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1 Department of Woman and Child Health, Karolinska Institute, St. Göran's Children's Hospital, 112 81 Stockholm, Sweden; 2 Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK-8000 Aarhus, Denmark; and 3 Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021-6399
Aquaporin-2 (AQP2), the protein that mediates arginine
vasopressin (AVP)-regulated apical water transport in the renal
collecting duct, possesses a single consensus phosphorylation site for
cAMP-dependent protein kinase A (PKA) at
Ser256. The aim of this study was
to examine whether AVP, and other agents that increase cAMP levels,
could stimulate the phosphorylation of AQP2 in intact rat renal tissue.
Rat renal papillae were prelabeled with
32P and incubated with vehicle or
drugs, and then AQP2 was immunoprecipitated. Two polypeptides
corresponding to nonglycosylated (29 kDa) and glycosylated (35-48
kDa) AQP2 were identified by SDS-PAGE. AVP caused a time- and
dose-dependent increase in phosphorylation of both glycosylated and
nonglycosylated AQP2. The threshold dose for a significant increase in
phosphorylation was 10 pM, which corresponds to a physiological serum
concentration of AVP. Maximal phosphorylation was reached within 1 min
of AVP incubation. This effect on AQP2 phosphorylation was mimicked by
the vasopressin (V2) agonist,
1-desamino-[8-D-arginine]vasopressin
(DDAVP), or forskolin. Two-dimensional phosphopeptide mapping indicated
that AVP and forskolin stimulated the phosphorylation of the same site in AQP2. Immunoblot analysis using a phosphorylation state-specific antiserum revealed an increase in phosphorylation of
Ser256 after incubation of
papillae with AVP. The results indicate that AVP stimulates
phosphorylation of AQP2 at Ser256
via activation of PKA, supporting the idea that this is one of the
first steps leading to increased water permeability in collecting duct cells.
adenosine 3',5'-cyclic monophosphate; collecting duct cells; protein kinase A; vasopressin receptor; water permeability
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