domain of the gastric H/K ATPase
    • Munson K, Lanbrecht N, Shin JM, Sachs G. Analysis of the membrane domain of the gastric H/K ATPase. J Exp Biol 2000; 203:161-170.
    • (2000) J Exp Biol , vol.203 , pp. 161-170
    • Munson, K.1    Lanbrecht, N.2    Shin, J.M.3    Sachs, G.4
  • 112
    • 0028361579 scopus 로고
    • Topological analysis of H+,K(+)-ATPase using in vitro translation
    • Bamberg K, Sachs G. Topological analysis of H+,K(+)-ATPase using in vitro translation. J Biol Chem 1994; 269:16,909-16,919.
    • (1994) J Biol Chem , vol.269 , pp. 16909-16919
    • Bamberg, K.1    Sachs, G.2
  • 113
    • 0032560144 scopus 로고    scopus 로고
    • Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
    • Auer M, Scarborough GA, Kuhlbrandt W. Three-dimensional map of the plasma membrane H+-ATPase in the open conformation. Nature 1998; 392:840-843.
    • (1998) Nature , vol.392 , pp. 840-843
    • Auer, M.1    Scarborough, G.A.2    Kuhlbrandt, W.3
  • 114
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution
    • Zhang P, Toyoshima C, Yonekura K, Green NM, Stokes DL. Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution. Nature 1998; 392:835-839.
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5
  • 115
    • 0028246635 scopus 로고
    • Identification of a region of the H,K-ATPase alpha subunit associated with the beta subunit
    • Shin JM, Sachs G. Identification of a region of the H,K-ATPase alpha subunit associated with the beta subunit. J Biol Chem 1994; 269:8642-8646.
    • (1994) J Biol Chem , vol.269 , pp. 8642-8646
    • Shin, J.M.1    Sachs, G.2
  • 116
    • 0032080152 scopus 로고    scopus 로고
    • Regions of association between the alpha and the beta subunit of the gastric H,K-ATPase
    • Melle-Milovanovic D, Milovanovic M, Nagpal S, Sachs G, Shin JM. Regions of association between the alpha and the beta subunit of the gastric H,K-ATPase. J Biol Chem 1998; 273:11,075-11,081.
    • (1998) J Biol Chem , vol.273 , pp. 11075-11081
    • Melle-Milovanovic, D.1    Milovanovic, M.2    Nagpal, S.3    Sachs, G.4    Shin, J.M.5
  • 117
    • 0026711112 scopus 로고
    • Gastric H-K-ATPase activity is inhibited by reduction of disulphide bonds in the beat-subunit
    • Chow DC, Browning CM, Forte JG. Gastric H-K-ATPase activity is inhibited by reduction of disulphide bonds in the beat-subunit. Am J Physiol 1992; 263:C39-C46.
    • (1992) Am J Physiol , vol.263 , pp. C39-C46
    • Chow, D.C.1    Browning, C.M.2    Forte, J.G.3
  • 118
    • 85128011269 scopus 로고
    • Molecular requirements for cell surface expression of multi-subunit ion-transporting ATPases
    • Caplan M, Gottardi CJ. Molecular requirements for cell surface expression of multi-subunit ion-transporting ATPases. J Biol Chem 1993; 268:24,921-24,931.
    • (1993) J Biol Chem , vol.268 , pp. 24921-24931
    • Caplan, M.1    Gottardi, C.J.2
  • 119
    • 0040888007 scopus 로고    scopus 로고
    • Beta subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase alpha-subunit
    • Beggah AT, Beguin P, Bamberg K, Sachs G, Geering K. Beta subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase alpha-subunit. J Biol Chem 1999; 274:8217-8223.
    • (1999) J Biol Chem , vol.274 , pp. 8217-8223
    • Beggah, A.T.1    Beguin, P.2    Bamberg, K.3    Sachs, G.4    Geering, K.5
  • 120
    • 0016163685 scopus 로고
    • The K+-stimulated ATPase system of microsomal membrane from gastric oxyntic cells
    • Forte JG, Ganser AL, Tanisawa AS. The K+-stimulated ATPase system of microsomal membrane from gastric oxyntic cells. Ann NY Acad Sci 1974; 242:255-267.
    • (1974) Ann NY Acad Sci , vol.242 , pp. 255-267
    • Forte, J.G.1    Ganser, A.L.2    Tanisawa, A.S.3
  • 122
    • 0028888879 scopus 로고
    • Gastric acid secretion
    • Hersey SJ, Sachs G. Gastric acid secretion. Physiol Rev 1995; 75:155-189.
    • (1995) Physiol Rev , vol.75 , pp. 155-189
    • Hersey, S.J.1    Sachs, G.2
  • 123
    • 0030948553 scopus 로고    scopus 로고
    • Regulation of colonic H+/K+-ATPase in large intestine and kidney by dietary Na depletion and dietary K depletion
    • Sangan P, Rajendran VM, Mann AS, Kashgarian M, Binder HJ. Regulation of colonic H+/K+-ATPase in large intestine and kidney by dietary Na depletion and dietary K depletion. Am J Physiol 1997; 272:C685-C696.
    • (1997) Am J Physiol , vol.272 , pp. C685-C696
    • Sangan, P.1    Rajendran, V.M.2    Mann, A.S.3    Kashgarian, M.4    Binder, H.J.5
  • 124
    • 0031684360 scopus 로고    scopus 로고
    • Colonic H+-K+-ATPase is induced and mediates increased HCOjT reabsorption in inner medullary collecting duct in potassium depletion
    • Nakamura S, Amlal H, Galla JH, Soleimani M. Colonic H+-K+-ATPase is induced and mediates increased HCOjT reabsorption in inner medullary collecting duct in potassium depletion. Kidney Int 1998; 54:1233-1239.
    • (1998) Kidney Int , vol.54 , pp. 1233-1239
    • Nakamura, S.1    Amlal, H.2    Galla, J.H.3    Soleimani, M.4
  • 125
    • 0033258326 scopus 로고    scopus 로고
    • Secretion in inner medullary collecting duct in potassium deprivation: Role of colonic H+-K+-ATPase
    • Nakamura S, Amlal H, Galla JH, Soleimani M. secretion in inner medullary collecting duct in potassium deprivation: role of colonic H+-K+-ATPase. Kidney Int 1999; 56:2160-2167.
    • (1999) Kidney Int , vol.56 , pp. 2160-2167
    • Nakamura, S.1    Amlal, H.2    Galla, J.H.3    Soleimani, M.4
  • 126
    • 0023554066 scopus 로고
    • Characterization of K-ATPase activity in distal nephron: Stimulation by K+ depletion
    • Doucet A, Marsy S. Characterization of K-ATPase activity in distal nephron: stimulation by K+ depletion. Am J Physiol 1987; 253:F418-F423.
    • (1987) Am J Physiol , vol.253 , pp. F418-F423
    • Doucet, A.1    Marsy, S.2
  • 127
    • 0023936434 scopus 로고
    • Ouabain-insensitive K-adenosine triphosphatase in distal nephron segments of the rabbit
    • Garg LC, Narang N. Ouabain-insensitive K-adenosine triphosphatase in distal nephron segments of the rabbit. J Clin Invest 1988; 81:1204-1208.
    • (1988) J Clin Invest , vol.81 , pp. 1204-1208
    • Garg, L.C.1    Narang, N.2
  • 129
    • 0028131421 scopus 로고
    • Effects of respiratory acidosis and respiratory alkalosis on renal transport enzymes
    • Eiam-Ong S, Laski ME, Kurtzman NA, Sabatini S. Effects of respiratory acidosis and respiratory alkalosis on renal transport enzymes. Am J Physiol 1994; 267:F390-F399.
    • (1994) Am J Physiol , vol.267 , pp. F390-F399
    • Eiam-Ong, S.1    Laski, M.E.2    Kurtzman, N.A.3    Sabatini, S.4
  • 130
    • 0028048869 scopus 로고
    • Stimulation of total CO2 flux by 10% CO2 in rabbit CCD: Role of an apical SCH-28080 and Ba-sensitive mechanism
    • Zhou X, Wingo CS. Stimulation of total CO2 flux by 10% CO2 in rabbit CCD: role of an apical SCH-28080 and Ba-sensitive mechanism. Am J Physiol 1994; 267:F114-F120.
    • (1994) Am J Physiol , vol.267 , pp. F114-F120
    • Zhou, X.1    Wingo, C.S.2
  • 131
    • 0029867508 scopus 로고    scopus 로고
    • Stimulation of apical H+/K+-ATPase in intercalated cells of cortical collecting duct with chronic metabolic acidosis
    • Silver RB, Frindt G, Mennitt P, Satlin L. Stimulation of apical H+/K+-ATPase in intercalated cells of cortical collecting duct with chronic metabolic acidosis. Am J Physiol 1996; 270:F539-F547.
    • (1996) Am J Physiol , vol.270 , pp. F539-F547
    • Silver, R.B.1    Frindt, G.2    Mennitt, P.3    Satlin, L.4
  • 133
    • 0027757066 scopus 로고
    • H-K-ATPase in distal renal tubular acidosis: Urinary tract obstruction, lithium, and amiloride
    • Eiam-Ong S, Dafnis E, Spohn M, Kurtzman NA, Sabatini S. H-K-ATPase in distal renal tubular acidosis: urinary tract obstruction, lithium, and amiloride. Am J Physiol 1993; 265:F875-F880.
    • (1993) Am J Physiol , vol.265 , pp. F875-F880
    • Eiam-Ong, S.1    Dafnis, E.2    Spohn, M.3    Kurtzman, N.A.4    Sabatini, S.5
  • 134
  • 136
    • 0027538120 scopus 로고
    • An ion-transporting ATPase encodes multiple apical localization signals
    • Gottardi CJ, Caplan MJ. An ion-transporting ATPase encodes multiple apical localization signals. J Cell Biol 1993; 121:283-293.
    • (1993) J Cell Biol , vol.121 , pp. 283-293
    • Gottardi, C.J.1    Caplan, M.J.2
  • 137
    • 0030797573 scopus 로고    scopus 로고
    • A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion
    • Courtois-Coutry N, Roush D, Rajendran V, McCarthy JB, Geibel J, Kashgarian M, Caplan MJ. A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion. Cell 1997; 90:501-510.
    • (1997) Cell , vol.90 , pp. 501-510
    • Courtois-Coutry, N.1    Roush, D.2    Rajendran, V.3    McCarthy, J.B.4    Geibel, J.5    Kashgarian, M.6    Caplan, M.J.7
  • 138
    • 0031731248 scopus 로고    scopus 로고
    • A tyrosine-based signal regulates HKATPase-mediated potassium absorption in the kidney
    • Wang T, Courtois-Coutry N, Giebisch G, Caplan MJ. A tyrosine-based signal regulates HKATPase-mediated potassium absorption in the kidney. Am J Physiol 1998; 275:F818-826.
    • (1998) Am J Physiol , vol.275 , pp. F818-F826
    • Wang, T.1    Courtois-Coutry, N.2    Giebisch, G.3    Caplan, M.J.4
  • 139
    • 0027745603 scopus 로고
    • Na/H antiporters, molecular devices that couple the Na+ and H+ circulation in cells
    • Padan E, Sculdiner S. Na/H antiporters, molecular devices that couple the Na+ and H+ circulation in cells. J Bioenerg Biomembr 1993; 25:647-669.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 647-669
    • Padan, E.1    Sculdiner, S.2
  • 140
    • 0029922104 scopus 로고    scopus 로고
    • Salt tolerance in plants and microorganisms: Toxicity targets and defense responses
    • Serrano R. Salt tolerance in plants and microorganisms: toxicity targets and defense responses. Int Rev Cytol 1996; 165:1-52.
    • (1996) Int Rev Cytol , vol.165 , pp. 1-52
    • Serrano, R.1
  • 141
    • 0027249470 scopus 로고
    • Energy transduction in the thermophilic anerobic bacterium Colstridium fervifus is exclusively coupled to Na ions
    • Speelmans G, poolman B, Abee T, Konings WN. Energy transduction in the thermophilic anerobic bacterium Colstridium fervifus is exclusively coupled to Na ions. Proc Natl Acad Sci USA 1993; 90:7975-7979.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7975-7979
    • Speelmans, G.1    poolman, B.2    Abee, T.3    Konings, W.N.4
  • 142
    • 0028534837 scopus 로고
    • Molecular physiology of the Na/H antiporter in Escherichia coli
    • Padan E, Sculdiner S. Molecular physiology of the Na/H antiporter in Escherichia coli. J Exp Biol 1994; 196:443-456.
    • (1994) J Exp Biol , vol.196 , pp. 443-456
    • Padan, E.1    Sculdiner, S.2
  • 143
    • 0025369650 scopus 로고
    • Electrogenic 2 Na+/1H+ exchange in crustaceans
    • Ahearn GA, Franco P, Clay LP. Electrogenic 2 Na+/1H+ exchange in crustaceans. J Membr Biol 1990; 116:215-226.
    • (1990) J Membr Biol , vol.116 , pp. 215-226
    • Ahearn, G.A.1    Franco, P.2    Clay, L.P.3
  • 144
    • 0024552377 scopus 로고
    • Molecular cloning, primary structure and expression of the human growth factor-activatable Na/H antiporter
    • Sardet C, Counillion L, Franchi A, Pouyssegur. Molecular cloning, primary structure and expression of the human growth factor-activatable Na/H antiporter. Cell 1989; 56:271-280.
    • (1989) Cell , vol.56 , pp. 271-280
    • Sardet, C.1    Counillion, L.2    Franchi, A.3    Pouyssegur4
  • 145
    • 0030984026 scopus 로고    scopus 로고
    • Na+/H+ exchangers of mammalian cells
    • Orlowski J, Grinstein S. Na+/H+ exchangers of mammalian cells. J Biol Chem 1997; 272:22,373-22,376.
    • (1997) J Biol Chem , vol.272 , pp. 22373-22376
    • Orlowski, J.1    Grinstein, S.2
  • 146
    • 0035907355 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel (Na+,K+)/H+ exchanger localized to the iraws-golgi network
    • Numata M, Orlowski J. Molecular cloning and characterization of a novel (Na+,K+)/H+ exchanger localized to the iraws-golgi network. J Biol Chem 2001; 276:17,387-17,394.
    • (2001) J Biol Chem , vol.276 , pp. 17387-17394
    • Numata, M.1    Orlowski, J.2
  • 149
    • 0029099062 scopus 로고
    • Expression of NHE-3 in the apical membrane of rat renal proximal tubule and thick ascending limb
    • Amemiya M, Loffing J, Lotscher M, Kaissling B, Alpern RJ, Moe OW. Expression of NHE-3 in the apical membrane of rat renal proximal tubule and thick ascending limb. Kidney Int 1995; 48:1206-1215.
    • (1995) Kidney Int , vol.48 , pp. 1206-1215
    • Amemiya, M.1    Loffing, J.2    Lotscher, M.3    Kaissling, B.4    Alpern, R.J.5    Moe, O.W.6
  • 151
    • 0023780483 scopus 로고
    • Role of Na/H antiport in rat proximal tubule NaCl absorption
    • Priesig PA, Rector FC Jr. Role of Na/H antiport in rat proximal tubule NaCl absorption. Am J Physiol 1988; 255:F461-F467.
    • (1988) Am J Physiol , vol.255 , pp. F461-F467
    • Priesig, P.A.1    Rector, F.C.2
  • 152
    • 85128101555 scopus 로고
    • Sodium-dependent bicarbonate absorption by the cortical thick ascending limb
    • Good DW. Sodium-dependent bicarbonate absorption by the cortical thick ascending limb. Am J Physiol 1988; 247:F821-F829.
    • (1988) Am J Physiol , vol.247 , pp. F821-F829
    • Good, D.W.1
  • 153
    • 0026495612 scopus 로고
    • Immunocyto-chemical characterization of Na(+)-H+ exchanger isoform NHE-1 in rabbit kidney
    • Biemesderfer D, Reilly RF, Exner M, Igarashi P, Aronson PS. Immunocyto-chemical characterization of Na(+)-H+ exchanger isoform NHE-1 in rabbit kidney. Am J Physiol 1992; 263:F833-F840.
    • (1992) Am J Physiol , vol.263 , pp. F833-F840
    • Biemesderfer, D.1    Reilly, R.F.2    Exner, M.3    Igarashi, P.4    Aronson, P.S.5
  • 154
    • 0030728255 scopus 로고    scopus 로고
    • Na+/H+ exchanger isoform 2 (NHE2) is expressed in the apical membrane of the medullary thick ascending limb
    • Sun AM, Liu Y, Dworkin LD, Tse CM, Donowitz M, Yip KP. Na+/H+ exchanger isoform 2 (NHE2) is expressed in the apical membrane of the medullary thick ascending limb. J Membr Biol 1997; 160:85-90.
    • (1997) J Membr Biol , vol.160 , pp. 85-90
    • Sun, A.M.1    Liu, Y.2    Dworkin, L.D.3    Tse, C.M.4    Donowitz, M.5    Yip, K.P.6
  • 155
    • 0030459406 scopus 로고    scopus 로고
    • Role of NHE3 in mediating renal brush border Na+-H+ exchange. Adaptation to metabolic acidosis
    • Wu MS, Biemesderfer D, Giebisch G, Aronson PS. Role of NHE3 in mediating renal brush border Na+-H+ exchange. Adaptation to metabolic acidosis. J Biol Chem 1996; 271:32,749-32,752.
    • (1996) J Biol Chem , vol.271 , pp. 32749-32752
    • Wu, M.S.1    Biemesderfer, D.2    Giebisch, G.3    Aronson, P.S.4
  • 156
    • 0010217910 scopus 로고    scopus 로고
    • Novel amiloride-sensitive sodium-dependent proton secretion in the mouse proximal convoluted tubule
    • Choi JY, Shah M, Lee MG, Schultheis PJ, Shull GE, Muallem S, Baum M. Novel amiloride-sensitive sodium-dependent proton secretion in the mouse proximal convoluted tubule. J Clin Invest 2000; 105:1141-1146.
    • (2000) J Clin Invest , vol.105 , pp. 1141-1146
    • Choi, J.Y.1    Shah, M.2    Lee, M.G.3    Schultheis, P.J.4    Shull, G.E.5    Muallem, S.6    Baum, M.7
  • 158
    • 85128076470 scopus 로고    scopus 로고
    • Basolateral NH4 efflux from the rat medullary thick ascending limb cell: A role for the NHE4 Na/H exchanger isoform [abstr]
    • Houillier P, Bourgeois S, Paillard M. Basolateral NH4 efflux from the rat medullary thick ascending limb cell: a role for the NHE4 Na/H exchanger isoform [abstr]. J Am Soc Nephrol 2000; 11:5A.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 5A
    • Houillier, P.1    Bourgeois, S.2    Paillard, M.3
  • 159
    • 0035793559 scopus 로고    scopus 로고
    • The yeast Na/H exchange Nhx1 is an N-linked glycopro-tein
    • Wells KM, Rao R. The yeast Na/H exchange Nhx1 is an N-linked glycopro-tein. J Biol Chem 2001; 276:3401-3407.
    • (2001) J Biol Chem , vol.276 , pp. 3401-3407
    • Wells, K.M.1    Rao, R.2
  • 160
    • 0034636804 scopus 로고    scopus 로고
    • Na(+)/H(+) exchanger NHE3 has 11 membrane spanning domains and a cleaved signal peptide: Topology analysis using in vitro transcription/ translation
    • Zizak M, Cavet ME, Bayle D, Tse CM, Hallen S, Sachs G, Donowitz M. Na(+)/H(+) exchanger NHE3 has 11 membrane spanning domains and a cleaved signal peptide: topology analysis using in vitro transcription/ translation. Biochemistry 2000; 39:8102-8112.
    • (2000) Biochemistry , vol.39 , pp. 8102-8112
    • Zizak, M.1    Cavet, M.E.2    Bayle, D.3    Tse, C.M.4    Hallen, S.5    Sachs, G.6    Donowitz, M.7
  • 161
    • 0031867155 scopus 로고    scopus 로고
    • Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using chymotryptic cleavage
    • Shrode LD, Gan BS, D'Souza SJ, Orlowski J, Grinstein S. Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using chymotryptic cleavage. Am J Physiol 1998; 275:C431-C439.
    • (1998) Am J Physiol , vol.275 , pp. C431-C439
    • Shrode, L.D.1    Gan, B.S.2    D'Souza, S.J.3    Orlowski, J.4    Grinstein, S.5
  • 162
    • 0034677758 scopus 로고    scopus 로고
    • A novel topology model of the human Na(+)/H(+) exchanger isoform 1
    • Wakabayashi S, Pang T, Su X, Shigekawa M. A novel topology model of the human Na(+)/H(+) exchanger isoform 1. J Biol Chem Mar 2000; 275: 7942-7949.
    • (2000) J Biol Chem Mar , vol.275 , pp. 7942-7949
    • Wakabayashi, S.1    Pang, T.2    Su, X.3    Shigekawa, M.4
  • 163
    • 0031035914 scopus 로고    scopus 로고
    • Molecular physiology of vertebrate Na+/H+ exchangers
    • Wakabayashi S, Shigekawa M, Pouyssegur J. Molecular physiology of vertebrate Na+/H+ exchangers. Physiol Rev 1997; 77:51-74.
    • (1997) Physiol Rev , vol.77 , pp. 51-74
    • Wakabayashi, S.1    Shigekawa, M.2    Pouyssegur, J.3
  • 165
    • 0033021073 scopus 로고    scopus 로고
    • Acute regulation of Na/H exchanger NHE-3 by protein kinase C: Role of NHE-3 phosphorylation
    • Wiederkehr MR, Zhao H, Moe OW. Acute regulation of Na/H exchanger NHE-3 by protein kinase C: role of NHE-3 phosphorylation. Am J Physiol 1999; 276:C1205-C1217.
    • (1999) Am J Physiol , vol.276 , pp. C1205-C1217
    • Wiederkehr, M.R.1    Zhao, H.2    Moe, O.W.3
  • 167
    • 0026582813 scopus 로고
    • The Na+/H+ antiporter cytoplasmic domain mediates growth factor signals and controls "H(+)-sensing."
    • Wakabayashi S, Fafournoux P, Sardet C, Pouyssegur J. The Na+/H+ antiporter cytoplasmic domain mediates growth factor signals and controls "H(+)-sensing." Proc Natl Acad Sci USA 1992; 89:2424-2428.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2424-2428
    • Wakabayashi, S.1    Fafournoux, P.2    Sardet, C.3    Pouyssegur, J.4
  • 168
    • 0019975497 scopus 로고
    • Modifier role of internal H+ in activating the Na+-H+ exchanger in renal microvillus membrane vesicles
    • Aronson PS, Nee J, Suhm MA. Modifier role of internal H+ in activating the Na+-H+ exchanger in renal microvillus membrane vesicles. Nature 1982; 299:161-163.
    • (1982) Nature , vol.299 , pp. 161-163
    • Aronson, P.S.1    Nee, J.2    Suhm, M.A.3
  • 169
    • 0030696884 scopus 로고    scopus 로고
    • Calmodulin-binding autoinhibitory domain controls "pH-sensing" in the Na+/H+ exchanger NHE1 through sequence-specific interaction
    • Wakabayashi S, Ikeda T, Iwamoto T, Pouyssegur J, Shigekawa M. Calmodulin-binding autoinhibitory domain controls "pH-sensing" in the Na+/H+ exchanger NHE1 through sequence-specific interaction. Biochemistry 1997; 36:12,854-12,861.
    • (1997) Biochemistry , vol.36 , pp. 12854-12861
    • Wakabayashi, S.1    Ikeda, T.2    Iwamoto, T.3    Pouyssegur, J.4    Shigekawa, M.5
  • 170
    • 20644457909 scopus 로고    scopus 로고
    • Thyroid hormone stimulates the renal Na/H exchanger NHE-3 by transcriptional activation
    • Cano A, Baum M, Moe OW. Thyroid hormone stimulates the renal Na/H exchanger NHE-3 by transcriptional activation. Am J Physiol 1999; 276:C102-C108.
    • (1999) Am J Physiol , vol.276 , pp. C102-C108
    • Cano, A.1    Baum, M.2    Moe, O.W.3
  • 171
    • 0025856542 scopus 로고
    • Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli
    • Taglicht D, Padan E, Schuldiner S. Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. J Biol Chem 1991; 266:11,289-11,294.
    • (1991) J Biol Chem , vol.266 , pp. 11289-11294
    • Taglicht, D.1    Padan, E.2    Schuldiner, S.3
  • 173
    • 0030983983 scopus 로고    scopus 로고
    • Na-H exchange in renal epithelia. Mechanisms of acute regulation by protein kinases
    • Moe OW. Na-H exchange in renal epithelia. Mechanisms of acute regulation by protein kinases. Curr Opin Nephrol Hypertens 1997; 6:440-446.
    • (1997) Curr Opin Nephrol Hypertens , vol.6 , pp. 440-446
    • Moe, O.W.1
  • 174
    • 0032736233 scopus 로고    scopus 로고
    • Acute regulation of proximal tubule Na/H exchanger NHE-3: Role of NHE-3 phosphorylation, trafficking and regulatory cofactors
    • Moe OW. Acute regulation of proximal tubule Na/H exchanger NHE-3: role of NHE-3 phosphorylation, trafficking and regulatory cofactors. J Am Soc Nephrol 1999; 10:2412-2425.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2412-2425
    • Moe, O.W.1
  • 175
    • 0032524329 scopus 로고    scopus 로고
    • Membrane topology of NHE3. Epitopes within the carboxyl-terminal hydrophilic domain are exoplasmic
    • Biemesderfer D, DeGray B, Aronson PS. Membrane topology of NHE3. Epitopes within the carboxyl-terminal hydrophilic domain are exoplasmic. J Biol Chem 1998; 273:12,391-12,396.
    • (1998) J Biol Chem , vol.273 , pp. 12391-12396
    • Biemesderfer, D.1    DeGray, B.2    Aronson, P.S.3
  • 176
    • 0033574637 scopus 로고    scopus 로고
    • Dual mechanism of acute regulation of Na/H exchanger NHE-3 by parathyroid hormone in rat kidney
    • Fan L, Wiederkehr MR, Collazo R, Huang H, Crowder, LA, Moe OW. Dual mechanism of acute regulation of Na/H exchanger NHE-3 by parathyroid hormone in rat kidney. J Biol Chem 1999; 274:11,289-11,295.
    • (1999) J Biol Chem , vol.274 , pp. 11289-11295
    • Fan, L.1    Wiederkehr, M.R.2    Collazo, R.3    Huang, H.4    Crowder, L.A.5    Moe, O.W.6
  • 178
    • 0034644740 scopus 로고    scopus 로고
    • Acute regulation of Na/H exchanger NHE3 by parathyroid hormone via NHE3 phosphorylation and dynamin-dependent endocytosis
    • Collazo R, Fan L, Zhao H, Wiederkehr M, Moe OW. Acute regulation of Na/H exchanger NHE3 by parathyroid hormone via NHE3 phosphorylation and dynamin-dependent endocytosis. J Biol Chem 2000; 276:31,601-31,608.
    • (2000) J Biol Chem , vol.276 , pp. 31601-31608
    • Collazo, R.1    Fan, L.2    Zhao, H.3    Wiederkehr, M.4    Moe, O.W.5
  • 179
    • 0034665980 scopus 로고    scopus 로고
    • RhoA and rho kinase regulate the epithelial Na+/H+ exchanger NHE3. Role of myosin light chain phosphorylation
    • Szaszi K, Kurashima K, Kapus A, Paulsen A, Kaibuchi K, Grinstein S, Orlowski J. RhoA and rho kinase regulate the epithelial Na+/H+ exchanger NHE3. Role of myosin light chain phosphorylation. J Biol Chem 2000; 275:28,599-28,606.
    • (2000) J Biol Chem , vol.275 , pp. 28599-28606
    • Szaszi, K.1    Kurashima, K.2    Kapus, A.3    Paulsen, A.4    Kaibuchi, K.5    Grinstein, S.6    Orlowski, J.7
  • 181
    • 0035920227 scopus 로고    scopus 로고
    • Dopamine stimulates dynamin-dependent endocytosis of NHE3 via PKA-mediated phosphorylation of NHE3
    • Hu MC, Fan L, Quiñones H, Crowder LA, Karim-Jimenez Z, Murer H, Moe OW. Dopamine stimulates dynamin-dependent endocytosis of NHE3 via PKA-mediated phosphorylation of NHE3. J Biol Chem 2001; 276:26906-26915.
    • (2001) J Biol Chem , vol.276 , pp. 26906-26915
    • Hu, M.C.1    Fan, L.2    Quiñones, H.3    Crowder, L.A.4    Karim-Jimenez, Z.5    Murer, H.6    Moe, O.W.7
  • 182
    • 0001836680 scopus 로고
    • CAMP-associated inhibition of Na/H exchanger in rabbit kidney
    • Weinman EJ, Shenolika S, Kahn AM. cAMP-associated inhibition of Na/H exchanger in rabbit kidney. Am J Physiol 1987; 352:F19-F25.
    • (1987) Am J Physiol , vol.352 , pp. F19-F25
    • Weinman, E.J.1    Shenolika, S.2    Kahn, A.M.3
  • 183
    • 0028859366 scopus 로고
    • Activation of protein kinase A acutely phosphorylates and inhibits Na/H exchanger NHE-3
    • Moe OW, Amemiya M, Yamaji Y. Activation of protein kinase A acutely phosphorylates and inhibits Na/H exchanger NHE-3. J Clin Invest 1995; 96:2187-2194.
    • (1995) J Clin Invest , vol.96 , pp. 2187-2194
    • Moe, O.W.1    Amemiya, M.2    Yamaji, Y.3
  • 184
    • 0030695944 scopus 로고    scopus 로고
    • Identification of sites required for down-regulation of Na+/H+ exchanger NHE3 activity by cAMP-dependent protein kinase. phosphorylation-dependent and -independent mechanisms
    • Kurashima K, Yu FH, Cabado AG, Szabo EZ, Grinstein S, Orlowski J. Identification of sites required for down-regulation of Na+/H+ exchanger NHE3 activity by cAMP-dependent protein kinase. phosphorylation-dependent and -independent mechanisms. J Biol Chem 1997; 272:28,672-28,679.
    • (1997) J Biol Chem , vol.272 , pp. 28672-28679
    • Kurashima, K.1    Yu, F.H.2    Cabado, A.G.3    Szabo, E.Z.4    Grinstein, S.5    Orlowski, J.6
  • 185
    • 0033548156 scopus 로고    scopus 로고
    • Acute regulation of Na/H exchanger NHE-3 by protein kinase A (PKA): Role of protein kinase A and NHE-3 phosphoserines 552 and 605
    • Zhao H, Wiederkehr MR, Collazo R, Fan L, Crowder LA, Moe OW. Acute regulation of Na/H exchanger NHE-3 by protein kinase A (PKA): role of protein kinase A and NHE-3 phosphoserines 552 and 605. J Biol Chem 1999; 274:3978-3987.
    • (1999) J Biol Chem , vol.274 , pp. 3978-3987
    • Zhao, H.1    Wiederkehr, M.R.2    Collazo, R.3    Fan, L.4    Crowder, L.A.5    Moe, O.W.6
  • 187
    • 0033609792 scopus 로고    scopus 로고
    • CAMP-induced phosphorylation inhibition of Na(+)/H(+) exchanger 3 (NHE3) are dependent on the presence but not the phosphorylation of NHE regulatory factor
    • Zizak M, Lamprecht G, Steplock D, Tariq N, Shenolikar S, Donowitz M, Yun CH, Weinman EJ. cAMP-induced phosphorylation inhibition of Na(+)/H(+) exchanger 3 (NHE3) are dependent on the presence but not the phosphorylation of NHE regulatory factor. J Biol Chem 1999; 274:24,753-24,558.
    • (1999) J Biol Chem , vol.274 , pp. 24753-24558
    • Zizak, M.1    Lamprecht, G.2    Steplock, D.3    Tariq, N.4    Shenolikar, S.5    Donowitz, M.6    Yun, C.H.7    Weinman, E.J.8
  • 188
    • 0034705178 scopus 로고    scopus 로고
    • NHERF associations with sodium-hydrogen exchanger isoform 3 (NHE3) and ezrin are essential for cAMP-mediated phosphorylation and inhibition of NHE3
    • Weinman EJ, Steplock D, Donowitz M, Shenolikar S. NHERF associations with sodium-hydrogen exchanger isoform 3 (NHE3) and ezrin are essential for cAMP-mediated phosphorylation and inhibition of NHE3. Biochemistry 2000; 39:6123-6129.
    • (2000) Biochemistry , vol.39 , pp. 6123-6129
    • Weinman, E.J.1    Steplock, D.2    Donowitz, M.3    Shenolikar, S.4
  • 189
    • 0030990430 scopus 로고    scopus 로고
    • CAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein
    • Yun CH, Oh S, Zizak M, Steplock D, Tsao S, Tse CM, Weinman EJ, Donowitz M. cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci USA 1997; 94:3010-3015.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3010-3015
    • Yun, C.H.1    Oh, S.2    Zizak, M.3    Steplock, D.4    Tsao, S.5    Tse, C.M.6    Weinman, E.J.7    Donowitz, M.8
  • 190
    • 0032491428 scopus 로고    scopus 로고
    • The role of NHERF and E3KARP in the cAMP mediated inhibition of NHE-3
    • Lamprecht G, Weinman EJ, Yun CHC. The role of NHERF and E3KARP in the cAMP mediated inhibition of NHE-3. J Biol Chem 1998; 273:29,972-29,978.
    • (1998) J Biol Chem , vol.273 , pp. 29972-29978
    • Lamprecht, G.1    Weinman, E.J.2    Yun, C.H.C.3
  • 191
    • 0034995853 scopus 로고    scopus 로고
    • Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK
    • Wade JB, Welling PA, Donowitz M, Shenolikar S, Weinman EJ. Differential renal distribution of NHERF isoforms and their colocalization with NHE3, ezrin, and ROMK. Am J Physiol 2001; 280:C192-C198.
    • (2001) Am J Physiol , vol.280 , pp. C192-C198
    • Wade, J.B.1    Welling, P.A.2    Donowitz, M.3    Shenolikar, S.4    Weinman, E.J.5
  • 193
    • 0030738872 scopus 로고    scopus 로고
    • Regulation of the epithelial brush border Na+/H+ exchanger isoform 3 stably expressed in fibroblasts by fibroblast growth factor and phorbol esters is not through changes in phosphorylation of the exchanger
    • Yip JW, Ko WH, Viberti G, Huganir RL, Donowitz M, Tse CM. Regulation of the epithelial brush border Na+/H+ exchanger isoform 3 stably expressed in fibroblasts by fibroblast growth factor and phorbol esters is not through changes in phosphorylation of the exchanger. J Biol Chem 1997; 272: 18,473-18,480.
    • (1997) J Biol Chem , vol.272 , pp. 18473-18480
    • Yip, J.W.1    Ko, W.H.2    Viberti, G.3    Huganir, R.L.4    Donowitz, M.5    Tse, C.M.6
  • 194
    • 0034529158 scopus 로고    scopus 로고
    • Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton
    • Szaszi K, Grinstein S, Orlowski J, Kapus A. Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton. Cell Physiol Biochem 2000; 10:265-272.
    • (2000) Cell Physiol Biochem , vol.10 , pp. 265-272
    • Szaszi, K.1    Grinstein, S.2    Orlowski, J.3    Kapus, A.4
  • 195
    • 0031055464 scopus 로고    scopus 로고
    • ATP dependence of Na+/H+ exchange. Nucleotide specificity and assessment of the role of phospholipids
    • Demaurex N, Romanek RR, Orlowski J, Grinstein S. ATP dependence of Na+/H+ exchange. Nucleotide specificity and assessment of the role of phospholipids. J Gen Physiol 1997; 109:117-128.
    • (1997) J Gen Physiol , vol.109 , pp. 117-128
    • Demaurex, N.1    Romanek, R.R.2    Orlowski, J.3    Grinstein, S.4
  • 196
    • 0034631854 scopus 로고    scopus 로고
    • Intra-cellular pH regulation by Na(+)/H(+) exchange requires phosphatidylinositol 4,5-bisphosphate
    • Aharonovitz O, Zaun HC, Balla T, York JD, Orlowski J, Grinstein S. Intra-cellular pH regulation by Na(+)/H(+) exchange requires phosphatidylinositol 4,5-bisphosphate. J Cell Biol 2000; 150:213-224.
    • (2000) J Cell Biol , vol.150 , pp. 213-224
    • Aharonovitz, O.1    Zaun, H.C.2    Balla, T.3    York, J.D.4    Orlowski, J.5    Grinstein, S.6
  • 197
    • 0030021831 scopus 로고    scopus 로고
    • Distinct structural domains confer cAMP sensitivity and ATP dependence to the Na+/H+ exchanger NHE3 isoform
    • Cabado AG, Yu FH, Kapus A, Lukacs G, Grinstein S, Orlowski J. Distinct structural domains confer cAMP sensitivity and ATP dependence to the Na+/H+ exchanger NHE3 isoform. J Biol Chem 1996; 271:3509-3590.
    • (1996) J Biol Chem , vol.271 , pp. 3509-3590
    • Cabado, A.G.1    Yu, F.H.2    Kapus, A.3    Lukacs, G.4    Grinstein, S.5    Orlowski, J.6
  • 198
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gß
    • Huang CL, Feng S, Hilgemann DW. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gß. Nature 1998; 391:803-806.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 199
    • 0033580827 scopus 로고    scopus 로고
    • Specific association of megalin and the Na+/H+ exchanger isoform NHE3 in the proximal tubule
    • Biemesderfer D, Nagy T, DeGray B, Aronson PS. Specific association of megalin and the Na+/H+ exchanger isoform NHE3 in the proximal tubule. J Biol Chem 1999; 274:17,518-17,524.
    • (1999) J Biol Chem , vol.274 , pp. 17518-17524
    • Biemesderfer, D.1    Nagy, T.2    DeGray, B.3    Aronson, P.S.4
  • 200
    • 0035971106 scopus 로고    scopus 로고
    • Active (9.6S) and inactive (21S) oligomers of NHE3 in distinct microdomains of the renal brush border
    • Biemesderfer D, DeGray B, Aronson PS. Active (9.6S) and inactive (21S) oligomers of NHE3 in distinct microdomains of the renal brush border. J Biol Chem. 2001; 276:10161-10167.
    • (2001) J Biol Chem , vol.276 , pp. 10161-10167
    • Biemesderfer, D.1    DeGray, B.2    Aronson, P.S.3
  • 201
    • 0024442896 scopus 로고
    • Parathyroid hormone-induced translocation of Na/H antiporters in rat proximal tubules
    • Hensley CB, Bradley ME, Mircheff AK. Parathyroid hormone-induced translocation of Na/H antiporters in rat proximal tubules. Am J Physiol 1989; 257:C637-C642.
    • (1989) Am J Physiol , vol.257 , pp. C637-C642
    • Hensley, C.B.1    Bradley, M.E.2    Mircheff, A.K.3
  • 203
    • 0033852354 scopus 로고    scopus 로고
    • Acid incubation causes exocytotic insertion of NHE3 into the apical membrane of OK cells
    • Yang X, Amemiya M, Peng Y, Moe, OW, Priesig PA, Alpern RJ. Acid incubation causes exocytotic insertion of NHE3 into the apical membrane of OK cells. Am J Physiol 2000; 279:C410-C419.
    • (2000) Am J Physiol , vol.279 , pp. C410-C419
    • Yang, X.1    Amemiya, M.2    Peng, Y.3    Moe, O.W.4    Priesig, P.A.5    Alpern, R.J.6
  • 206
    • 0032516852 scopus 로고    scopus 로고
    • Endosomal recycling of the Na+/H+ exchanger NHE3 isoform is regulated by the phos-phatidylinositol 3-kinase pathway
    • Kurashima K, Szabo EZ, Lukacs G, Orlowski J, Grinstein S. Endosomal recycling of the Na+/H+ exchanger NHE3 isoform is regulated by the phos-phatidylinositol 3-kinase pathway. J Biol Chem 1998; 273:20,828-20,836.
    • (1998) J Biol Chem , vol.273 , pp. 20828-20836
    • Kurashima, K.1    Szabo, E.Z.2    Lukacs, G.3    Orlowski, J.4    Grinstein, S.5
  • 207
    • 0034728348 scopus 로고    scopus 로고
    • C-terminal domains of Na(+)/H(+) exchanger isoform 3 are involved in the basal and serum-stimulated membrane trafficking of the exchanger
    • Akhter S, Cavet ME, Tse CM, Donowitz M. C-terminal domains of Na(+)/H(+) exchanger isoform 3 are involved in the basal and serum-stimulated membrane trafficking of the exchanger. Biochemistry 2000; 39:1990-2000.
    • (2000) Biochemistry , vol.39 , pp. 1990-2000
    • Akhter, S.1    Cavet, M.E.2    Tse, C.M.3    Donowitz, M.4
  • 208
    • 0034677953 scopus 로고    scopus 로고
    • Basic fibroblast growth factor stimulates surface expression and activity of Na+/H+ exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase
    • Janecki AJ, Janecki M, Akhter S, Donowitz M. Basic fibroblast growth factor stimulates surface expression and activity of Na+/H+ exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase. J Biol Chem 2000; 275:8133-8142.
    • (2000) J Biol Chem , vol.275 , pp. 8133-8142
    • Janecki, A.J.1    Janecki, M.2    Akhter, S.3    Donowitz, M.4
  • 209
    • 0033537928 scopus 로고    scopus 로고
    • Proline-rich motifs of the Na+/H+ exchanger 2 isoform. Binding of Src homology domain 3 and role in apical targeting in epithelia
    • Chow CW, Woodside M, Demaurex N, Yu FH, Plant P, Rotin D, Grinstein S, Orlowski J. Proline-rich motifs of the Na+/H+ exchanger 2 isoform. Binding of Src homology domain 3 and role in apical targeting in epithelia. J Biol Chem 1999; 74:10,481-10,488.
    • (1999) J Biol Chem , vol.74 , pp. 10481-10488
    • Chow, C.W.1    Woodside, M.2    Demaurex, N.3    Yu, F.H.4    Plant, P.5    Rotin, D.6    Grinstein, S.7    Orlowski, J.8
  • 210
    • 0028866025 scopus 로고
    • Chronic regulation of the proximal tubular Na/H antiporter: From HCO3 to SRC
    • Alpern RJ, Moe OW, Preisig PA. Chronic regulation of the proximal tubular Na/H antiporter: from HCO3 to SRC. Kidney Int 1995; 48:1386-1396.
    • (1995) Kidney Int , vol.48 , pp. 1386-1396
    • Alpern, R.J.1    Moe, O.W.2    Preisig, P.A.3
  • 211
    • 0030787309 scopus 로고    scopus 로고
    • Na+/H+ exchanger subtypes in the renal tubule: Function and regulation in physiology and disease
    • Paillard M. Na+/H+ exchanger subtypes in the renal tubule: function and regulation in physiology and disease. Exp Nephrol 1997; 5:277-284.
    • (1997) Exp Nephrol , vol.5 , pp. 277-284
    • Paillard, M.1
  • 213
    • 0031029526 scopus 로고    scopus 로고
    • Chronic metabolic acidosis enhances NHE-3 protein abundance and transport activity in the rat thick ascending limb by increasing NHE-3 mRNA
    • Laghmani K, Borensztein P, Ambühl P, Froissart M, Bichara M, Moe OW, Alpern RJ, Paillard M. Chronic metabolic acidosis enhances NHE-3 protein abundance and transport activity in the rat thick ascending limb by increasing NHE-3 mRNA. J Clin Invest 1997; 99:24-30.
    • (1997) J Clin Invest , vol.99 , pp. 24-30
    • Laghmani, K.1    Borensztein, P.2    Ambühl, P.3    Froissart, M.4    Bichara, M.5    Moe, O.W.6    Alpern, R.J.7    Paillard, M.8
  • 215
    • 0032896825 scopus 로고    scopus 로고
    • Incubation of OKP cells in low-K+ media increases NHE3 activity after early decrease in intracellular pH
    • Amemiya M, Tabei K, Kusano E, Asano Y, Alpern RJ. Incubation of OKP cells in low-K+ media increases NHE3 activity after early decrease in intracellular pH. Am J Physiol 1999; 276:C711-C716.
    • (1999) Am J Physiol , vol.276 , pp. C711-C716
    • Amemiya, M.1    Tabei, K.2    Kusano, E.3    Asano, Y.4    Alpern, R.J.5
  • 218
    • 0025966286 scopus 로고
    • Exclusion of the Na+/H+ antiporter as a candidate gene in human essential hypertension
    • Lifton RP, Hunt SC, Williams RR, Pouyssegur J, Lalouel JM. Exclusion of the Na+/H+ antiporter as a candidate gene in human essential hypertension. Hypertension 1991; 17:8-14.
    • (1991) Hypertension , vol.17 , pp. 8-14
    • Lifton, R.P.1    Hunt, S.C.2    Williams, R.R.3    Pouyssegur, J.4    Lalouel, J.M.5
  • 221
    • 0032830932 scopus 로고    scopus 로고
    • Targeted disruption of the Nhe1 gene prevents muscarinic agonist-induced up-regulation of Na(+)/H(+) exchange in mouse parotid acinar cells
    • Evans RL, Bell SM, Schultheis PJ, Shull GE, Melvin JE. Targeted disruption of the Nhe1 gene prevents muscarinic agonist-induced up-regulation of Na(+)/H(+) exchange in mouse parotid acinar cells. J Biol Chem 1999; 274:29,025-29,030.
    • (1999) J Biol Chem , vol.274 , pp. 29025-29030
    • Evans, R.L.1    Bell, S.M.2    Schultheis, P.J.3    Shull, G.E.4    Melvin, J.E.5
  • 228
    • 0024534816 scopus 로고
    • Structure and function of the red blood cell anion transport system
    • Jennings ML. Structure and function of the red blood cell anion transport system. Annu Rev Biophys Biochem Chem 1989; 18:397-430.
    • (1989) Annu Rev Biophys Biochem Chem , vol.18 , pp. 397-430
    • Jennings, M.L.1
  • 229
    • 0024595839 scopus 로고
    • Arginine vasopressin enhances pHi regulation in the presence of HCO3- by stimulating three acid-base transport systems
    • Ganz MB, Boyarsky G, Sterzel RB, Boron WF. Arginine vasopressin enhances pHi regulation in the presence of HCO3- by stimulating three acid-base transport systems. Nature 1989; 337:648-651.
    • (1989) Nature , vol.337 , pp. 648-651
    • Ganz, M.B.1    Boyarsky, G.2    Sterzel, R.B.3    Boron, W.F.4
  • 230
    • 0022924213 scopus 로고
    • Anion exchange in sheep Purkinje fibres
    • Vaughn-Jones RD. Anion exchange in sheep Purkinje fibres. J Physiol 1986; 379:377-406.
    • (1986) J Physiol , vol.379 , pp. 377-406
    • Vaughn-Jones, R.D.1
  • 231
    • 0024453572 scopus 로고
    • Rapid hypertonic cell volume regulation in the perfused inner medullary collecting duct
    • Sun A, Hebert SC. Rapid hypertonic cell volume regulation in the perfused inner medullary collecting duct. Kidney Int 1989; 36(5):831-842.
    • (1989) Kidney Int , vol.36 , Issue.5 , pp. 831-842
    • Sun, A.1    Hebert, S.C.2
  • 232
    • 0025690859 scopus 로고
    • Molecular biology of the anion exchanger gene family
    • Kopito RR. Molecular biology of the anion exchanger gene family. Int Rev Cytol 1990; 123:177-199.
    • (1990) Int Rev Cytol , vol.123 , pp. 177-199
    • Kopito, R.R.1
  • 233
    • 0020620336 scopus 로고
    • Anion dependence of rabbit medullary collecting duct acidification
    • Stone DK, Seldin DW, Kokko JP, Jacobson HR. Anion dependence of rabbit medullary collecting duct acidification. J Clin Invest 1983; 71:1505-1508.
    • (1983) J Clin Invest , vol.71 , pp. 1505-1508
    • Stone, D.K.1    Seldin, D.W.2    Kokko, J.P.3    Jacobson, H.R.4
  • 234
    • 0024206665 scopus 로고
    • Fluorescent characterization of collecting duct cells: A second H+-secreting type
    • Schwartz GJ, Satlin LM, Bergmann JE. Fluorescent characterization of collecting duct cells: a second H+-secreting type. Am J Physiol 1988; 255:F1003-F1014.
    • (1988) Am J Physiol , vol.255 , pp. F1003-F1014
    • Schwartz, G.J.1    Satlin, L.M.2    Bergmann, J.E.3
  • 235
    • 0022353710 scopus 로고
    • Bicarbonate secretion and chloride absorption by rabbit cortical collecting ducts. Role of chloride/bicarbonate exchange
    • Star RA, Burg MB, Knepper MA. Bicarbonate secretion and chloride absorption by rabbit cortical collecting ducts. Role of chloride/bicarbonate exchange. J Clin Invest 1985; 76:1123-1130.
    • (1985) J Clin Invest , vol.76 , pp. 1123-1130
    • Star, R.A.1    Burg, M.B.2    Knepper, M.A.3
  • 236
    • 0022411389 scopus 로고
    • Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney
    • Drenckhahn D, Schluter K, Allen DP, Bennett V. Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney. Science 1985; 230:1287-1289.
    • (1985) Science , vol.230 , pp. 1287-1289
    • Drenckhahn, D.1    Schluter, K.2    Allen, D.P.3    Bennett, V.4
  • 237
    • 0022489887 scopus 로고
    • Two types of collecting duct mitochondrial-rich cells: Lectin and band 3 cytochemistry
    • Schuster VL, Bonsib SM, Jennings ML. Two types of collecting duct mitochondrial-rich cells: lectin and band 3 cytochemistry. Am J Physiol 1986; 251:C347-C355.
    • (1986) Am J Physiol , vol.251 , pp. C347-C355
    • Schuster, V.L.1    Bonsib, S.M.2    Jennings, M.L.3
  • 238
    • 0023637333 scopus 로고
    • Immunochemical characterization of a band-3 like anion exchanger in collecting duct of human kidney
    • Wagner S, Vogel R, Lietzke R, Koob R, Drenckkahn D. Immunochemical characterization of a band-3 like anion exchanger in collecting duct of human kidney. Am J Physiol 1987; 253:F213-F221.
    • (1987) Am J Physiol , vol.253 , pp. F213-F221
    • Wagner, S.1    Vogel, R.2    Lietzke, R.3    Koob, R.4    Drenckkahn, D.5
  • 239
    • 0023793187 scopus 로고
    • Immunocyto-chemical localization of band 3 protein in the rat collecting duct
    • Verlander JW, Madsen KM, Low PS, Allen DP, Tisher CC. Immunocyto-chemical localization of band 3 protein in the rat collecting duct. Am J Physiol 1988; 255:F115-F125.
    • (1988) Am J Physiol , vol.255 , pp. F115-F125
    • Verlander, J.W.1    Madsen, K.M.2    Low, P.S.3    Allen, D.P.4    Tisher, C.C.5
  • 240
    • 0028148539 scopus 로고
    • Differential expression of AE1 in renal -secreting and reabsorbing intercalated cells
    • Fejes-Toth G, Chen WR, Rusvai E, Moser T, Naray-Nejes-Toth A. Differential expression of AE1 in renal -secreting and reabsorbing intercalated cells. J Biol Chem 1994; 269:26,717-26,721.
    • (1994) J Biol Chem , vol.269 , pp. 26717-26721
    • Fejes-Toth, G.1    Chen, W.R.2    Rusvai, E.3    Moser, T.4    Naray-Nejes-Toth, A.5
  • 243
    • 0031779780 scopus 로고    scopus 로고
    • Immunolocalization and tissue-specific splicing of AE2 anion exchanger in mouse kidney
    • Stuart-Tilley AK, Shmukler BE, Brown D, Alper SL. Immunolocalization and tissue-specific splicing of AE2 anion exchanger in mouse kidney. J Am Soc Nephrol 1998; 9:946-959.
    • (1998) J Am Soc Nephrol , vol.9 , pp. 946-959
    • Stuart-Tilley, A.K.1    Shmukler, B.E.2    Brown, D.3    Alper, S.L.4
  • 244
    • 0025999029 scopus 로고
    • Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line
    • Lee BS, Gunn RB, Kopito RR. Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line. J Biol Chem 1991; 266:11,448-11,454.
    • (1991) J Biol Chem , vol.266 , pp. 11448-11454
    • Lee, B.S.1    Gunn, R.B.2    Kopito, R.R.3
  • 245
    • 0028500377 scopus 로고
    • PHi serum regulate AE2-mediated exchange in CHOP cells of defined transient transfection status
    • Jiang L, Stuart-Tilley A, Parkash J, Alper SL. pHi serum regulate AE2-mediated exchange in CHOP cells of defined transient transfection status. Am J Physiol 1994; 267:C845-C856.
    • (1994) Am J Physiol , vol.267 , pp. C845-C856
    • Jiang, L.1    Stuart-Tilley, A.2    Parkash, J.3    Alper, S.L.4
  • 246
  • 247
    • 0028888516 scopus 로고
    • Hypertonic activation of AE2 anion exchanger in Xenopus oocytes via NHE-mediated intracellular alkalinization
    • Humphreys BD, Jiang L, Chernova MN, Alper SL. Hypertonic activation of AE2 anion exchanger in Xenopus oocytes via NHE-mediated intracellular alkalinization. Am J Physiol 1995; 268:C201-C209.
    • (1995) Am J Physiol , vol.268 , pp. C201-C209
    • Humphreys, B.D.1    Jiang, L.2    Chernova, M.N.3    Alper, S.L.4
  • 248
    • 0028298801 scopus 로고
    • Band 3 protein: Structure, flexibility, and function
    • Wang DN. Band 3 protein: structure, flexibility, and function. FEBS Lett 1994; 346:26-31.
    • (1994) FEBS Lett , vol.346 , pp. 26-31
    • Wang, D.N.1
  • 249
    • 0030278948 scopus 로고    scopus 로고
    • Band 3 protein: Physiology, function and structure
    • Hamasaki N, Okubo K. Band 3 protein: physiology, function and structure. Mol Cell Biol 1996; 42:1025-1039.
    • (1996) Mol Cell Biol , vol.42 , pp. 1025-1039
    • Hamasaki, N.1    Okubo, K.2
  • 250
    • 0031466796 scopus 로고    scopus 로고
    • The structure and function of Band 3(AE1): Recent developments
    • Tanner MJA. The structure and function of Band 3(AE1): recent developments. Mol Membr Biol 1997; 14:155-165.
    • (1997) Mol Membr Biol , vol.14 , pp. 155-165
    • Tanner, M.J.A.1
  • 251
    • 0032452006 scopus 로고    scopus 로고
    • Anion exchangers in the red cell and beyond
    • Casey JR, Reithmeier RAF. Anion exchangers in the red cell and beyond. Biochem Cell Biol 1998; 76:709-713.
    • (1998) Biochem Cell Biol , vol.76 , pp. 709-713
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 252
    • 0027740329 scopus 로고
    • Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus
    • Kollert-Jons A, Wagner S, Hubner S, Appelhans H, Drenckhahn D. Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus. Am J Physiol 1993; 265:F813-F821.
    • (1993) Am J Physiol , vol.265 , pp. F813-F821
    • Kollert-Jons, A.1    Wagner, S.2    Hubner, S.3    Appelhans, H.4    Drenckhahn, D.5
  • 253
    • 0028065446 scopus 로고
    • The structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene
    • Schofield AE, Martin PG, Spillett D, Tanner MJ. The structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene. Blood 1994; 84:2000-2012.
    • (1994) Blood , vol.84 , pp. 2000-2012
    • Schofield, A.E.1    Martin, P.G.2    Spillett, D.3    Tanner, M.J.4
  • 254
    • 0029812755 scopus 로고    scopus 로고
    • Mapping of ankyrin binding determinants on the erythroid anion exchanger, AE1
    • Ding Y, Kobayashi S, Kopito R. Mapping of ankyrin binding determinants on the erythroid anion exchanger, AE1. J Biol Chem 1996; 271:22, 494-22,498.
    • (1996) J Biol Chem , vol.271 , pp. 22494-22498
    • Ding, Y.1    Kobayashi, S.2    Kopito, R.3
  • 255
    • 0026689374 scopus 로고
    • Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681
    • Jennings ML, Smith JS. Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681. J Biol Chem 1992; 267:13,964-13,971.
    • (1992) J Biol Chem , vol.267 , pp. 13964-13971
    • Jennings, M.L.1    Smith, J.S.2
  • 256
    • 0032575609 scopus 로고    scopus 로고
    • Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger
    • Tang XB, Fujinaga J, Kopito R, Casey JR. Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger. J Biol Chem 1998; 273:22,545-22,553.
    • (1998) J Biol Chem , vol.273 , pp. 22545-22553
    • Tang, X.B.1    Fujinaga, J.2    Kopito, R.3    Casey, J.R.4
  • 257
    • 0033561328 scopus 로고    scopus 로고
    • Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined scanning and insertional Bglycosylation mutagenesis
    • Popov M, Li J, Reithmeier RA. Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined scanning and insertional Bglycosylation mutagenesis. Biochem J 1999; 339:269-279.
    • (1999) Biochem J , vol.339 , pp. 269-279
    • Popov, M.1    Li, J.2    Reithmeier, R.A.3
  • 258
    • 0031870450 scopus 로고    scopus 로고
    • Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer
    • Blackman SM, Piston DW, Beth AH. Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer. Biophys J 1998; 75:1117-1130.
    • (1998) Biophys J , vol.75 , pp. 1117-1130
    • Blackman, S.M.1    Piston, D.W.2    Beth, A.H.3
  • 259
    • 0033614828 scopus 로고    scopus 로고
    • AE2 anion exchanger polypeptide is a homooligomer in pig gastric membranes: A chemical cross-linking study
    • Zolotarev AS, Shmukler BE, Alper SL. AE2 anion exchanger polypeptide is a homooligomer in pig gastric membranes: a chemical cross-linking study. Biochemistry 1999; 38:8521-8531.
    • (1999) Biochemistry , vol.38 , pp. 8521-8531
    • Zolotarev, A.S.1    Shmukler, B.E.2    Alper, S.L.3
  • 260
    • 0027155339 scopus 로고
    • Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals
    • Dolder M, Walz T, Hefti A, Engel A. Human erythrocyte band 3. Solubilization and reconstitution into two-dimensional crystals. J Mol Biol 1993; 231:119-132.
    • (1993) J Mol Biol , vol.231 , pp. 119-132
    • Dolder, M.1    Walz, T.2    Hefti, A.3    Engel, A.4
  • 261
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3
    • Wang DN, Sarabia VE, Reithmeier RA, Kuhlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. EMBO J 1994; 13:3230-3235.
    • (1994) EMBO J , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.3    Kuhlbrandt, W.4
  • 262
    • 0027266988 scopus 로고
    • Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane
    • Wang DN, Kuhlbrandt W, Sarabia VE, Reithmeier RA. Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane. EMBO J 1993; 12:2233-2339.
    • (1993) EMBO J , vol.12 , pp. 2233-2339
    • Wang, D.N.1    Kuhlbrandt, W.2    Sarabia, V.E.3    Reithmeier, R.A.4
  • 263
    • 0027999835 scopus 로고
    • Kinetic evidence for ternary complex formation and allosteric interactions in chloride and stilbene-disulfonate binding to band 3
    • Salhany JM, Sloan RL, Cordes KA, Schopfer LM. Kinetic evidence for ternary complex formation and allosteric interactions in chloride and stilbene-disulfonate binding to band 3. Biochemistry 1994; 33:11,909-11,916.
    • (1994) Biochemistry , vol.33 , pp. 11909-11916
    • Salhany, J.M.1    Sloan, R.L.2    Cordes, K.A.3    Schopfer, L.M.4
  • 264
    • 0030279607 scopus 로고    scopus 로고
    • Allosteric effects in stilbene disulphonate binding to band 3 protein (AE1)
    • Salhany JM. Allosteric effects in stilbene disulphonate binding to band 3 protein (AE1). Mol Cell Biol 1996; 42:1065-1096.
    • (1996) Mol Cell Biol , vol.42 , pp. 1065-1096
    • Salhany, J.M.1
  • 265
    • 0029920948 scopus 로고    scopus 로고
    • The cytoplasmic and transmembrane domains of AE2 both contribute to regulation of anion exchange by pH
    • Zhang Y, Chernova MN, Stuart-Tilley AK, Jiang L, Alper SL. The cytoplasmic and transmembrane domains of AE2 both contribute to regulation of anion exchange by pH. J Biol Chem 1996; 271:5741-5749.
    • (1996) J Biol Chem , vol.271 , pp. 5741-5749
    • Zhang, Y.1    Chernova, M.N.2    Stuart-Tilley, A.K.3    Jiang, L.4    Alper, S.L.5
  • 266
    • 0028882542 scopus 로고
    • A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2
    • Sekler I, Lo RS, Kopito RR. A conserved glutamate is responsible for ion selectivity and pH dependence of the mammalian anion exchangers AE1 and AE2. J Biol Chem 1995; 270:28,751-28,758.
    • (1995) J Biol Chem , vol.270 , pp. 28751-28758
    • Sekler, I.1    Lo, R.S.2    Kopito, R.R.3
  • 267
    • 0029866149 scopus 로고    scopus 로고
    • Augments net acid secretion by a ouabain-sensitive mechanism in isolated perfused inner medullary collecting ducts
    • Wall SM. augments net acid secretion by a ouabain-sensitive mechanism in isolated perfused inner medullary collecting ducts. Am J Physiol 1996; 270:F432-F439.
    • (1996) Am J Physiol , vol.270 , pp. F432-F439
    • Wall, S.M.1
  • 268
    • 0033383895 scopus 로고    scopus 로고
    • Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis
    • Huber S, Asan E, Jons T, Kerscher C, Puschel B, Drenckhahn D. Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis. Am J Physiol 1999; 277:F841-F849.
    • (1999) Am J Physiol , vol.277 , pp. F841-F849
    • Huber, S.1    Asan, E.2    Jons, T.3    Kerscher, C.4    Puschel, B.5    Drenckhahn, D.6
  • 269
    • 0026100301 scopus 로고
    • Rat kidney band 3 mRNA modulation in chronic respiratory acidosis
    • Da Silva JC Jr, Perrone RD, Johns CA, Madias NE. Rat kidney band 3 mRNA modulation in chronic respiratory acidosis. Am J Physiol 1991; 260:F204-F209.
    • (1991) Am J Physiol , vol.260 , pp. F204-F209
    • Da Silva, J.C.1    Perrone, R.D.2    Johns, C.A.3    Madias, N.E.4
  • 270
    • 0027419260 scopus 로고
    • Function and regulation of collecting duct intercalated cells
    • Schuster V. Function and regulation of collecting duct intercalated cells. Annu Rev Physiol 1993; 55:267-288.
    • (1993) Annu Rev Physiol , vol.55 , pp. 267-288
    • Schuster, V.1
  • 271
    • 0031896720 scopus 로고    scopus 로고
    • Regulation of AE2 mRNA expression in the cortical collecting duct by acid/base balance
    • Fejes-Toth G, Rusvai E, Cleaveland ES, Naray-Fejes-Toth A. Regulation of AE2 mRNA expression in the cortical collecting duct by acid/base balance. Am J Physiol 1998; 274:F596-F601.
    • (1998) Am J Physiol , vol.274 , pp. F596-F601
    • Fejes-Toth, G.1    Rusvai, E.2    Cleaveland, E.S.3    Naray-Fejes-Toth, A.4
  • 272
    • 0026775240 scopus 로고
    • Biogenesis and normal and abnormal red cell membrane skeletons
    • Hanspal M, Palek J. Biogenesis and normal and abnormal red cell membrane skeletons. Semin Hematol 1992; 29:305-325.
    • (1992) Semin Hematol , vol.29 , pp. 305-325
    • Hanspal, M.1    Palek, J.2
  • 273
    • 0029084972 scopus 로고
    • Genetic disorders of red cell membranes
    • Delauney. Genetic disorders of red cell membranes. FEBS Lett 1995; 369:34-37.
    • (1995) FEBS Lett , vol.369 , pp. 34-37
    • Delauney1
  • 274
    • 15844377239 scopus 로고    scopus 로고
    • Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation
    • Inaba M, Yawata A, Koshino I, Sato K, Takeuchi M, Takakuwa Y, Manno S, Yawata Y, Kanzaki A, Sakai J, Ban A, Ono K, Maede Y. Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation. J Clin Invest 1996; 97:1804-1817.
    • (1996) J Clin Invest , vol.97 , pp. 1804-1817
    • Inaba, M.1    Yawata, A.2    Koshino, I.3    Sato, K.4    Takeuchi, M.5    Takakuwa, Y.6    Manno, S.7    Yawata, Y.8    Kanzaki, A.9    Sakai, J.10    Ban, A.11    Ono, K.12    Maede, Y.13
  • 279
    • 0033638694 scopus 로고    scopus 로고
    • Atypical distal renal tubular acidosis confirmed by mutation analysis
    • Weber S, Soergel M, Jeck N, Konrad M. Atypical distal renal tubular acidosis confirmed by mutation analysis. Pediatr Nephrol 2000; 15:201-204.
    • (2000) Pediatr Nephrol , vol.15 , pp. 201-204
    • Weber, S.1    Soergel, M.2    Jeck, N.3    Konrad, M.4
  • 280
    • 0033017396 scopus 로고    scopus 로고
    • Autosomal dominant distal renal tubular acidosis and the AE1 gene
    • DuBose TD. Autosomal dominant distal renal tubular acidosis and the AE1 gene. Am J Kidney Dis 1999; 33:1190-1197.
    • (1999) Am J Kidney Dis , vol.33 , pp. 1190-1197
    • DuBose, T.D.1
  • 282
    • 0142064871 scopus 로고    scopus 로고
    • Structure-function relationships of band 3 variants
    • Bruce LJ, Tanner MJ. Structure-function relationships of band 3 variants. Cell Mol Biol 1996; 42:953-973.
    • (1996) Cell Mol Biol , vol.42 , pp. 953-973
    • Bruce, L.J.1    Tanner, M.J.2
  • 284
    • 0028027718 scopus 로고
    • The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal
    • Liu SC, Jarolim P, Rubin HL, Palek J, Amato D, Hassan K, Zaik M, Sapak P. The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal. Blood 1994; 84:3590-3591.
    • (1994) Blood , vol.84 , pp. 3590-3591
    • Liu, S.C.1    Jarolim, P.2    Rubin, H.L.3    Palek, J.4    Amato, D.5    Hassan, K.6    Zaik, M.7    Sapak, P.8
  • 285
    • 0027263968 scopus 로고
    • Molecular characterization of the band 3 protein from Southeast Asian ovalocytes
    • Sarabia VE, Casey JR, Reithmeier RA. Molecular characterization of the band 3 protein from Southeast Asian ovalocytes. J Biol Chem 1993; 268:10,676-10,680.
    • (1993) J Biol Chem , vol.268 , pp. 10676-10680
    • Sarabia, V.E.1    Casey, J.R.2    Reithmeier, R.A.3
  • 286
    • 0029029602 scopus 로고
    • Molecular basis of altered red blood cell membrane properties in Southeast Asian ovalocytosis: Role of the mutant band 3 protein in band 3 oligomerization and retention by the membrane skeleton
    • Liu SC, Palek J, Yi SJ, Nichols PE, Derick LH, Chiou SS, Amato D, Corbett JD, Cho MR, Golan DE. Molecular basis of altered red blood cell membrane properties in Southeast Asian ovalocytosis: role of the mutant band 3 protein in band 3 oligomerization and retention by the membrane skeleton. Blood 1995; 86:349-358.
    • (1995) Blood , vol.86 , pp. 349-358
    • Liu, S.C.1    Palek, J.2    Yi, S.J.3    Nichols, P.E.4    Derick, L.H.5    Chiou, S.S.6    Amato, D.7    Corbett, J.D.8    Cho, M.R.9    Golan, D.E.10
  • 290
    • 0029825262 scopus 로고    scopus 로고
    • Hereditary spherocytosis: A review of the clinical and molecular aspects of the disease
    • Hassoun H, Palek J. Hereditary spherocytosis: a review of the clinical and molecular aspects of the disease. Blood Rev 1996; 10:129-147.
    • (1996) Blood Rev , vol.10 , pp. 129-147
    • Hassoun, H.1    Palek, J.2
  • 291
    • 0030766722 scopus 로고    scopus 로고
    • Incomplete distal renal tubular acidosis coinherited with a mutation in the band 3 (AE1) gene
    • Rysava R, Tesar V, Jirsa M, Brabec V, Jarolim P. Incomplete distal renal tubular acidosis coinherited with a mutation in the band 3 (AE1) gene. Nephrol Dial Transplant 1997; 12:1869-1867.
    • (1997) Nephrol Dial Transplant , vol.12 , pp. 1869-1867
    • Rysava, R.1    Tesar, V.2    Jirsa, M.3    Brabec, V.4    Jarolim, P.5
  • 292
    • 0020700008 scopus 로고
    • Intracellular pH regulation in the renal proximal tubule of the salamander. Basolateral HCO- transport
    • Boron WF, Boulpaep EL. Intracellular pH regulation in the renal proximal tubule of the salamander. Basolateral HCO- transport. J Gen Physiol 1983; 81:53-94.
    • (1983) J Gen Physiol , vol.81 , pp. 53-94
    • Boron, W.F.1    Boulpaep, E.L.2
  • 293
    • 0023162339 scopus 로고
    • The regulation of intracellular pH by identified glial cells and neurones in the central nervous system of the leech
    • Deitmer JW, Schlue WR. The regulation of intracellular pH by identified glial cells and neurones in the central nervous system of the leech. J Physiol 1987; 388:261-283.
    • (1987) J Physiol , vol.388 , pp. 261-283
    • Deitmer, J.W.1    Schlue, W.R.2
  • 294
    • 0026610840 scopus 로고
    • Na(+)-HCO3-symport in the sheep cardiac Purkinje fibre
    • Dart C, Vaughan-Jones RD. Na(+)-HCO3-symport in the sheep cardiac Purkinje fibre. J Physiol 1992; 451:365-385.
    • (1992) J Physiol , vol.451 , pp. 365-385
    • Dart, C.1    Vaughan-Jones, R.D.2
  • 295
    • 0017103272 scopus 로고
    • Role of chloride transport in regulation of intracellular pH
    • Russell JM, Boron WF. Role of chloride transport in regulation of intracellular pH. Nature 1976; 264:73-74.
    • (1976) Nature , vol.264 , pp. 73-74
    • Russell, J.M.1    Boron, W.F.2
  • 296
    • 0028971228 scopus 로고
    • K(+)- and HCO3(-)-dependent acid-base transport in squid giant axons
    • Hogan EM, Cohen MA, Boron WF. K(+)- and HCO3(-)-dependent acid-base transport in squid giant axons. J Gen Physiol 1995; 106:821-862.
    • (1995) J Gen Physiol , vol.106 , pp. 821-862
    • Hogan, E.M.1    Cohen, M.A.2    Boron, W.F.3
  • 297
    • 0032587119 scopus 로고    scopus 로고
    • Electrogenic Na+/HCO- cotransporters: Cloning and physiology
    • Romero MF, Boron WF. Electrogenic Na+/HCO- cotransporters: cloning and physiology. Annu Rev Physiol 1999; 61:699-723.
    • (1999) Annu Rev Physiol , vol.61 , pp. 699-723
    • Romero, M.F.1    Boron, W.F.2
  • 298
    • 0034637441 scopus 로고    scopus 로고
    • Cloning and characterization of a Na+-driven anion exchanger (NDAE1): A new transporter
    • Romero MF, Henry D, Nelson S, Harte PJ, Dillon AK, Sciortino. Cloning and characterization of a Na+-driven anion exchanger (NDAE1): a new transporter. J Biol Chem 2000; 275:24,552-24,559.
    • (2000) J Biol Chem , vol.275 , pp. 24552-24559
    • Romero, M.F.1    Henry, D.2    Nelson, S.3    Harte, P.J.4    Dillon, A.K.5    Sciortino6
  • 299
    • 0034634583 scopus 로고    scopus 로고
    • The Na+-driven exchanger. Cloning, tissue distribution, and functional characterization
    • Wang CZ, Yano H, Nagashima K, Seino S. The Na+-driven exchanger. Cloning, tissue distribution, and functional characterization. J Biol Chem 2000; 275:35,486-35,490.
    • (2000) J Biol Chem , vol.275 , pp. 35486-35490
    • Wang, C.Z.1    Yano, H.2    Nagashima, K.3    Seino, S.4
  • 300
    • 0022413879 scopus 로고
    • Mechanism of basolateral membrane H+/OH-/HCO- transport in the rat proximal convoluted tubule. A sodium-coupled electrogenic process
    • Alpern RJ. Mechanism of basolateral membrane H+/OH-/HCO- transport in the rat proximal convoluted tubule. A sodium-coupled electrogenic process. J Gen Physiol 1985; 86:613-636.
    • (1985) J Gen Physiol , vol.86 , pp. 613-636
    • Alpern, R.J.1
  • 301
    • 0022826756 scopus 로고
    • Electrogenic sodium/bicarbonate cotransport in rabbit renal cortical basolateral membrane vesicles
    • Akiba T, Alpern RJ, Eveloff J, Calamina J, Warnock DG. Electrogenic sodium/bicarbonate cotransport in rabbit renal cortical basolateral membrane vesicles. J Clin Invest 1986; 78:1472-1478.
    • (1986) J Clin Invest , vol.78 , pp. 1472-1478
    • Akiba, T.1    Alpern, R.J.2    Eveloff, J.3    Calamina, J.4    Warnock, D.G.5
  • 302
    • 0023267793 scopus 로고
    • Stoichiometry of Na+-HCO- cotran-sport in basolateral membrane vesicles isolated from rabbit renal cortex
    • Soleimani M, Grassi SM, Aronson PS. Stoichiometry of Na+-HCO- cotran-sport in basolateral membrane vesicles isolated from rabbit renal cortex. J Clin Invest 1987; 79:1276-1280.
    • (1987) J Clin Invest , vol.79 , pp. 1276-1280
    • Soleimani, M.1    Grassi, S.M.2    Aronson, P.S.3
  • 303
    • 0024452286 scopus 로고
    • Ionic mechanism of cotransport in rabbit renal basolateral membrane vesicles
    • Soleimani M, Aronson PS. Ionic mechanism of cotransport in rabbit renal basolateral membrane vesicles. J Biol Chem 1989; 264: 18,302-18,308.
    • (1989) J Biol Chem , vol.264 , pp. 18302-18308
    • Soleimani, M.1    Aronson, P.S.2
  • 304
    • 0032916918 scopus 로고    scopus 로고
    • Immu-nolocalization of the electrogenic cotransporter in mammalian and amphibian kidney
    • Schmitt BM, Biemesderfer D, Romero MF, Boulpaep EL, Boron WF. Immu-nolocalization of the electrogenic cotransporter in mammalian and amphibian kidney. Am J Physiol 1999; 276:F27-F38.
    • (1999) Am J Physiol , vol.276 , pp. F27-F38
    • Schmitt, B.M.1    Biemesderfer, D.2    Romero, M.F.3    Boulpaep, E.L.4    Boron, W.F.5
  • 306
    • 0034094786 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of NBC3 sodium-bicarbonate cotransporter in rat kidney
    • Kwon TH, Pushkin A, Abuladze N, Nielsen S, Kurtz I. Immunoelectron microscopic localization of NBC3 sodium-bicarbonate cotransporter in rat kidney. Am J Physiol 2000; 278:F327-F336.
    • (2000) Am J Physiol , vol.278 , pp. F327-F336
    • Kwon, T.H.1    Pushkin, A.2    Abuladze, N.3    Nielsen, S.4    Kurtz, I.5
  • 308
    • 85128037151 scopus 로고    scopus 로고
    • The stoichiometry of the sodium bicarbonate cotransporter is mouse pancreatic cells is [abstr]
    • Gross EZ, Abuladze N, Pushkin A, Kurtz I, Cotton CU. The stoichiometry of the sodium bicarbonate cotransporter is mouse pancreatic cells is [abstr]. J Am Soc Nephrol 2000; 11:4A.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 4A
    • Gross, E.Z.1    Abuladze, N.2    Pushkin, A.3    Kurtz, I.4    Cotton, C.U.5
  • 310
    • 0032750546 scopus 로고    scopus 로고
    • Cation and voltage dependence of rat kidney electrogenic cotransporter, rkNBC, expressed in oocytes
    • Sciortino CM, Romero MF. Cation and voltage dependence of rat kidney electrogenic cotransporter, rkNBC, expressed in oocytes. Am J Physiol 1999; 277:F611-F623.
    • (1999) Am J Physiol , vol.277 , pp. F611-F623
    • Sciortino, C.M.1    Romero, M.F.2
  • 311
    • 0034063098 scopus 로고    scopus 로고
    • Extracellular HCO (3) (-) dependence of electrogenic Na/HCO(3) cotransporters cloned from salamander and rat kidney
    • Grichtchenko II, Romero MF, Boron WF. Extracellular HCO (3) (-) dependence of electrogenic Na/HCO(3) cotransporters cloned from salamander and rat kidney. J Gen Physiol 2000; 115:533-546.
    • (2000) J Gen Physiol , vol.115 , pp. 533-546
    • Grichtchenko, I.I.1    Romero, M.F.2    Boron, W.F.3
  • 312
    • 0025813253 scopus 로고
    • Cation specificity and modes of the cotransport in renal basolateral membrane vesicles
    • Soleimani M, Lesoine GA, Bergman JA, Aronson PS. Cation specificity and modes of the cotransport in renal basolateral membrane vesicles. J Biol Chem 1991; 266:8706-8710.
    • (1991) J Biol Chem , vol.266 , pp. 8706-8710
    • Soleimani, M.1    Lesoine, G.A.2    Bergman, J.A.3    Aronson, P.S.4
  • 313
    • 0023395450 scopus 로고
    • Parallel adaptation of the rabbit renal cortical sodium/proton antiporter and sodium/bicarbonate cotransporter in metabolic acidosis and alkalosis
    • Akiba T, Rocco VK, Warnock DG. Parallel adaptation of the rabbit renal cortical sodium/proton antiporter and sodium/bicarbonate cotransporter in metabolic acidosis and alkalosis. J Clin Invest 1987; 80:308-315.
    • (1987) J Clin Invest , vol.80 , pp. 308-315
    • Akiba, T.1    Rocco, V.K.2    Warnock, D.G.3
  • 314
    • 0023689705 scopus 로고
    • Chronic metabolic acidosis causes an adaptation in the apical membrane Na/H antiporter and basolateral membrane Na(IICO3)3 symporter in the rat proximal convoluted tubule
    • Preisig PA, Alpern RJ. Chronic metabolic acidosis causes an adaptation in the apical membrane Na/H antiporter and basolateral membrane Na(IICO3)3 symporter in the rat proximal convoluted tubule. J Clin Invest 1988; 82:1445-1453.
    • (1988) J Clin Invest , vol.82 , pp. 1445-1453
    • Preisig, P.A.1    Alpern, R.J.2
  • 315
    • 0026637079 scopus 로고
    • Effect of in vitro metabolic acidosis on luminal Na+/H+ exchange and basolateral cotransport in rabbit kidney proximal tubules
    • Soleimani M, Bizal GL, McKinney TD, Hattabaugh YJ. Effect of in vitro metabolic acidosis on luminal Na+/H+ exchange and basolateral cotransport in rabbit kidney proximal tubules. J Clin Invest 1992; 90:211-218.
    • (1992) J Clin Invest , vol.90 , pp. 211-218
    • Soleimani, M.1    Bizal, G.L.2    McKinney, T.D.3    Hattabaugh, Y.J.4
  • 316
    • 0030709484 scopus 로고    scopus 로고
    • Functional upregulation of H+-ATPase by lethal acid stress in cultured inner medullary collecting duct cells
    • Amlal H, Wang Z, Soleimani M. Functional upregulation of H+-ATPase by lethal acid stress in cultured inner medullary collecting duct cells. Am J Physiol 1997; 273:C1194-C1205.
    • (1997) Am J Physiol , vol.273 , pp. C1194-C1205
    • Amlal, H.1    Wang, Z.2    Soleimani, M.3
  • 317
    • 0025169229 scopus 로고
    • Potassium depletion increases luminal Na+/H+ exchange and basolateral cotransport in rat renal cortex
    • Soleimani M, Bergman JA, Hosford MA, McKinney TD. Potassium depletion increases luminal Na+/H+ exchange and basolateral cotransport in rat renal cortex. J Clin Invest 1990; 86:1076-1083.
    • (1990) J Clin Invest , vol.86 , pp. 1076-1083
    • Soleimani, M.1    Bergman, J.A.2    Hosford, M.A.3    McKinney, T.D.4
  • 318
    • 0033830019 scopus 로고    scopus 로고
    • Potassium deprivation upregulates expression of renal basolateral Na(+)-HCO(3)(-) cotransporter (NBC-1)
    • Amlal H, Habo K, Soleimani M. Potassium deprivation upregulates expression of renal basolateral Na(+)-HCO(3)(-) cotransporter (NBC-1). Am J Physiol 2000; 279:F532-F543.
    • (2000) Am J Physiol , vol.279 , pp. F532-F543
    • Amlal, H.1    Habo, K.2    Soleimani, M.3
  • 319
    • 0033932697 scopus 로고    scopus 로고
    • Glucocorticoids enhance the expression of the basolateral cotransporter in renal proximal tubules
    • Ali R, Amlal H, Burnham CE, Soleimani M. Glucocorticoids enhance the expression of the basolateral cotransporter in renal proximal tubules. Kidney Int 2000; 57:1063-1071.
    • (2000) Kidney Int , vol.57 , pp. 1063-1071
    • Ali, R.1    Amlal, H.2    Burnham, C.E.3    Soleimani, M.4
  • 320
    • 0017737482 scopus 로고
    • Familial proximal tubular acidosis: A distinct disease entity
    • Brenes LG, Brenes JM, Hernandez MM. Familial proximal tubular acidosis: a distinct disease entity. Am J Med 1977; 63:244-252.
    • (1977) Am J Med , vol.63 , pp. 244-252
    • Brenes, L.G.1    Brenes, J.M.2    Hernandez, M.M.3
  • 321
    • 0018728201 scopus 로고
    • Congenital persistent proximal type renal tubular acidosis in two brothers
    • Winsnes RW, Monn E, Stokke O, Feyling T. Congenital persistent proximal type renal tubular acidosis in two brothers. Acta Pediatr Scand 1979; 68: 861-868.
    • (1979) Acta Pediatr Scand , vol.68 , pp. 861-868
    • Winsnes, R.W.1    Monn, E.2    Stokke, O.3    Feyling, T.4
  • 323
    • 0028107343 scopus 로고
    • Persistent isolated proximal renal tubular acidosis-a systemic disease with a distinct clinical entity
    • Igarashi T, Ishii T, Watanabe K, Hayakawa H, Horio K, Sone Y, Ohga K. Persistent isolated proximal renal tubular acidosis-a systemic disease with a distinct clinical entity. Pediatr Nephrol 1994; 8:70-71.
    • (1994) Pediatr Nephrol , vol.8 , pp. 70-71
    • Igarashi, T.1    Ishii, T.2    Watanabe, K.3    Hayakawa, H.4    Horio, K.5    Sone, Y.6    Ohga, K.7
  • 325
    • 84875134370 scopus 로고    scopus 로고
    • A nonsense mutation in the Na/HCO3 cotransporter gene (SLC4a4) in a patient with permanent isolated proximal renal tubular acidosis and bilateral glaucoma [abstr]
    • Igarashi T, Inatomi J, Sekine T, Takeshima Y, Yoshikaa N, Endou H. A nonsense mutation in the Na/HCO3 cotransporter gene (SLC4a4) in a patient with permanent isolated proximal renal tubular acidosis and bilateral glaucoma [abstr]. J Am Soc Nephrol 2000; 11:106A.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 106A
    • Igarashi, T.1    Inatomi, J.2    Sekine, T.3    Takeshima, Y.4    Yoshikaa, N.5    Endou, H.6
  • 326
    • 0024348912 scopus 로고
    • What is the underlying defect in patients with isolated, proximal renal tubular acidosis
    • Halperin ML, Kamel KS, Ethier JH, Magner PO. What is the underlying defect in patients with isolated, proximal renal tubular acidosis? Am J Nephrol 1989; 9:265-268.
    • (1989) Am J Nephrol , vol.9 , pp. 265-268
    • Halperin, M.L.1    Kamel, K.S.2    Ethier, J.H.3    Magner, P.O.4
  • 327
    • 0017751595 scopus 로고
    • Urinary values quantified by age groups in a healthy pediatric population
    • Thompson JA, Miles BS, Fennessey PV. Urinary values quantified by age groups in a healthy pediatric population. Clin Chem 1977; 23:1734-1738.
    • (1977) Clin Chem , vol.23 , pp. 1734-1738
    • Thompson, J.A.1    Miles, B.S.2    Fennessey, P.V.3
  • 328
    • 0000597157 scopus 로고
    • Roles and mechanisms of urinary buffer excretion
    • Hamm LL, Simon EE. Roles and mechanisms of urinary buffer excretion. Am J Physiol 1987; 22:F595-F605.
    • (1987) Am J Physiol , vol.22 , pp. F595-F605
    • Hamm, L.L.1    Simon, E.E.2
  • 329
    • 85128053707 scopus 로고
    • Urine, volume, and physio chemical data
    • In: Lenter C, ed. Bassel, Switzerland: Ciba-Geigy
    • Urine, volume, and physio chemical data. In: Lenter C, ed. Geigy Scientific Tables. Bassel, Switzerland: Ciba-Geigy, 1981:53-95.
    • (1981) Geigy Scientific Tables , pp. 53-95
  • 331
    • 0033844773 scopus 로고    scopus 로고
    • Molecular pharmacology of renal organic anion transporters
    • Van Aubel RA, Masereeuw R, Russel FG. Molecular pharmacology of renal organic anion transporters. Am J Physiol 2000; 279:F216-F232.
    • (2000) Am J Physiol , vol.279 , pp. F216-F232
    • Van Aubel, R.A.1    Masereeuw, R.2    Russel, F.G.3
  • 332
    • 0034784971 scopus 로고    scopus 로고
    • Physiological roles and regulation of mammalian sulfate transporters
    • Markovich D. Physiological roles and regulation of mammalian sulfate transporters. Physiol Rev 2001; 81:1499-1533.
    • (2001) Physiol Rev , vol.81 , pp. 1499-1533
    • Markovich, D.1
  • 333
    • 0020731756 scopus 로고
    • Citrate excretion: A window to renal metabolism
    • Simpson DP. Citrate excretion: a window to renal metabolism. Am J Physiol 1983; 244:F223-F234.
    • (1983) Am J Physiol , vol.244 , pp. F223-F234
    • Simpson, D.P.1
  • 334
    • 0031806539 scopus 로고    scopus 로고
    • Renal cortical mitochondrial aconitase is regulated in hypo- and hypercitraturia
    • Melnick JZ, Preisig PA, Moe OW, Srere P, Alpern RJ. Renal cortical mitochondrial aconitase is regulated in hypo- and hypercitraturia. Kidney Int 1998; 54:160-165.
    • (1998) Kidney Int , vol.54 , pp. 160-165
    • Melnick, J.Z.1    Preisig, P.A.2    Moe, O.W.3    Srere, P.4    Alpern, R.J.5
  • 336
    • 0022133563 scopus 로고
    • Transport of citrate across brush border membrane: Effect of dietary acid and alkali loading
    • Jenkins AD, Dousa TP, Smith LH. Transport of citrate across brush border membrane: effect of dietary acid and alkali loading. Am J Physiol 1985; 249:F590-F595.
    • (1985) Am J Physiol , vol.249 , pp. F590-F595
    • Jenkins, A.D.1    Dousa, T.P.2    Smith, L.H.3
  • 338
    • 0028957041 scopus 로고
    • Sequence and functional characterization of a renal sodium/ dicarboxylate cotransporter
    • Pajor AM. Sequence and functional characterization of a renal sodium/ dicarboxylate cotransporter. J Biol Chem 1995; 270:5779-5785.
    • (1995) J Biol Chem , vol.270 , pp. 5779-5785
    • Pajor, A.M.1
  • 339
    • 0029968824 scopus 로고    scopus 로고
    • Molecular cloning and functional expression ofa sodium-dicarboxy-late cotransporter from human kidney
    • Pajor AM. Molecular cloning and functional expression ofa sodium-dicarboxy-late cotransporter from human kidney. Am J Physiol 1996; 270:F642-F658.
    • (1996) Am J Physiol , vol.270 , pp. F642-F658
    • Pajor, A.M.1
  • 342
    • 0030870019 scopus 로고    scopus 로고
    • Expression cloning ofNaDC-2, an intestinal Na(+)- or Li(+)-dependent dicarboxylate transporter
    • Bai L, Pajor AM. Expression cloning ofNaDC-2, an intestinal Na(+)- or Li(+)-dependent dicarboxylate transporter. Am J Physiol 1997; 273:G267-G274.
    • (1997) Am J Physiol , vol.273 , pp. G267-G274
    • Bai, L.1    Pajor, A.M.2
  • 343
    • 0033524933 scopus 로고    scopus 로고
    • Primary structure and functional characteristics of a mammalian sodium-coupled high affinity dicarboxylate transporter
    • Kekuda R, Wang H, Huang W, Pajor AM, Leibach FH, Devoe LD, Prasad PD, Ganapathy V. Primary structure and functional characteristics of a mammalian sodium-coupled high affinity dicarboxylate transporter. J Biol Chem 1999; 274:3422-3429.
    • (1999) J Biol Chem , vol.274 , pp. 3422-3429
    • Kekuda, R.1    Wang, H.2    Huang, W.3    Pajor, A.M.4    Leibach, F.H.5    Devoe, L.D.6    Prasad, P.D.7    Ganapathy, V.8
  • 344
  • 345
    • 0021254084 scopus 로고
    • Sodium-dependent dicarboxylate transport in rat renal basolateral membrane vesicles
    • Burckhardt G. Sodium-dependent dicarboxylate transport in rat renal basolateral membrane vesicles. Pflugers Arch 1984; 401:254-261.
    • (1984) Pflugers Arch , vol.401 , pp. 254-261
    • Burckhardt, G.1
  • 346
    • 0023579684 scopus 로고
    • Succinate and citrate transport in renal basolateral and brush-border membranes
    • Wright SH, Wunz TM. Succinate and citrate transport in renal basolateral and brush-border membranes. Am J Physiol 1987; 253:F432-F439.
    • (1987) Am J Physiol , vol.253 , pp. F432-F439
    • Wright, S.H.1    Wunz, T.M.2
  • 347
    • 0023759094 scopus 로고
    • Effect of pH on citrate reabsorption in the proximal tubule
    • Brennan S, Hering-Smith K, Hamm LL. Effect of pH on citrate reabsorption in the proximal tubule. Am J Physiol 1988; 255:F301-F306.
    • (1988) Am J Physiol , vol.255 , pp. F301-F306
    • Brennan, S.1    Hering-Smith, K.2    Hamm, L.L.3
  • 348
    • 18244431934 scopus 로고
    • Effects of pH, calcium, and succinate on sodium citrate cotransport in renal microvilli
    • Barac-Nieto M. Effects of pH, calcium, and succinate on sodium citrate cotransport in renal microvilli. Am J Physiol 1984; 247:F282-F290.
    • (1984) Am J Physiol , vol.247 , pp. F282-F290
    • Barac-Nieto, M.1
  • 349
    • 0029853499 scopus 로고    scopus 로고
    • Functional differences between rabbit and human Na(+) -dicarboxylate cotransporters, NaDC-1 and hNaDC-1
    • Pajor AM, Sun N. Functional differences between rabbit and human Na(+) -dicarboxylate cotransporters, NaDC-1 and hNaDC-1. Am J Physiol 1996; 271:F1093-F1099.
    • (1996) Am J Physiol , vol.271 , pp. F1093-F1099
    • Pajor, A.M.1    Sun, N.2
  • 350
    • 0029940669 scopus 로고    scopus 로고
    • Expression of the renal Na+/dicarboxylate cotran-sporter, NaDC-1, in COS-7 cells
    • Pajor AM, Valmonte HG. Expression of the renal Na+/dicarboxylate cotran-sporter, NaDC-1, in COS-7 cells. Pflugers Arch 1996; 431:645-651.
    • (1996) Pflugers Arch , vol.431 , pp. 645-651
    • Pajor, A.M.1    Valmonte, H.G.2
  • 351
    • 0033037180 scopus 로고    scopus 로고
    • Sodium-coupled transporters for Krebs cycle intermediates
    • Pajor AM. Sodium-coupled transporters for Krebs cycle intermediates. Annu Rev Physiol 1999; 61:663-683.
    • (1999) Annu Rev Physiol , vol.61 , pp. 663-683
    • Pajor, A.M.1
  • 352
    • 0021025269 scopus 로고
    • Effect of K and H on sodium/citrate cotran-sport in renal brush border vesicles
    • Grassl SM, Heinz E, Kinne R. Effect of K and H on sodium/citrate cotran-sport in renal brush border vesicles. Biochem Biophy Acta 1983; 736:178-188.
    • (1983) Biochem Biophy Acta , vol.736 , pp. 178-188
    • Grassl, S.M.1    Heinz, E.2    Kinne, R.3
  • 353
    • 0026332901 scopus 로고
    • Chronic K depletion stimulates rat renal brush-border membrane Na-citrate cotransporter
    • Levi M, McDonald LA, Preisig PA, Alpern RJ. Chronic K depletion stimulates rat renal brush-border membrane Na-citrate cotransporter. Am J Physiol 1991; 261:F767-F773.
    • (1991) Am J Physiol , vol.261 , pp. F767-F773
    • Levi, M.1    McDonald, L.A.2    Preisig, P.A.3    Alpern, R.J.4
  • 357
    • 0033775213 scopus 로고    scopus 로고
    • Proximal tubular phosphate reabsorption: Molecular mechanism
    • Murer H, Hernando N, Forster I, Biber J. Proximal tubular phosphate reabsorption: molecular mechanism. Physiol Rev 2000; 80:1373-1409.
    • (2000) Physiol Rev , vol.80 , pp. 1373-1409
    • Murer, H.1    Hernando, N.2    Forster, I.3    Biber, J.4
  • 359
    • 0033918512 scopus 로고    scopus 로고
    • Proton-sensitive transitions of renal type II Na-coupled phosphate cotransporter kinetics
    • Forster IC, Biber J, Murer H. Proton-sensitive transitions of renal type II Na-coupled phosphate cotransporter kinetics. Biophys J 2000; 79:215-230.
    • (2000) Biophys J , vol.79 , pp. 215-230
    • Forster, I.C.1    Biber, J.2    Murer, H.3
  • 360
    • 0019459719 scopus 로고
    • Sodium gradient-dependent phosphate transport in renal brush border membrane vesicles
    • Cheng L, Sacktor B. Sodium gradient-dependent phosphate transport in renal brush border membrane vesicles. J Biol Chem 1981; 256:1556-1564.
    • (1981) J Biol Chem , vol.256 , pp. 1556-1564
    • Cheng, L.1    Sacktor, B.2
  • 361
    • 0023124946 scopus 로고
    • Effect of pH on the kinetics of Na-dependent phosphate transport in rat renal brush border membranes
    • Bindels RJM, van den Broek LAM, van Os CH. Effect of pH on the kinetics of Na-dependent phosphate transport in rat renal brush border membranes. Biochem Biophys Acta 1987; 897:83-92.
    • (1987) Biochem Biophys Acta , vol.897 , pp. 83-92
    • Bindels, R.J.M.1    van den Broek, L.A.M.2    van Os, C.H.3
  • 362
    • 0031822417 scopus 로고    scopus 로고
    • The voltage dependence of a cloned mammalian renal type II Na+/Pi cotransporter (NaPi-2)
    • Forster I, Hernando N, Biber J, Murer H. The voltage dependence of a cloned mammalian renal type II Na+/Pi cotransporter (NaPi-2). J Gen Physiol 1998; 112:1-18.
    • (1998) J Gen Physiol , vol.112 , pp. 1-18
    • Forster, I.1    Hernando, N.2    Biber, J.3    Murer, H.4
  • 363
    • 0031849866 scopus 로고    scopus 로고
    • Regulation of renal phosphate transport by acute and chronic metabolic acidosis in the rat
    • Ambhhl PM, Zajicek HK, Wang H, Puttaparthi K, Levi M. Regulation of renal phosphate transport by acute and chronic metabolic acidosis in the rat. Kidney Int 1998; 53:1288-1298.
    • (1998) Kidney Int , vol.53 , pp. 1288-1298
    • Ambhhl, P.M.1    Zajicek, H.K.2    Wang, H.3    Puttaparthi, K.4    Levi, M.5
  • 364
    • 0028335037 scopus 로고
    • Expression of Na-P(i) cotransport in rat kidney: Localization by RT-PCR and immunohistochemistry
    • Custer M, Lotscher M, Biber J, Murer H, Kaissling B. Expression of Na-P(i) cotransport in rat kidney: localization by RT-PCR and immunohistochemistry. Am J Physiol 1994; 266:F767-F774.
    • (1994) Am J Physiol , vol.266 , pp. F767-F774
    • Custer, M.1    Lotscher, M.2    Biber, J.3    Murer, H.4    Kaissling, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.