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Volumn 563, Issue 2, 2005, Pages 421-431

Activation of ferret erythrocyte Na+-K+-2Cl- cotransport by deoxygenation

Author keywords

[No Author keywords available]

Indexed keywords

ARSENITE SODIUM; CALYCULIN A; MAGNESIUM ION; PHOSPHOTRANSFERASE; SODIUM POTASSIUM CHLORIDE COTRANSPORTER; STAUROSPORINE; THREONINE; 4 AMINO 7 TERT BUTYL 5 (4 METHYLPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; CHLORIDE ION; MAGNESIUM; PHOSPHATASE; POTASSIUM ION; SODIUM ION;

EID: 14944384544     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2004.080507     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 4243278194 scopus 로고
    • A non-metabolic role for oxygen in the control of passive cation permeability in the duck red cell
    • Allen DW & McManus TJ (1968). A non-metabolic role for oxygen in the control of passive cation permeability in the duck red cell. Biophys J 8, A125.
    • (1968) Biophys. J. , vol.8
    • Allen, D.W.1    McManus, T.J.2
  • 2
    • 0032994757 scopus 로고    scopus 로고
    • Deoxygenation and elevation of intracellular magnesium induce tyrosine phosphorylation of band 3 in human erythrocytes
    • Barbul A, Zipser Y, Nachles A & Korenstein R (1999). Deoxygenation and elevation of intracellular magnesium induce tyrosine phosphorylation of band 3 in human erythrocytes. FEBS Lett 455 87-91.
    • (1999) FEBS Lett. , vol.455 , pp. 87-91
    • Barbul, A.1    Zipser, Y.2    Nachles, A.3    Korenstein, R.4
  • 4
    • 0036659906 scopus 로고    scopus 로고
    • Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes
    • Bordin L, Brunati AM, Donella-Deana A, Baggio B, Toninello A & Clari G (2002). Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes. Blood 100, 276-282.
    • (2002) Blood , vol.100 , pp. 276-282
    • Bordin, L.1    Brunati, A.M.2    Donella-Deana, A.3    Baggio, B.4    Toninello, A.5    Clari, G.6
  • 5
    • 0034663190 scopus 로고    scopus 로고
    • Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: Identification of primary and secondary phosphorylation sites
    • Brunati AM, Bordin L, Clari G, James P, Quadroni M, Baritono E, Pinna LA & Donella-Deana A (2000). Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites. Blood 96, 1550-1557.
    • (2000) Blood , vol.96 , pp. 1550-1557
    • Brunati, A.M.1    Bordin, L.2    Clari, G.3    James, P.4    Quadroni, M.5    Baritono, E.6    Pinna, L.A.7    Donella-Deana, A.8
  • 8
    • 0022005738 scopus 로고
    • Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3
    • Chétrite G & Cassoly R (1985). Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3. J Mol Biol 185, 639-644.
    • (1985) J. Mol. Biol. , vol.185 , pp. 639-644
    • Chétrite, G.1    Cassoly, R.2
  • 9
    • 0035860734 scopus 로고    scopus 로고
    • Modulation of ion transport by direct targeting of protein phosphatase type I to the Na-K-Cl cotransporter
    • Darman RB, Flemmer A & Forbush B (2001). Modulation of ion transport by direct targeting of protein phosphatase type I to the Na-K-Cl cotransporter. J Biol Chem 276, 34359-34362.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34359-34362
    • Darman, R.B.1    Flemmer, A.2    Forbush, B.3
  • 10
    • 0037020145 scopus 로고    scopus 로고
    • A regulatory locus of phosphorylation in the N terminus of the Na-K-Cl cotransporter, NKCC1
    • Darman RB & Forbush B (2002). A regulatory locus of phosphorylation in the N terminus of the Na-K-Cl cotransporter, NKCC1. J Biol Chem 277, 37542-37550.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37542-37550
    • Darman, R.B.1    Forbush, B.2
  • 11
    • 0042847432 scopus 로고    scopus 로고
    • PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1)
    • Dowd BFX & Forbush B (2003). PASK (proline-alanine-rich STE20-related kinase), a regulatory kinase of the Na-K-Cl cotransporter (NKCC1). J Biol Chem 278, 27347-27353.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27347-27353
    • Dowd, B.F.X.1    Forbush, B.2
  • 12
    • 0018908733 scopus 로고
    • The effect of buffer composition and deoxygenation on the concentration of ionized magnesium inside human red blood cells
    • Flatman PW (1980). The effect of buffer composition and deoxygenation on the concentration of ionized magnesium inside human red blood cells. J Physiol 300, 19-30.
    • (1980) J. Physiol. , vol.300 , pp. 19-30
    • Flatman, P.W.1
  • 13
    • 0020642945 scopus 로고
    • Sodium and potassium transport in ferret red cells
    • Flatman PW (1983). Sodium and potassium transport in ferret red cells. J Physiol 341, 545-557.
    • (1983) J. Physiol. , vol.341 , pp. 545-557
    • Flatman, P.W.1
  • 14
    • 0023880386 scopus 로고
    • The effects of magnesium on potassium transport in ferret red cells
    • Flatman PW (1988). The effects of magnesium on potassium transport in ferret red cells. J Physiol 397, 471-487.
    • (1988) J. Physiol. , vol.397 , pp. 471-487
    • Flatman, P.W.1
  • 15
    • 0037073286 scopus 로고    scopus 로고
    • Regulation of Na-K-2Cl cotransport by phosphorylation and protein-protein interactions
    • Flatman PW (2002). Regulation of Na-K-2Cl cotransport by phosphorylation and protein-protein interactions. Biochim Biophys Acta 1566, 140-151.
    • (2002) Biochim. Biophys. Acta , vol.1566 , pp. 140-151
    • Flatman, P.W.1
  • 16
    • 0033564822 scopus 로고    scopus 로고
    • - cotransport by protein phosphorylation in ferret erythrocytes
    • - cotransport by protein phosphorylation in ferret erythrocytes. J Physiol 517, 699-708.
    • (1999) J. Physiol. , vol.517 , pp. 699-708
    • Flatman, P.W.1    Creanor, J.2
  • 17
    • 0033567134 scopus 로고    scopus 로고
    • - cotransport by arsenite in ferret erythrocytes
    • - cotransport by arsenite in ferret erythrocytes. J Physiol 519 143-152.
    • (1999) J. Physiol. , vol.519 , pp. 143-152
    • Flatman, P.W.1    Creanor, J.2
  • 18
    • 0018910543 scopus 로고
    • Magnesium buffering in intact human red blood cells measured using the ionophore A23187
    • Flatman PW & Lew VL (1980). Magnesium buffering in intact human red blood cells measured using the ionophore A23187. J Physiol 305, 13-30.
    • (1980) J. Physiol. , vol.305 , pp. 13-30
    • Flatman, P.W.1    Lew, V.L.2
  • 19
    • 0037020095 scopus 로고    scopus 로고
    • Activation of the Na-K-Cl cotransporter NKCC1 detected with a phospho-specific antibody
    • Flemmer AW, Giménez I, Dowd BFX, Darman RB & Forbush B (2002). Activation of the Na-K-Cl cotransporter NKCC1 detected with a phospho-specific antibody. J Biol Chem 277, 37551-37558.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37551-37558
    • Flemmer, A.W.1    Giménez, I.2    Dowd, B.F.X.3    Darman, R.B.4    Forbush, B.5
  • 20
    • 0034088368 scopus 로고    scopus 로고
    • Oxygen-sensitive membrane transporters in vertebrate red cells
    • Gibson JS, Cossins AR & Ellory JC (2000). Oxygen-sensitive membrane transporters in vertebrate red cells. J Exp Biol 203 1395-1407.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1395-1407
    • Gibson, J.S.1    Cossins, A.R.2    Ellory, J.C.3
  • 22
    • 1642565061 scopus 로고    scopus 로고
    • Evidence for up-regulation of the endogenous Na-K-2Cl co-transporter by molecular interactions with the anion exchanger tAE1 expressed in Xenopus oocyte
    • Guizouarn H, Gabillat N & Borgese F (2004). Evidence for up-regulation of the endogenous Na-K-2Cl co-transporter by molecular interactions with the anion exchanger tAE1 expressed in Xenopus oocyte. J Biol Chem 279, 11513-11520.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11513-11520
    • Guizouarn, H.1    Gabillat, N.2    Borgese, F.3
  • 23
    • 0028156602 scopus 로고
    • The Na-K-Cl cotransporters
    • Haas M (1994). The Na-K-Cl cotransporters. Am J Physiol 267, C869-C885.
    • (1994) Am. J. Physiol. , vol.267
    • Haas, M.1
  • 27
    • 0013547957 scopus 로고
    • PH equilibrium across the red cell membrane
    • ed. Ellory JC, Lew VL Academic, London
    • Hladky SB & Rink TJ (1977). pH equilibrium across the red cell membrane. In Membrane Transport in Red Cells, ed. Ellory JC, Lew VL, pp. 115-135. Academic, London.
    • (1977) Membrane Transport in Red Cells , pp. 115-135
    • Hladky, S.B.1    Rink, T.J.2
  • 28
    • 0030014074 scopus 로고    scopus 로고
    • The effects of oxygenation upon the Cl-dependent K flux pathway in equine red cells
    • Honess NA, Gibson JS & Cossins AR (1996). The effects of oxygenation upon the Cl-dependent K flux pathway in equine red cells. Pflugers Arch 432, 270-277.
    • (1996) Pflugers Arch. , vol.432 , pp. 270-277
    • Honess, N.A.1    Gibson, J.S.2    Cossins, A.R.3
  • 29
    • 0000272968 scopus 로고
    • + transport across the carp red blood cell membrane
    • + transport across the carp red blood cell membrane. J Exp Biol 171, 349-371.
    • (1992) J. Exp. Biol. , vol.171 , pp. 349-371
    • Jensen, F.B.1
  • 30
    • 0029169929 scopus 로고
    • Regulatory volume decrease in carp red blood cells: Mechanisms and oxygenation-dependency of volume-activated potassium and amino acid transport
    • Jensen FB (1995). Regulatory volume decrease in carp red blood cells: mechanisms and oxygenation-dependency of volume-activated potassium and amino acid transport. J Exp Biol 198, 155-165.
    • (1995) J. Exp. Biol. , vol.198 , pp. 155-165
    • Jensen, F.B.1
  • 32
    • 4243452808 scopus 로고    scopus 로고
    • Oxygen-dependent KCl cotransport in ghosts from normal human red blood cells
    • Khan A, Gibson JS & Ellory JC (2000). Oxygen-dependent KCl cotransport in ghosts from normal human red blood cells. J Physiol 527.P, 38 P.
    • (2000) J. Physiol. , vol.527 P
    • Khan, A.1    Gibson, J.S.2    Ellory, J.C.3
  • 33
    • 0029200068 scopus 로고
    • Volume-sensitive myosin phosphorylation in vascular endothelial cells: Correlation with Na-K-2Cl cotransport
    • Klein JD & O'Neill WC (1995). Volume-sensitive myosin phosphorylation in vascular endothelial cells: correlation with Na-K-2Cl cotransport. Am J Physiol 269, C1524-C1531.
    • (1995) Am. J. Physiol. , vol.269
    • Klein, J.D.1    O'Neill, W.C.2
  • 37
    • 0031006262 scopus 로고    scopus 로고
    • Activation of the avian erythrocyte Na-K-Cl cotransport protein by cell shrinkage, cAMP, fluoride, and calyculin-A involves phosphorylation at common sites
    • Lytle C (1997). Activation of the avian erythrocyte Na-K-Cl cotransport protein by cell shrinkage, cAMP, fluoride, and calyculin-A involves phosphorylation at common sites. J Biol Chem 272, 15069-15077.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15069-15077
    • Lytle, C.1
  • 38
    • 0026465685 scopus 로고
    • The Na-K-Cl cotransport protein of shark rectal gland. II. Regulation by direct phosphorylation
    • Lytle C & Forbush B III (1992). The Na-K-Cl cotransport protein of shark rectal gland. II. Regulation by direct phosphorylation. J Biol Chem 267, 25438-25443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25438-25443
    • Lytle, C.1    Forbush III, B.2
  • 39
    • 0029188965 scopus 로고
    • Distribution and diversity of Na-K-Cl cotransport proteins: A study with monoclonal antibodies
    • Lytle C, Xu J-C, Biemesderfer D & Forbush B III (1995). Distribution and diversity of Na-K-Cl cotransport proteins: a study with monoclonal antibodies. Am J Physiol 269, C1496-C1505.
    • (1995) Am. J. Physiol. , vol.269
    • Lytle, C.1    Xu, J.-C.2    Biemesderfer, D.3    Forbush III, B.4
  • 40
    • 0001114391 scopus 로고
    • Comparative biology of red cells
    • McManus TJ (1967). Comparative biology of red cells. Fed Proc 26, 1821-1826.
    • (1967) Fed. Proc. , vol.26 , pp. 1821-1826
    • McManus, T.J.1
  • 41
    • 6444238507 scopus 로고    scopus 로고
    • - cotransport by threonine phosphorylation in ferret red cells
    • - cotransport by threonine phosphorylation in ferret red cells. J Physiol 547.P, C20.
    • (2003) J. Physiol. , vol.547 P
    • Matskevich, I.1    Flatman, P.W.2
  • 45
    • 0033153125 scopus 로고    scopus 로고
    • - cotransport in turkey red cells: The role of oxygen tension and protein phosphorylation
    • - cotransport in turkey red cells: the role of oxygen tension and protein phosphorylation. J Physiol 517, 421-429.
    • (1999) J. Physiol. , vol.517 , pp. 421-429
    • Muzyamba, M.C.1    Cossins, A.R.2    Gibson, J.S.3
  • 46
    • 0026587639 scopus 로고
    • Membrane transport and control of hemoglobin-oxygen affinity in nucleated erythrocytes
    • Nikinmaa M (1992). Membrane transport and control of hemoglobin-oxygen affinity in nucleated erythrocytes. Physiol Rev 72, 301-321.
    • (1992) Physiol. Rev. , vol.72 , pp. 301-321
    • Nikinmaa, M.1
  • 47
    • 0030901801 scopus 로고    scopus 로고
    • Oxygen and carbon dioxide transport in vertebrate erythrocytes: An evolutionary change in the role of membrane transport
    • Nikinmaa M (1997). Oxygen and carbon dioxide transport in vertebrate erythrocytes: an evolutionary change in the role of membrane transport. J Exp Biol 200, 369-380.
    • (1997) J. Exp. Biol. , vol.200 , pp. 369-380
    • Nikinmaa, M.1
  • 48
    • 0029188465 scopus 로고
    • Endothelial Na-K-Cl cotransport regulation by tonicity and hormones: Phosphorylation of cotransport protein
    • O'Donnell ME, Martinez A & Sun D (1995). Endothelial Na-K-Cl cotransport regulation by tonicity and hormones: phosphorylation of cotransport protein. Am J Physiol 269, C1513-C1523.
    • (1995) Am. J. Physiol. , vol.269
    • O'Donnell, M.E.1    Martinez, A.2    Sun, D.3
  • 49
    • 84965187002 scopus 로고
    • The potassium absorption by pigeon blood cells
    • Ørskov SL (1954). The potassium absorption by pigeon blood cells. Acta Physiol Scand 31, 221-229.
    • (1954) Acta Physiol. Scand. , vol.31 , pp. 221-229
    • Ørskov, S.L.1
  • 52
    • 0038813693 scopus 로고    scopus 로고
    • The Src-selective kinase inhibitor PP1 also inhibits Kit and Bcr-Abl tyrosine kinases
    • Tatton L, Morley GM, Chopra R & Khwaja A (2003). The Src-selective kinase inhibitor PP1 also inhibits Kit and Bcr-Abl tyrosine kinases. J Biol Chem 278, 4847-4853.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4847-4853
    • Tatton, L.1    Morley, G.M.2    Chopra, R.3    Khwaja, A.4
  • 54
    • 6444238586 scopus 로고    scopus 로고
    • Signalling mechanisms underlying the rapid and additive stimulation of NKCC activity by insulin and hypertonicity in rat L6 skeletal muscle cells
    • Zhao H, Hyde R & Hundal HS (2004). Signalling mechanisms underlying the rapid and additive stimulation of NKCC activity by insulin and hypertonicity in rat L6 skeletal muscle cells. J Physiol 560 123-136.
    • (2004) J. Physiol. , vol.560 , pp. 123-136
    • Zhao, H.1    Hyde, R.2    Hundal, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.