Dataset Information

Postnatal expression of V2 vasopressin receptor splice variants in the rat cerebellum.

ABSTRACT: The V(2) vasopressin receptor gene contains an alternative splice site in exon-3, which leads to the generation of two splice variants (V(2a) and V(2b)) first identified in the kidney. The open reading frame of the alternatively spliced V(2b) transcript encodes a truncated receptor, showing the same amino acid sequence as the canonical V(2a) receptor up to the sixth transmembrane segment, but displaying a distinct sequence to the corresponding seventh transmembrane segment and C-terminal domain relative to the V(2a) receptor. Here, we demonstrate the postnatal expression of V(2a) and V(2b) variants in the rat cerebellum. Most importantly, we showed by in situ hybridization and immunocytochemistry that both V(2) splice variants were preferentially expressed in Purkinje cells, from early to late postnatal development. In addition, both variants were transiently expressed in the neuroblastic external granule cells and Bergmann fibers. These results indicate that the cellular distributions of both splice variants are developmentally regulated, and suggest that the transient expression of the V(2) receptor is involved in the mechanisms of cerebellar cytodifferentiation by AVP. Finally, transfected CHO-K1 expressing similar amounts of both V(2) splice variants, as that found in the cerebellum, showed a significant reduction in the surface expression of V(2a) receptors, suggesting that the differential expression of the V(2) splice variants regulates the vasopressin signaling in the cerebellum.

SUBMITTER: Vargas KJ

PROVIDER: S-EPMC2846433 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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Postnatal expression of V2 vasopressin receptor splice variants in the rat cerebellum.

Vargas Karina J KJ Sarmiento José M JM Ehrenfeld Pamela P Añazco Carolina C CC Villanueva Carolina I CI Carmona Pamela L PL Brenet Marianne M Navarro Javier J Müller-Esterl Werner W González Carlos B CB

Differentiation; research in biological diversity 20090120 4

The V(2) vasopressin receptor gene contains an alternative splice site in exon-3, which leads to the generation of two splice variants (V(2a) and V(2b)) first identified in the kidney. The open reading frame of the alternatively spliced V(2b) transcript encodes a truncated receptor, showing the same amino acid sequence as the canonical V(2a) receptor up to the sixth transmembrane segment, but displaying a distinct sequence to the corresponding seventh transmembrane segment and C-terminal domain ...[more]

PMID: 19281786

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Project description:Vasopressin controls water balance largely through PKA-dependent effects to regulate the collecting duct water channel aquaporin-2 (AQP2). Although considerable information has accrued regarding the regulation of water and solute transport in collecting duct cells, information is sparse regarding the signaling connections between PKA and transport responses. Here, we exploited recent advancements in protein mass spectrometry to perform a comprehensive, multiple-replicate analysis of changes in the phosphoproteome of native rat inner medullary collecting duct cells in response to the vasopressin V2 receptor-selective agonist 1-desamino-8D-arginine vasopressin. Of the 10,738 phosphopeptides quantified, only 156 phosphopeptides were significantly increased in abundance, and only 63 phosphopeptides were decreased, indicative of a highly selective response to vasopressin. The list of upregulated phosphosites showed several general characteristics: 1) a preponderance of sites with basic (positively charged) amino acids arginine (R) and lysine (K) in position -2 and -3 relative to the phosphorylated amino acid, consistent with phosphorylation by PKA and/or other basophilic kinases; 2) a greater-than-random likelihood of sites previously demonstrated to be phosphorylated by PKA; 3) a preponderance of sites in membrane proteins, consistent with regulation by membrane association; and 4) a greater-than-random likelihood of sites in proteins with class I COOH-terminal PDZ ligand motifs. The list of downregulated phosphosites showed a preponderance of those with proline in position +1 relative to the phosphorylated amino acid, consistent with either downregulation of proline-directed kinases (e.g., MAPKs or cyclin-dependent kinases) or upregulation of one or more protein phosphatases that selectively dephosphorylate such sites (e.g., protein phosphatase 2A). The phosphoproteomic data were used to create a web resource for the investigation of G protein-coupled receptor signaling and regulation of AQP2-mediated water transport.

Dataset Information

Postnatal expression of V2 vasopressin receptor splice variants in the rat cerebellum.

Publications

Postnatal expression of V2 vasopressin receptor splice variants in the rat cerebellum.

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