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J. Biol. Chem., Vol. 275, Issue 47, 36839-36846, November 24, 2000
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From the In the renal collecting duct, vasopressin
increases osmotic water permeability (Pf) by
triggering trafficking of aquaporin-2 vesicles to the apical plasma
membrane. We investigated the role of vasopressin-induced intracellular
Ca2+ mobilization in this process. In isolated inner
medullary collecting ducts (IMCDs), vasopressin (0.1 nM)
and 8-(4-chlorophenylthio)-cAMP (0.1 mM) elicited marked
increases in [Ca2+]i (fluo-4).
Vasopressin-induced Ca2+ mobilization was completely
blocked by preloading with the Ca2+ chelator BAPTA. In
parallel experiments, BAPTA completely blocked the vasopressin-induced
increase in Pf without affecting adenosine
3',5'-cyclic monophosphate (cAMP) production. Previously, we
demonstrated the lack of activation of the phosphoinositide-signaling pathway by vasopressin in IMCD, suggesting an inositol
1,4,5-trisphosphate-independent mechanism of Ca2+ release.
Evidence for expression of the type 1 ryanodine receptor (RyR1) in IMCD
was obtained by immunofluorescence, immunoblotting, and reverse
transcription-polymerase chain reaction. Ryanodine (100 µM), a ryanodine receptor antagonist, blocked the
arginine vasopressin-mediated increase in Pf and
blocked vasopressin-stimulated redistribution of aquaporin-2 to the
plasma membrane domain in primary cultures of IMCD cells, as assessed
by immunofluorescence immunocytochemistry. Calmodulin inhibitors (W7
and trifluoperazine) blocked the Pf response to
vasopressin and the vasopressin-stimulated redistribution of
aquaporin-2. The results suggest that Ca2+ release from
ryanodine-sensitive stores plays an essential role in
vasopressin-mediated aquaporin-2 trafficking via a
calmodulin-dependent mechanism.
Regulation of Aquaporin-2 Trafficking by Vasopressin in the Renal
Collecting Duct
ROLES OF RYANODINE-SENSITIVE Ca2+ STORES AND
CALMODULIN*
,,,,
Laboratory of Kidney and Electrolyte
Metabolism, NHLBI, National Institutes of Health, Bethesda, Maryland
20892, § Department of Physiology and Biophysics, College of
Medicine, University of South Florida, Tampa, Florida 33612, and
¶ Department of Physiology, School of Medicine, University of
Maryland, Baltimore, Maryland 21201
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Laboratory of
Kidney and Electrolyte Metabolism, NHLBI, National Institutes of Health, 10 Center Dr., MSC 1603, Bldg. 10, Rm. 6N260, Bethesda, MD
20892. Tel.: 301-496-3064; Fax: 301-402-1443; E-mail:
knep@helix.nih.gov.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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