title: Effect of PCMBS on CO2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant.
abstract: A recent study on Xenopus oocytes [N. L. Nakhoul, M. F. Romero, B. A. Davis, and W. F. Boron. Am. J. Physiol. 274 (Cell Physiol. 43): C543-548, 1998] injected with carbonic anhydrase showed that expressing aquaporin 1 (AQP1) increases by approximately 40% the rate at which exposing the cell to CO2 causes intracellular pH to fall. This observation is consistent with several interpretations. Overexpressing AQP1 might increase apparent CO2 permeability by 1) allowing CO2 to pass through AQP1, 2) stimulating injected carbonic anhydrase, 3) enhancing the CO2 solubility of the membrane's lipid, or 4) increasing the expression of a native "gas channel." The purpose of the present study was to distinguish among these possibilities. We found that expressing the H2O channel AQP1 in Xenopus oocytes increases the CO2 permeability of oocytes in an expression-dependent fashion, whereas expressing the K+ channel ROMK1 has no effect. The mercury derivative p-chloromercuriphenylsulfonic acid (PCMBS), which inhibits the H2O movement through AQP1, also blocks the AQP1-dependent increase in CO2 permeability. The mercury-insensitive C189S mutant of AQP1 increases the CO2 permeability of the oocyte to the same extent as does the wild-type channel. However, the C189S-dependent increase in CO2 permeability is unaffected by treatment with PCMBS. These data rule out options 2-4 listed above. Thus our results suggest that CO2 passes through the pore of AQP1 and are the first data to demonstrate that a gas can enter a cell by a means other than diffusing through the membrane lipid.
authors.affiliation: Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
authors.forename: G J
authors.initials: GJ
authors.lastname: Cooper
authors.forename: W F
authors.initials: WF
authors.lastname: Boron
mesh_terms: D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology*; D000143:Acids / Q000378:metabolism; D000818:Animals; D051398:Aquaporin 1; D020346:Aquaporins / Q000235:genetics* / Q000378:metabolism*; D002245:Carbon Dioxide / Q000378:metabolism*; D002470:Cell Survival / Q000502:physiology; D005260:Female; D009154:Mutation / Q000502:physiology*; D009865:Oocytes / Q000378:metabolism* / Q000502:physiology; D010539:Permeability / Q000187:drug effects; D015221:Potassium Channels / Q000378:metabolism; D024661:Potassium Channels, Inwardly Rectifying; D014982:Xenopus laevis
chemical_list: D000143:Acids; D020346:Aquaporins; D015221:Potassium Channels; D024661:Potassium Channels, Inwardly Rectifying; D002245:Carbon Dioxide; D051398:Aquaporin 1; D002731:4-Chloromercuribenzenesulfonate