FASEB J. Mp Biomedicals
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
fj.07-9097comv1
fj.07-9097comv2
fj.07-9097comv3
22/1/64    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Endeward, V.
Right arrow Articles by Gros, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Endeward, V.
Right arrow Articles by Gros, G.
Published online before print September 20, 2007 as doi: 10.1096/fj.07-9097com.

RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane

Volker Endeward, Jean-Pierre Cartron, Pierre Ripoche, and Gerolf Gros

E-mail contact: gros.gerolf@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.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
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]

Home page
 GeneticsHome page
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]

Home page
 haematolHome page
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]

Home page
 haematolHome page
J. F. Flatt and L. J. Bruce
The hereditary stomatocytoses
Haematologica, August 1, 2009; 94(8): 1039 - 1041.
[Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
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]

Home page
 Proc. Natl. Acad. Sci. USAHome page
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]

Home page
 J. Physiol.Home page
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]

Home page
 BloodHome page
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]

Home page
 Am. J. Physiol. Cell Physiol.Home page
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
Copyright © 2007 by The Federation of American Societies for Experimental Biology.