Red cell membrane CO2 permeability in normal human blood and in blood deficient in various blood groups, and effect of DIDS.
The red cell membrane has an exceptionally high permeability for CO2, PCO2 approximately 0.15 cm/s, which is two to three orders of magnitude greater than that of some epithelial membranes and similarly greater than the permeability of the red cell membrane for HCO3-. As shown previously, this high PCO2 can be drastically inhibited by 10 microM 4,4'-diisothiocyanato-2,2'-stilbenedisulfonate (DIDS), indicating that membrane proteins may be involved in this high gas permeability. Here, we have studied the possible contribution of several blood group proteins to CO2 permeation across the red cell membrane by comparing PCO2 of red cells deficient in specific blood group proteins with that of normal red cells. While PCO2 of normal red cells is approximately 0.15 cm/s and that of Fy(null) and Jk(null) red cells is similar, PCO2's of Colton null (deficient in aquaporin-1) and Rh(null) cells (deficient in Rh/RhAG) are both reduced to about 0.07 cm/s, i.e. to about one half. In addition, the inhibitory effect of DIDS is about half as great in Rh(null) and in Colton null red cells as it is in normal red cells. We conclude that aquaporin-1 and Rh/RhAG proteins contribute substantially to the high permeability of the human red cell membrane for CO2. Together these proteins are responsible for 50% or more of the CO2 permeability of red cell membranes. The CO2 pathways of both proteins can be partly inhibited by DIDS, which is why this compound very effectively reduces membrane CO2 permeability.
Zentrum Physiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany.
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D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000494:pharmacology*; D051398:Aquaporin 1 / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D001692:Biological Transport; D001789:Blood Group Antigens / Q000235:genetics / Q000502:physiology*; D001798:Blood Proteins / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D002245:Carbon Dioxide / Q000097:blood*; D002463:Cell Membrane Permeability / Q000187:drug effects; D004375:Duffy Blood-Group System / Q000235:genetics / Q000502:physiology; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D017136:Ion Transport / Q000187:drug effects; D007626:Kell Blood-Group System / Q000235:genetics / Q000502:physiology; D007667:Kidd Blood-Group System / Q000235:genetics / Q000502:physiology; D008562:Membrane Glycoproteins / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D026901:Membrane Transport Proteins / Q000172:deficiency / Q000235:genetics / Q000502:physiology; D010313:Partial Pressure; D011956:Receptors, Cell Surface / Q000172:deficiency / Q000235:genetics / Q000502:physiology; D012204:Rh-Hr Blood-Group System / Q000235:genetics / Q000502:physiology; D000096982:Urea Transporters
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; D051398:Aquaporin 1; D001789:Blood Group Antigens; D001798:Blood Proteins; D002245:Carbon Dioxide; D004375:Duffy Blood-Group System; D007626:Kell Blood-Group System; D007667:Kidd Blood-Group System; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D011956:Receptors, Cell Surface; D012204:Rh-Hr Blood-Group System; D000096982:Urea Transporters; C473745:ACKR1 protein, human; C496020:AQP1 protein, human; C498523:RHAG protein, human