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Volumn 391, Issue 1, 2005, Pages 33-40

Human Rhesus B and Rhesus C glycoproteins: Properties of facilitated ammonium transport in recombinant kidney cells

Author keywords

Ammonium transport; Kidney cell; NH3 channel; Rhesus family (Rh); Stopped flow fluorimetry

Indexed keywords

ACIDITY; CELLS; METABOLISM; PLASMA APPLICATIONS; RATE CONSTANTS; SUBSTRATES;

EID: 26844523112     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050657     Document Type: Article
Times cited : (76)

References (43)
  • 2
    • 0035053248 scopus 로고    scopus 로고
    • New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues
    • Huang, C. H. and Liu, P. Z. (2001) New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues. Blood Cells Mol. Dis. 27, 90-101
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 90-101
    • Huang, C.H.1    Liu, P.Z.2
  • 3
    • 0033506288 scopus 로고    scopus 로고
    • RH blood group system and molecular basis of Rh-deficiency
    • Cartron, J. P. (1999) RH blood group system and molecular basis of Rh-deficiency. Baillieres Best Pract. Res. Clin. Haematol. 12, 655-689
    • (1999) Baillieres Best Pract. Res. Clin. Haematol. , vol.12 , pp. 655-689
    • Cartron, J.P.1
  • 4
    • 0034651012 scopus 로고    scopus 로고
    • The Rh blood group system: A review
    • Avent, N. D. and Reid, M. E. (2000) The Rh blood group system: a review. Blood 95, 375-387
    • (2000) Blood , vol.95 , pp. 375-387
    • Avent, N.D.1    Reid, M.E.2
  • 5
    • 0033757434 scopus 로고    scopus 로고
    • The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast
    • Marini, A. M., Matassi, G., Raynal, V., Andre, B., Cartron, J. P. and Cherif-Zahar, B. (2000) The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. Nat. Genet. 26, 341-344
    • (2000) Nat. Genet. , vol.26 , pp. 341-344
    • Marini, A.M.1    Matassi, G.2    Raynal, V.3    Andre, B.4    Cartron, J.P.5    Cherif-Zahar, B.6
  • 6
    • 0037066722 scopus 로고    scopus 로고
    • Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter
    • Westhoff, C. M., Ferreri-Jacobia, M., Mak, D. O. and Foskett, J. K. (2002) Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter. J. Biol. Chem. 277, 12499-12502
    • (2002) J. Biol. Chem. , vol.277 , pp. 12499-12502
    • Westhoff, C.M.1    Ferreri-Jacobia, M.2    Mak, D.O.3    Foskett, J.K.4
  • 7
    • 0034682768 scopus 로고    scopus 로고
    • Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis
    • Liu, Z., Chen, Y., Mo, R., Hui, C., Cheng, J. F., Mohandas, N. and Huang, C. H. (2000) Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis. J. Biol. Chem. 275, 25641-25651
    • (2000) J. Biol. Chem. , vol.275 , pp. 25641-25651
    • Liu, Z.1    Chen, Y.2    Mo, R.3    Hui, C.4    Cheng, J.F.5    Mohandas, N.6    Huang, C.H.7
  • 8
    • 0035847047 scopus 로고    scopus 로고
    • Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals
    • Liu, Z., Peng, J., Mo, R., Hui, C. and Huang, C. H. (2001) Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals. J. Biol. Chem. 276, 1424-1433
    • (2001) J. Biol. Chem. , vol.276 , pp. 1424-1433
    • Liu, Z.1    Peng, J.2    Mo, R.3    Hui, C.4    Huang, C.H.5
  • 12
    • 0038636372 scopus 로고    scopus 로고
    • Localization of the ammonium transporters, Rh B glycoprotein and Rh C glycoprotein, in the mouse liver
    • Weiner, I. D., Miller, R. T. and Verlander, J. W. (2003) Localization of the ammonium transporters, Rh B glycoprotein and Rh C glycoprotein, in the mouse liver. Gastroenterology 124, 1432-1440
    • (2003) Gastroenterology , vol.124 , pp. 1432-1440
    • Weiner, I.D.1    Miller, R.T.2    Verlander, J.W.3
  • 13
    • 4344682249 scopus 로고    scopus 로고
    • Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mlMCD-3)
    • Handlogten, M. E., Hong, S. P., Westhoff, C. M. and Weiner, I. D. (2004) Basolateral ammonium transport by the mouse inner medullary collecting duct cell (mlMCD-3). Am. J. Physiol. Renal Physiol. 287, F628-F638
    • (2004) Am. J. Physiol. Renal Physiol. , vol.287
    • Handlogten, M.E.1    Hong, S.P.2    Westhoff, C.M.3    Weiner, I.D.4
  • 15
    • 4644262798 scopus 로고    scopus 로고
    • Electroneutral ammonium transport by basolateral rhesus B glycoprotein
    • Ludewig, U. (2004) Electroneutral ammonium transport by basolateral rhesus B glycoprotein. J. Physiol. 559, 751-759
    • (2004) J. Physiol. , vol.559 , pp. 751-759
    • Ludewig, U.1
  • 17
    • 2342423024 scopus 로고    scopus 로고
    • Mechanism of genetic complementation of ammonium transport in yeast by human erythrocyte Rh-associated glycoprotein
    • Westhoff, C. M., Siegel, D. L., Burd, C. G. and Foskett, J. K. (2004) Mechanism of genetic complementation of ammonium transport in yeast by human erythrocyte Rh-associated glycoprotein. J. Biol. Chem. 279, 17443-17448
    • (2004) J. Biol. Chem. , vol.279 , pp. 17443-17448
    • Westhoff, C.M.1    Siegel, D.L.2    Burd, C.G.3    Foskett, J.K.4
  • 18
    • 0031179949 scopus 로고    scopus 로고
    • + conductance in Xenopus laevis oocytes. I. Basic observations
    • + conductance in Xenopus laevis oocytes. I. Basic observations. Pflugers Arch. 434, 306-312
    • (1997) Pflugers Arch. , vol.434 , pp. 306-312
    • Burckhardt, B.C.1    Burckhardt, G.2
  • 21
    • 0036682963 scopus 로고    scopus 로고
    • Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein
    • Mouro-Chanteloup, I., D'Ambrosio, A. M., Gane, P., Le Van Kim, C., Raynal, V., Dhermy, D., Cartron, J. P. and Colin, Y. (2002) Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein. Blood 100, 1038-1047
    • (2002) Blood , vol.100 , pp. 1038-1047
    • Mouro-Chanteloup, I.1    D'Ambrosio, A.M.2    Gane, P.3    Le Van Kim, C.4    Raynal, V.5    Dhermy, D.6    Cartron, J.P.7    Colin, Y.8
  • 23
    • 0027523653 scopus 로고
    • Apical membrane of the gastric parietal cell: Water, proton, and nonelectrolyte permeabilities
    • Priver, N. A., Rabon, E. C. and Zeidel, M. L. (1993) Apical membrane of the gastric parietal cell: water, proton, and nonelectrolyte permeabilities. Biochemistry 32, 2459-2468
    • (1993) Biochemistry , vol.32 , pp. 2459-2468
    • Priver, N.A.1    Rabon, E.C.2    Zeidel, M.L.3
  • 24
    • 0023748263 scopus 로고
    • 3 permeation through the apical membrane of MDCK cells is via a lipid pathway
    • 3 permeation through the apical membrane of MDCK cells is via a lipid pathway. Am. J. Physiol. 255, F135-F141
    • (1988) Am. J. Physiol. , vol.255
    • Golchini, K.1    Kurtz, I.2
  • 27
    • 0023235679 scopus 로고
    • + exchanger is constitutively activated in P19 embryonal carcinoma cells, but not in a differentiated derivative. Responsiveness to growth factors and other stimuli
    • + exchanger is constitutively activated in P19 embryonal carcinoma cells, but not in a differentiated derivative. Responsiveness to growth factors and other stimuli. J. Biol. Chem. 262, 9621-9628
    • (1987) J. Biol. Chem. , vol.262 , pp. 9621-9628
    • Bierman, A.J.1    Tertoolen, L.G.2    De Laat, S.W.3    Moolenaar, W.H.4
  • 28
    • 0028934857 scopus 로고
    • Ammonia permeability of erythrocyte membrane studied by 14N and 15N saturation transfer NMR spectroscopy
    • Labotka, R. J., Lundberg, P. and Kuchel, P. W. (1995) Ammonia permeability of erythrocyte membrane studied by 14N and 15N saturation transfer NMR spectroscopy. Am. J. Physiol. 268, C686-C699
    • (1995) Am. J. Physiol. , vol.268
    • Labotka, R.J.1    Lundberg, P.2    Kuchel, P.W.3
  • 29
    • 0027368023 scopus 로고
    • Concurrent expression of erythroid and renal aquaporin CHIP and appearance of water channel activity in perinatal rats
    • Smith, B. L., Baumgarten, R., Nielsen, S., Raben, D., Zeidel, M. L. and Agre, P. (1993) Concurrent expression of erythroid and renal aquaporin CHIP and appearance of water channel activity in perinatal rats. J. Clin. Invest. 92, 2035-2041
    • (1993) J. Clin. Invest. , vol.92 , pp. 2035-2041
    • Smith, B.L.1    Baumgarten, R.2    Nielsen, S.3    Raben, D.4    Zeidel, M.L.5    Agre, P.6
  • 30
    • 10344262632 scopus 로고    scopus 로고
    • The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli
    • Zheng, L., Kostrewa, D., Berneche, S., Winkler, F. K. and Li, X. D. (2004) The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 101, 17090-17095
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17090-17095
    • Zheng, L.1    Kostrewa, D.2    Berneche, S.3    Winkler, F.K.4    Li, X.D.5
  • 32
  • 33
    • 0037133927 scopus 로고    scopus 로고
    • + by the root hair plasma membrane ammonium transporter LeAMT1;1
    • + by the root hair plasma membrane ammonium transporter LeAMT1;1. J. Biol. Chem. 277, 13548-13555
    • (2002) J. Biol. Chem. , vol.277 , pp. 13548-13555
    • Ludewig, U.1    Von Wiren, N.2    Frommer, W.B.3
  • 36
    • 1542288949 scopus 로고    scopus 로고
    • Secondary active transport mediated by a prokaryotic homologue of CIC Cl-channels
    • Accardi, A. and Miller, C. (2004) Secondary active transport mediated by a prokaryotic homologue of CIC Cl-channels. Nature (London) 427, 803-807
    • (2004) Nature (London) , vol.427 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 37
    • 0033964857 scopus 로고    scopus 로고
    • Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules
    • Niemietz, C. M. and Tyerman, S. D. (2000) Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules. FEBS Lett. 465, 110-114
    • (2000) FEBS Lett. , vol.465 , pp. 110-114
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 43
    • 2442640345 scopus 로고    scopus 로고
    • Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2
    • Soupene, E., Inwood, W. and Kustu, S. (2004) Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2. Proc. Natl. Acad. Sci. U.S.A. 101, 7787-7792
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7787-7792
    • Soupene, E.1    Inwood, W.2    Kustu, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.