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J Biol Chem, Vol. 273, Issue 50, 33123-33126, December 11, 1998

COMMUNICATION
Reconstituted Aquaporin 1 Water Channels Transport CO₂ across Membranes

From the Laboratory of Epithelial Cell Biology, Renal Electrolyte Division, and Protein Purification Laboratory, Department of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213

Biological membranes provide selective barriers to a number of molecules and gases. However, the factors that affect permeability to gases remain unclear because of the difficulty of accurately measuring gas movements. To determine the roles of lipid composition and the aquaporin 1 (AQP1) water channel in altering CO₂ flux across membranes, we developed a fluorometric assay to measure CO₂ entry into vesicles. Maximal CO₂ flux was ~1000-fold above control values with 0.5 mg/ml carbonic anhydrase. Unilamellar phospholipid vesicles of varying composition gave widely varying water permeabilities but similar CO₂ permeabilities at 25 °C. When AQP1 purified from human red blood cells was reconstituted into proteoliposomes, however, it increased water and CO₂ permeabilities markedly. Both increases were abolished with HgCl₂, and the mercurial inhibition was reversible with -mercaptoethanol. We conclude that unlike water and small nonelectrolytes, CO₂ permeation is not significantly altered by lipid bilayer composition or fluidity. AQP1 clearly serves to increase CO₂ permeation, likely through the water pore; under certain circumstances, gas permeation through membranes is protein-mediated.

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