Publications

• Relative CO(2)/NH(3) permeabilities of human RhAG, RhBG and RhCG.

  Geyer R.R., Parker M.D., Toye A.M., Boron W.F., Musa-Aziz R.

  Mammalian glycosylated rhesus (Rh) proteins include the erythroid RhAG and the nonerythroid RhBG and RhCG. RhBG and RhCG are expressed in multiple tissues, including hepatocytes and the collecting duct (CD) of the kidney. Here, we expressed human RhAG, RhBG and RhCG in Xenopus oocytes (vs. H2O-inj ... >> More

  Mammalian glycosylated rhesus (Rh) proteins include the erythroid RhAG and the nonerythroid RhBG and RhCG. RhBG and RhCG are expressed in multiple tissues, including hepatocytes and the collecting duct (CD) of the kidney. Here, we expressed human RhAG, RhBG and RhCG in Xenopus oocytes (vs. H2O-injected control oocytes) and used microelectrodes to monitor the maximum transient change in surface pH (DpHS) caused by exposing the same oocyte to 5 % CO₂/33 mM HCO₃⁻ (an increase) or 0.5 mM NH₃/NH₄⁺ (a decrease). Subtracting the respective values for day-matched, H₂O-injected control oocytes yielded channel-specific values (*). (ΔpH*(S))(CO₂) and (-ΔpH*(S))(NH₃) were each significantly >0 for all channels, indicating that RhBG and RhCG--like RhAG--can carry CO₂ and NH₃. We also investigated the role of a conserved aspartate residue, which was reported to inhibit NH₃ transport. However, surface biotinylation experiments indicate the mutants RhBG(D178N) and RhCG(D177N) have at most a very low abundance in the oocyte plasma membrane. We demonstrate for the first time that RhBG and RhCG--like RhAG--have significant CO₂ permeability, and we confirm that RhAG, RhBG and RhCG all have significant NH₃ permeability. However, as evidenced by (ΔpH*(S))(CO₂)/ (-ΔpH*(S))(NH₃) values, we could not distinguish among the CO₂/ NH₃ permeability ratios for RhAG, RhBG and RhCG. Finally, we propose a mechanism whereby RhBG and RhCG contribute to acid secretion in the CD by enhancing the transport of not only NH₃ but also CO₂ across the membranes of CD cells. << Less

  J. Membr. Biol. 246:915-926(2013) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Laccaria bicolor aquaporin LbAQP1 is required for Hartig net development in trembling aspen (Populus tremuloides).

  Navarro-RoDenas A., Xu H., Kemppainen M., Pardo A.G., Zwiazek J.J.

  The development of ectomycorrhizal associations is crucial for growth of many forest trees. However, the signals that are exchanged between the fungus and the host plant during the colonization process are still poorly understood. In this study, we have identified the relationship between expressi ... >> More

  The development of ectomycorrhizal associations is crucial for growth of many forest trees. However, the signals that are exchanged between the fungus and the host plant during the colonization process are still poorly understood. In this study, we have identified the relationship between expression patterns of Laccaria bicolor aquaporin LbAQP1 and the development of ectomycorrhizal structures in trembling aspen (Populus tremuloides) seedlings. The peak expression of LbAQP1 was 700-fold higher in the hyphae within the root than in the free-living mycelium after 24 h of direct interaction with the roots. Moreover, in LbAQP1 knock-down strains, a non-mycorrhizal phenotype was developed without the Hartig net and the expression of the mycorrhizal effector protein MiSSP7 quickly declined after an initial peak on day 5 of interaction of the fungal hyphae with the roots. The increase in the expression of LbAQP1 required a direct contact of the fungus with the root and it modulated the expression of MiSSP7. We have also determined that LbAQP1 facilitated NO, H2 O2 and CO2 transport when heterologously expressed in yeast. The report demonstrates that the L. bicolor aquaporin LbAQP1 acts as a molecular signalling channel, which is fundamental for the development of Hartig net in root tips of P. tremuloides. << Less

  Plant Cell Environ. 38:2475-2486(2015) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Reconstituted aquaporin 1 water channels transport CO2 across membranes.

  Prasad G.V., Coury L.A., Finn F., Zeidel M.L.

  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 ch ... >> More

  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 approximately 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 degreesC. 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 beta-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. << Less

  J Biol Chem 273:33123-33126(1998) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.