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1 Institute of Anatomy, University of Aarhus, The Water and Salt Research Center, Aarhus, Denmark
* To whom correspondence should be addressed. E-mail: rofe{at}ana.au.dk.
Arginine vasopressin (AVP) is essential for body fluid homeostasis. The antidiuretic effects of AVP are initialized by binding of AVP to the type 2 vasopressin receptor (V2R) in the kidney collecting duct (CD), resulting in exocytic insertion of aquaporin-2 water channels into the plasma membrane. In this article we describe the generation and characterization of an antibody targeted against the NH2-terminal of the rat V2R. HEK293 cells over-expressing the rat, mouse or human V2R showed strong intracellular immunolabeling. Additionally, immunostaining of M-1 kidney cells expressing a V2R-GFP fusion construct showed co-localization between GFP and antibody specific V2R labeling. Immunoblots of rat kidney showed 43- and 47kDa proteins in all zones that were reduced to 34kDa by N-glycosidase F. Protein solubilization with nonionic detergents or the use of homobifunctional cross-linkers demonstrated that rat V2R exists as a protein complex in native kidney. Immunohistochemistry of rat and mouse kidney revealed abundant labeling of the CD. Double labeling confocal immunofluorescence microscopy (using DCT / CNT specific marker calbindin and CNT / CD specific marker AQP-2) showed V2R labeling in both CD and CNT. There was no immunolabeling in vascular structures and other renal tubules, including the TAL, although RT-PCR of microdissected tubules showed expression of V2R mRNA in TAL. Confocal microscopy demonstrated that at the subcellular level, V2R labeling was predominantly intracellular in normal kidneys, although some staining was apparent in basolateral membrane domains. Confocal microscopy of isolated IMCD tubules showed that the V2R is expressed both intracellularly and in basolateral membrane domains.
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