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Vol. 57, Issue 3, 576-588, March 2000
Departments of Physiology (H.L.B., G.M.Y., A.J.Y.), Pharmacology
(J.W.R., A.J.Y.), and Pharmacology and Toxicology (T.L.A., S.L.,
J.W.R.), University of Arizona College of Pharmacy, Tucson, Arizona;
and Programs in Pharmacology and Toxicology (G.M.Y., J.W.R., A.J.Y.)
and Neuroscience (D.B., J.W.R., A.J.Y.), University of Arizona, Tucson,
Arizona
Aquaporin-1 (AQP1) is a member of the membrane intrinsic protein (MIP)
gene family and is known to provide pathways for water flux across cell
membranes. We show here that cloned human AQP1 not only mediates water
flux but also serves as a cGMP-gated ion channel. Two-electrode
voltage-clamp analyses showed consistent activation of an ionic
conductance in wild-type AQP1-expressing oocytes after the direct
injection of cGMP (50 nl of 100 mM). Current activation was not
observed in control (water-injected) oocytes or in AQP5-expressing
oocytes with osmotic water permeabilities equivalent to those seen with
AQP1. Patch-clamp recordings revealed large conductance channels (150 pS in K+ saline) in excised patches from AQP1-expressing
oocytes after the application of cGMP to the internal side. Amino acid
sequence alignments between AQP1 and sensory cyclic-nucleotide-gated
channels showed similarities between the cyclic-nucleotide-gated
binding domain and the AQP1 carboxyl terminus that were not present in AQP5. Competitive radioligand-binding assays with
[3H]cGMP demonstrated specific binding
(KD = 0.2 µM) in AQP1-expressing Sf9 cells but not in controls. These results indicate that AQP1 channels have the capacity to participate in ionic signaling after the
activation of cGMP second-messenger pathways.
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