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Volumn 13, Issue 1-2 SPEC. ISS., 2006, Pages 123-127

Red cell membrane CO2 permeability in normal human blood and in blood deficient in various blood groups, and effect of DIDS

Author keywords

Aquaporin 1; Blood group deficiencies; Human red cells; Membrane CO2 permeability; Rh proteins

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; AQUAPORIN 1; CARBON DIOXIDE; CARBONIC ACID; GLYCOPROTEIN; MEMBRANE PROTEIN; RH PROTEIN; RHAG PROTEIN; UNCLASSIFIED DRUG;

EID: 33646026698     PISSN: 12467820     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tracli.2006.02.007     Document Type: Article
Times cited : (51)

References (31)
  • 3
    • 23844541971 scopus 로고    scopus 로고
    • Low carbon dioxide permeability of the apical epithelial membrane of guinea-pig colon
    • Endeward V., and Gros G. Low carbon dioxide permeability of the apical epithelial membrane of guinea-pig colon. J. Physiol. 567 (2005) 253-265
    • (2005) J. Physiol. , vol.567 , pp. 253-265
    • Endeward, V.1    Gros, G.2
  • 4
    • 0033506288 scopus 로고    scopus 로고
    • RH blood group system and molecular basis of Rh-deficiency
    • Cartron J.P. RH blood group system and molecular basis of Rh-deficiency. Baillieres. Best Pract. Res. Clin. Haematol. 12 (1999) 655-689
    • (1999) Baillieres. Best Pract. Res. Clin. Haematol. , vol.12 , pp. 655-689
    • Cartron, J.P.1
  • 5
    • 0034093078 scopus 로고    scopus 로고
    • The Duffy protein: a malarial and chemokine receptor
    • Pogo A.O., and Chaudhuri A. The Duffy protein: a malarial and chemokine receptor. Semin. Hematol. 37 (2000) 122-129
    • (2000) Semin. Hematol. , vol.37 , pp. 122-129
    • Pogo, A.O.1    Chaudhuri, A.2
  • 6
    • 0027372505 scopus 로고
    • A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor
    • Horuk R., Chitnis C.E., Darbonne W.C., Colby T.J., Rybicki A., Hadley T.J., et al. A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor. Science 261 (1993) 1182-1184
    • (1993) Science , vol.261 , pp. 1182-1184
    • Horuk, R.1    Chitnis, C.E.2    Darbonne, W.C.3    Colby, T.J.4    Rybicki, A.5    Hadley, T.J.6
  • 7
    • 0032557563 scopus 로고    scopus 로고
    • Characterization of the gene encoding the human Kidd blood group urea transporter protein-evidence for splice site mutations in Jk(null) individuals
    • Lucien N., Sidoux-Walter F., Olives B., Moulds J., Le Pennec P.Y., Cartron J.P., et al. Characterization of the gene encoding the human Kidd blood group urea transporter protein-evidence for splice site mutations in Jk(null) individuals. J. Biol. Chem. 273 (1998) 12973-12980
    • (1998) J. Biol. Chem. , vol.273 , pp. 12973-12980
    • Lucien, N.1    Sidoux-Walter, F.2    Olives, B.3    Moulds, J.4    Le Pennec, P.Y.5    Cartron, J.P.6
  • 8
    • 0034031642 scopus 로고    scopus 로고
    • Functional and structural aspects of the Kell blood group system
    • Lee S., Russo D., and Redman C.M. Functional and structural aspects of the Kell blood group system. Trans. Med. Reviews. 14 (2000) 93-103
    • (2000) Trans. Med. Reviews. , vol.14 , pp. 93-103
    • Lee, S.1    Russo, D.2    Redman, C.M.3
  • 9
    • 0034651012 scopus 로고    scopus 로고
    • The Rh blood group system: a review
    • Avent N.D., and Reid M.E. The Rh blood group system: a review. Blood 95 (2000) 375-387
    • (2000) Blood , vol.95 , pp. 375-387
    • Avent, N.D.1    Reid, M.E.2
  • 10
    • 33646060093 scopus 로고    scopus 로고
    • Rh proteins: key structural and functional components of the red cell membrane
    • [Epub ahead of print]
    • Le Van Kim C., Colin Y., and Cartron J.P. Rh proteins: key structural and functional components of the red cell membrane. Blood Rev. Jun (2005) 13 [Epub ahead of print]
    • (2005) Blood Rev. , Issue.Jun , pp. 13
    • Le Van Kim, C.1    Colin, Y.2    Cartron, J.P.3
  • 11
    • 0034038007 scopus 로고    scopus 로고
    • Molecular biology and genetics of the Rh blood group system
    • Huang C.H., Liu P.Z., and Cheng J.G. Molecular biology and genetics of the Rh blood group system. Semin. Hematol. 37 (2000) 150-165
    • (2000) Semin. Hematol. , vol.37 , pp. 150-165
    • Huang, C.H.1    Liu, P.Z.2    Cheng, J.G.3
  • 12
    • 0036682963 scopus 로고    scopus 로고
    • Cell-surface expression of RhD blood group polypeptide is post-transcriptionally regulated by the RhAG glycoprotein
    • Mouro-Chanteloup I., D'Ambrosio A.M., Gane P., Le Van Kim C., Raynal V., Dhermy D., et al. Cell-surface expression of RhD blood group polypeptide is post-transcriptionally regulated by the RhAG glycoprotein. Blood 100 (2002) 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
  • 13
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: the evolving tale of aquaporin biology
    • King L.S., Kozono D., and Agre P. From structure to disease: the evolving tale of aquaporin biology. Nat. Rev. Mol. Cell Biol. 5 (2004) 687-698
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 14
    • 0028088012 scopus 로고
    • Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels
    • Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., and Agre P. Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science 265 (1994) 1585-1587
    • (1994) Science , vol.265 , pp. 1585-1587
    • Preston, G.M.1    Smith, B.L.2    Zeidel, M.L.3    Moulds, J.J.4    Agre, P.5
  • 15
    • 0027980902 scopus 로고
    • Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens
    • Smith B.L., Preston G.M., Spring F.A., Anstee D.J., and Agre P. Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. J. Clin. Invest. 94 (1994) 1043-1049
    • (1994) J. Clin. Invest. , vol.94 , pp. 1043-1049
    • Smith, B.L.1    Preston, G.M.2    Spring, F.A.3    Anstee, D.J.4    Agre, P.5
  • 16
    • 0017750205 scopus 로고
    • Diffusion of carbon dioxide through lipid bilayer membranes: effects of carbonic anhydrase, bicarbonate, and unstirred layers
    • Gutknecht J., Bisson M.A., and Tosteson F.C. Diffusion of carbon dioxide through lipid bilayer membranes: effects of carbonic anhydrase, bicarbonate, and unstirred layers. J. Gen. Physiol. 69 (1977) 779-794
    • (1977) J. Gen. Physiol. , vol.69 , pp. 779-794
    • Gutknecht, J.1    Bisson, M.A.2    Tosteson, F.C.3
  • 17
    • 0023768507 scopus 로고
    • Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
    • Denker B.M., Smith B.L., Kuhajda F.P., and Agre P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J. Biol. Chem. 263 (1988) 15634-15642
    • (1988) J. Biol. Chem. , vol.263 , pp. 15634-15642
    • Denker, B.M.1    Smith, B.L.2    Kuhajda, F.P.3    Agre, P.4
  • 18
    • 0038157322 scopus 로고    scopus 로고
    • A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane
    • Bruce L.J., Beckmann R., Ribeiro M.L., Peters L.L., Chasis J.A., Delaunay J., et al. A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane. Blood 101 (2003) 4180-4188
    • (2003) Blood , vol.101 , pp. 4180-4188
    • Bruce, L.J.1    Beckmann, R.2    Ribeiro, M.L.3    Peters, L.L.4    Chasis, J.A.5    Delaunay, J.6
  • 19
    • 33646053216 scopus 로고    scopus 로고
    • Membrane dynamics of the water transport protein aquaporin-1 in intact human RBCs
    • Cho M.R., Knowles D.W., Smith B.L., Moulds J.J., Agre P., Mohandas N., et al. Membrane dynamics of the water transport protein aquaporin-1 in intact human RBCs. Blood. Rev. 20 (2006) 93-110
    • (2006) Blood. Rev. , vol.20 , pp. 93-110
    • Cho, M.R.1    Knowles, D.W.2    Smith, B.L.3    Moulds, J.J.4    Agre, P.5    Mohandas, N.6
  • 24
    • 0034723202 scopus 로고    scopus 로고
    • Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes
    • Yang B., Fukuda N., Van Hoek A., Matthay M.A., Ma T., and Verkman A.S. Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes. J. Biol. Chem. 275 (2000) 2686-2692
    • (2000) J. Biol. Chem. , vol.275 , pp. 2686-2692
    • Yang, B.1    Fukuda, N.2    Van Hoek, A.3    Matthay, M.A.4    Ma, T.5    Verkman, A.S.6
  • 27
    • 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. The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli. Proc. Natl. Acad. Sci. USA 101 (2004) 17090-17095
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17090-17095
    • Zheng, L.1    Kostrewa, D.2    Berneche, S.3    Winkler, F.K.4    Li, X.D.5
  • 28
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H., Han B.G., Lee J.K., Wallan P., and Jap B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature 414 (2001) 872-878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Wallan, P.4    Jap, B.K.5
  • 29
    • 0036544847 scopus 로고    scopus 로고
    • New roles for old holes: ion channel function in aquaporin-1
    • Yool A.J., and Weinstein A.M. New roles for old holes: ion channel function in aquaporin-1. News Physiol. Sci. 17 (2002) 68-72
    • (2002) News Physiol. Sci. , vol.17 , pp. 68-72
    • Yool, A.J.1    Weinstein, A.M.2
  • 31
    • 33646040719 scopus 로고    scopus 로고
    • Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures
    • (this issue)
    • Callebaut I., Dulin F., Bertrand O., Ripoche P., Colin Y., Mornon J.P., et al. Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures. Trans. Clin. Biol. (2006) (this issue)
    • (2006) Trans. Clin. Biol.
    • Callebaut, I.1    Dulin, F.2    Bertrand, O.3    Ripoche, P.4    Colin, Y.5    Mornon, J.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.