<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Faust D</submitter><pubmed_abstract>Arginine-vasopressin (AVP) facilitates water reabsorption by renal collecting duct principal cells and thereby fine-tunes body water homeostasis. AVP binds to vasopressin V2 receptors (V2R) on the surface of the cells and thereby induces synthesis of cAMP. This stimulates cellular signaling processes leading to changes in the phosphorylation of the water channel aquaporin-2 (AQP2). Protein kinase A phoshorylates AQP2 and thereby triggers the translocation of AQP2 from intracellular vesicles into the plasma membrane facilitating water reabsorption from primary urine. Aberrations of AVP release from the pituitary or AVP-activated signaling in principal cells can cause central or nephrogenic diabetes insipidus, respectively; an elevated blood plasma AVP level is associated with cardiovascular</pubmed_abstract><journal>Journal of visualized experiments : JoVE</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3728753</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Culturing primary rat inner medullary collecting duct cells.</pubmed_title><pmcid>PMC3728753</pmcid><pubmed_authors>Wiesner B</pubmed_authors><pubmed_authors>Rosenthal W</pubmed_authors><pubmed_authors>Geelhaar A</pubmed_authors><pubmed_authors>Eisermann B</pubmed_authors><pubmed_authors>Klussmann E</pubmed_authors><pubmed_authors>Faust D</pubmed_authors><pubmed_authors>Eichhorst J</pubmed_authors><pubmed_authors>Klussman E</pubmed_authors></additional><is_claimable>false</is_claimable><name>Culturing primary rat inner medullary collecting duct cells.</name><description>Arginine-vasopressin (AVP) facilitates water reabsorption by renal collecting duct principal cells and thereby fine-tunes body water homeostasis. AVP binds to vasopressin V2 receptors (V2R) on the surface of the cells and thereby induces synthesis of cAMP. This stimulates cellular signaling processes leading to changes in the phosphorylation of the water channel aquaporin-2 (AQP2). Protein kinase A phoshorylates AQP2 and thereby triggers the translocation of AQP2 from intracellular vesicles into the plasma membrane facilitating water reabsorption from primary urine. Aberrations of AVP release from the pituitary or AVP-activated signaling in principal cells can cause central or nephrogenic diabetes insipidus, respectively; an elevated blood plasma AVP level is associated with cardiovascular</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Jun</publication><modification>2026-07-09T11:51:17.694Z</modification><creation>2026-07-09T11:02:24.088Z</creation></dates><accession>S-EPMC3728753</accession><cross_references><pubmed>23852264</pubmed><doi>10.3791/50366</doi></cross_references></HashMap>