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1 Service of Nephrology, Fondation pour Recherches Medicales, Geneva, GE, Switzerland
2 The Water and Salt Research Center, University of Aarhus, Aarhus, Denmark
* To whom correspondence should be addressed. E-mail: Eric.Feraille{at}medecine.unige.ch.
Prevailing expression levels of aquaporin-2 (AQP2) mRNA play a major role in regulating AQP2 protein abundance. Here, we investigated whether AQP2 protein abundance is regulated at a post-transcriptional level as well. The expression levels of both AQP2 mRNA and protein increase in response to vasopressin (AVP) in a concentration- and time-dependent manner in cultured immortalized mouse collecting duct principal cells (mpkCCDcl4 cells). AVP washout from the medium of AVP-pretreated cells revealed that AQP2 mRNA expression progressively decreased over time while AQP2 protein abundance first increased immediately following AVP washout and then gradually decreased over time. Inversely, increasing AVP concentration led to a time-dependent increase of AQP2 mRNA while AQP2 protein abundance first decreased immediately following AVP supplementation and then gradually increased over time. These transient effects arose from altered V2-receptor activity since they could be abolished by SR121463B, a specific V2-receptor antagonist. While cycloheximide administration had no effect on transient alterations of AQP2 protein content these effects were attenuated by administration of chloroquine, a lysosomal inhibitor, or lactacystin, a proteasomal inhibitor. Short-term inhibition of PKA activity significantly increased AQP2 protein abundance and blunted the transient alterations of AQP2 protein content induced by AVP washout and supplementation. In addition, phosphorylated AQP2 abundance increased immediately following AVP supplementation. These results indicate that in response to AVP AQP2 protein abundance in collecting duct principal cells is principally influenced by AQP2 mRNA content but is additionally regulated by PKA-dependent negative feed-back acting on AQP2 protein degradation.
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