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Aquaporin-1 and HCO₃^--Cl^- transporter-mediated transport of CO₂ across the human erythrocyte membrane

Michael E. Blank and Heimo Ehmke

Recent studies have suggested that aquaporin-1 (AQP1) as well as the HCO₃^--Cl^- transporter may be involved in CO₂ transport across biological membranes, but the physiological importance of this route of gas transport remained unknown. We studied CO₂ transport in human red blood cell ghosts at physiological temperatures (37 °C). Replacement of inert with CO₂-containing gas above a stirred cell suspension caused an outside-to-inside directed CO₂ gradient and generated a rapid biphasic intracellular acidification. The gradient of the acidifying gas was kept small to favour high affinity entry of CO₂ passing the membrane. All rates of acidification except that of the approach to physicochemical equilibrium of the uncatalysed reaction were restricted to the intracellular environment. Inhibition of carbonic anhydrase (CA) demonstrated that CO₂-induced acidification required the catalytic activity of CA. Blockade of the function of either AQP1 (by HgCl₂ at 65 µM) or the HCO₃^--Cl^- transporter (by DIDS at 15 µM) completely prevented fast acidification. These data indicate that, at low chemical gradients for CO₂, nearly the entire CO₂ transport across the red cell membrane is mediated by AQP1 and the HCO₃^--Cl^- transporter. Therefore, these proteins may function as high affinity sites for CO₂ transport across the erythrocyte membrane.

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