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10.1152/ajprenal.00141.2014 http://scihub22266oqcxt.onion/10.1152/ajprenal.00141.2014 C4187043!4187043 !25100281     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25100281 &cmd=llinks): Failed to open stream: HTTP request failed! 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Angiotensin II type 2 receptor regulates ROMK-like K? channel activity in the renal cortical collecting duct during high dietary K? adaptation |pdf=|usr=}}{{25100281 }} gab.com Text Angiotensin II type 2 receptor regulates ROMK-like K channel activity in the renal cortical collecting duct during high dietary K adaptation JO: Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=25100281 #FOAvip The kidney adjusts K? excretion to match intake in part by regulation of the activity of apical K? secretory channels, including renal outer medullary K? (ROMK)-like K? channels, in the cortical collecting duct (CCD). ANG II inhibits ROMK channels via the ANG II type 1 receptor (AT1R) during dietary K? restriction. Because AT1Rs and ANG II type 2 receptors (AT2Rs) generally function in an antagonistic manner, we sought to characterize the regulation of ROMK channels by the AT2R. Patch-clamp experiments revealed that ANG II increased ROMK channel activity in CCDs isolated from high-K? (HK)-fed but not normal K? (NK)-fed rats. This response was blocked by PD-123319, an AT2R antagonist, but not by losartan, an AT1R antagonist, and was mimicked by the AT2R agonist CGP-42112. Nitric oxide (NO) synthase is present in CCD cells that express ROMK channels. Blockade of NO synthase with N-nitro-l-arginine methyl ester and free NO with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide potassium salt completely abolished ANG II-stimulated ROMK channel activity. NO enhances the synthesis of cGMP, which inhibits phosphodiesterases (PDEs) that normally degrade cAMP; cAMP increases ROMK channel activity. Pretreatment of CCDs with IBMX, a broad-spectrum PDE inhibitor, or cilostamide, a PDE3 inhibitor, abolished the stimulatory effect of ANG II on ROMK channels. Furthermore, PKA inhibitor peptide, but not an activator of the exchange protein directly activated by cAMP (Epac), also prevented the stimulatory effect of ANG II. We conclude that ANG II acts at the AT2R to stimulate ROMK channel activity in CCDs from HK-fed rats, a response opposite to that mediated by the AT1R in dietary K?-restricted animals, via a NO/cGMP pathway linked to a cAMP-PKA pathway. Twit Text FOAVip Angiotensin II type 2 receptor regulates ROMK-like K channel activity in the renal cortical collecting duct during high dietary K adaptation ????Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=25100281 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25100281 #FOAvip English Wikipedia <ref>{{Cite pmid|25100281 }}</ref> Angiotensin II type 2 receptor regulates ROMK-like K? channel activity in the renal cortical collecting duct during high dietary K? adaptation #MMPMID25100281 Wei Y ; Liao Y ; Zavilowitz B ; Ren J ; Liu W ; Chan P ; Rohatgi R ; Estilo G ; Jackson EK ; Wang WH ; Satlin LM Am J Physiol Renal Physiol 2014[Oct]; 307 (7 ): F833-43 PMID25100281 show ga The kidney adjusts K? excretion to match intake in part by regulation of the activity of apical K? secretory channels, including renal outer medullary K? (ROMK)-like K? channels, in the cortical collecting duct (CCD). ANG II inhibits ROMK channels via the ANG II type 1 receptor (AT1R) during dietary K? restriction. Because AT1Rs and ANG II type 2 receptors (AT2Rs) generally function in an antagonistic manner, we sought to characterize the regulation of ROMK channels by the AT2R. Patch-clamp experiments revealed that ANG II increased ROMK channel activity in CCDs isolated from high-K? (HK)-fed but not normal K? (NK)-fed rats. This response was blocked by PD-123319, an AT2R antagonist, but not by losartan, an AT1R antagonist, and was mimicked by the AT2R agonist CGP-42112. Nitric oxide (NO) synthase is present in CCD cells that express ROMK channels. Blockade of NO synthase with N-nitro-l-arginine methyl ester and free NO with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide potassium salt completely abolished ANG II-stimulated ROMK channel activity. NO enhances the synthesis of cGMP, which inhibits phosphodiesterases (PDEs) that normally degrade cAMP; cAMP increases ROMK channel activity. Pretreatment of CCDs with IBMX, a broad-spectrum PDE inhibitor, or cilostamide, a PDE3 inhibitor, abolished the stimulatory effect of ANG II on ROMK channels. Furthermore, PKA inhibitor peptide, but not an activator of the exchange protein directly activated by cAMP (Epac), also prevented the stimulatory effect of ANG II. We conclude that ANG II acts at the AT2R to stimulate ROMK channel activity in CCDs from HK-fed rats, a response opposite to that mediated by the AT1R in dietary K?-restricted animals, via a NO/cGMP pathway linked to a cAMP-PKA pathway. |Adaptation, Physiological [MESH] |Animals [MESH] |Female [MESH] |Kidney Tubules, Collecting/*metabolism [MESH] |Male [MESH] |Patch-Clamp Techniques [MESH] |Potassium Channels, Inwardly Rectifying/*metabolism [MESH] |Potassium, Dietary/*metabolism [MESH] |Rats, Sprague-Dawley [MESH]Angiotensin II type 2 receptor regulates ROMK-like K? channel activity(epmc).pdf DeepDyve Pubget Overpricing