|
|
||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,
,
* Abteilung Vegetative Physiologie, Medizinische Hochschule Hannover, Hannover, Germany;
Institut National de la Santé et de la Recherche Médicale, Paris, France; and
Institut National de la Transfusion Sanguine, Paris, France
1Correspondence: Abt. Vegetative Physiologie Medizinische Hochschule Hannover, 30623-Hannover, Germany. E-mail: gros.gerolf{at}mh-hannover.de
We have determined CO2 permeabilities, PCO2, of red cells of normal human blood and of blood deficient in various blood group proteins by a previously described mass spectrometric technique. While PCO2 of normal red cells is
0.15 cm/s, we find in red blood cells (RBCs) lacking the Rh protein complex (Rhnull) a significantly reduced PCO2 of 0.07 cm/s ±0.02 cm/s (P<0.02). This value is similar to the value we have reported previously for RBCs lacking aquaporin-1 protein (AQP-1null), suggesting that each of the Rh and AQP-1 proteins is responsible for
1/2 of the normal CO2 permeability of the RBC membrane. Four other blood group deficiencies tested lack diverse membrane proteins but exhibit normal CO2 permeability. The CO2 pathway constituted by Rh proteins was inhibitable at pHe= 7.4 by NH4Cl with an I50 of
10 mM corresponding to an I50 for NH3 of
0.3 mM. The pathway independent of Rh proteins, presumably that constituted by AQP-1, was not inhibitable by NH4Cl/NH3. However, both pathways were strongly inhibited by DIDS, which accounts for the marked inhibitory effect of DIDS on normal PCO2, while in contrast another AE1 inhibitor, DiBAC, does not inhibit PCO2, although it markedly reduces PHCO3-. We conclude that Rh protein, presumably the Rh-associated glycoprotein RhAG, possesses a gas channel that allows passage of CO2 in addition to NH3.—Endeward, V., Cartron, J.-P., Ripoche, P., and Gros, G. RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane.
Key Words: Rhesus-associated glycoprotein membrane CO2 permeability ammonia aquaporin-1
This article has been cited by other articles:
![]() |
T. Nakada, C. M. Westhoff, Y. Yamaguchi, S. Hyodo, X. Li, T. Muro, A. Kato, N. Nakamura, and S. Hirose Rhesus Glycoprotein P2 (Rhp2) Is a Novel Member of the Rh Family of Ammonia Transporters Highly Expressed in Shark Kidney J. Biol. Chem., January 22, 2010; 285(4): 2653 - 2664. [Abstract] [Full Text] [PDF] |
||||
![]() |
W. B. Inwood, J. A. Hall, K.-S. Kim, R. Fong, and S. Kustu Genetic Evidence for an Essential Oscillation of Transmembrane-Spanning Segment 5 in the Escherichia coli Ammonium Channel AmtB Genetics, December 1, 2009; 183(4): 1341 - 1355. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. P. Jeremy, Z. E. Plummer, D. J. Head, T. E. Madgett, K. L. Sanders, A. Wallington, J. R. Storry, F. Gilsanz, J. Delaunay, and N. D. Avent 4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins Haematologica, October 1, 2009; 94(10): 1354 - 1361. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. F. Flatt and L. J. Bruce The hereditary stomatocytoses Haematologica, August 1, 2009; 94(8): 1039 - 1041. [Full Text] [PDF] |
||||
![]() |
A. C. N. Brown, D. Hallouane, W. J. Mawby, F. E. Karet, M. A. Saleem, A. J. Howie, and A. M. Toye RhCG is the major putative ammonia transporter expressed in the human kidney, and RhBG is not expressed at detectable levels Am J Physiol Renal Physiol, June 1, 2009; 296(6): F1279 - F1290. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Musa-Aziz, L.-M. Chen, M. F. Pelletier, and W. F. Boron Relative CO2/NH3 selectivities of AQP1, AQP4, AQP5, AmtB, and RhAG PNAS, March 31, 2009; 106(13): 5406 - 5411. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Endeward and G. Gros Extra- and intracellular unstirred layer effects in measurements of CO2 diffusion across membranes - a novel approach applied to the mass spectrometric 18O technique for red blood cells J. Physiol., March 15, 2009; 587(6): 1153 - 1167. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. J. Bruce, H. Guizouarn, N. M. Burton, N. Gabillat, J. Poole, J. F. Flatt, R. L. Brady, F. Borgese, J. Delaunay, and G. W. Stewart The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein Blood, February 5, 2009; 113(6): 1350 - 1357. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Zidi-Yahiaoui, I. Callebaut, S. Genetet, C. Le Van Kim, J.-P. Cartron, Y. Colin, P. Ripoche, and I. Mouro-Chanteloup Functional analysis of human RhCG: comparison with E. coli ammonium transporter reveals similarities in the pore and differences in the vestibule Am J Physiol Cell Physiol, January 1, 2009; 297(3): C537 - C547. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |