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10.1152/ajprenal.00693.2013 http://scihub22266oqcxt.onion/10.1152/ajprenal.00693.2013 C4101628!4101628 !24740791     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24740791 &cmd=llinks): Failed to open stream: HTTP request failed! 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Mechanisms of AT1a receptor-mediated uptake of angiotensin II by proximal tubule cells: a novel role of the multiligand endocytic receptor megalin |pdf=|usr=}}{{24740791 }} gab.com Text Mechanisms of AT1a receptor-mediated uptake of angiotensin II by proximal tubule cells: a novel role of the multiligand endocytic receptor megalin JO: Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=24740791 #FOAvip The present study tested the hypothesis that the multiligand endocytic receptor megalin is partially involved in the uptake of ANG II and downstream signaling responses in mouse proximal tubule cells (mPCT) by interacting with AT1a receptors. mPCT cells of wild-type (WT) and AT1a receptor-deficient (AT1a-KO) mice were treated with vehicle, the AT1 receptor blocker losartan (10 ?M), or a selective megalin small interfering (si) RNA for 48 h. The uptake of fluorescein (FITC)-labeled ANG II (10 nM, 37°C) and downstream signaling responses were analyzed by fluorescence imaging and Western blotting. AT1a receptors and megalin were abundantly expressed in mPCT cells, whereas AT1a receptors were absent in AT1a-KO mPCT cells (P < 0.01). In WT mPCT cells, FITC-ANG II uptake was visualized at 30 min in the cytoplasm and in the nuclei 1 h after exposure. Losartan alone completely blocked the uptake of FITC-ANG II, whereas megalin siRNA inhibited only 30% of the response (P < 0.01). The remaining FITC-ANG II uptake in the presence of megalin siRNA was completely abolished by losartan. ANG II induced threefold increases in phosphorylated MAP kinases ERK1/2 and a onefold increase in phosphorylated sodium and hydrogen exchanger 3 (NHE3) proteins, which were also blocked by losartan and megalin-siRNA. By contrast, losartan and megalin siRNA had no effects on these signaling proteins in AT1a-KO mPCT cells. We conclude that the uptake of ANG II and downstream MAP kinases ERK1/2 and NHE3 signaling responses in mPCT cells are mediated primarily by AT1a receptors. However, megalin may also play a partial role in these responses to ANG II. Twit Text FOAVip Mechanisms of AT1a receptor-mediated uptake of angiotensin II by proximal tubule cells: a novel role of the multiligand endocytic receptor megalin ????Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=24740791 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24740791 #FOAvip English Wikipedia <ref>{{Cite pmid|24740791 }}</ref> Mechanisms of AT1a receptor-mediated uptake of angiotensin II by proximal tubule cells: a novel role of the multiligand endocytic receptor megalin #MMPMID24740791 Li XC ; Zhuo JL Am J Physiol Renal Physiol 2014[Jul]; 307 (2 ): F222-33 PMID24740791 show ga The present study tested the hypothesis that the multiligand endocytic receptor megalin is partially involved in the uptake of ANG II and downstream signaling responses in mouse proximal tubule cells (mPCT) by interacting with AT1a receptors. mPCT cells of wild-type (WT) and AT1a receptor-deficient (AT1a-KO) mice were treated with vehicle, the AT1 receptor blocker losartan (10 ?M), or a selective megalin small interfering (si) RNA for 48 h. The uptake of fluorescein (FITC)-labeled ANG II (10 nM, 37°C) and downstream signaling responses were analyzed by fluorescence imaging and Western blotting. AT1a receptors and megalin were abundantly expressed in mPCT cells, whereas AT1a receptors were absent in AT1a-KO mPCT cells (P < 0.01). In WT mPCT cells, FITC-ANG II uptake was visualized at 30 min in the cytoplasm and in the nuclei 1 h after exposure. Losartan alone completely blocked the uptake of FITC-ANG II, whereas megalin siRNA inhibited only 30% of the response (P < 0.01). The remaining FITC-ANG II uptake in the presence of megalin siRNA was completely abolished by losartan. ANG II induced threefold increases in phosphorylated MAP kinases ERK1/2 and a onefold increase in phosphorylated sodium and hydrogen exchanger 3 (NHE3) proteins, which were also blocked by losartan and megalin-siRNA. By contrast, losartan and megalin siRNA had no effects on these signaling proteins in AT1a-KO mPCT cells. We conclude that the uptake of ANG II and downstream MAP kinases ERK1/2 and NHE3 signaling responses in mPCT cells are mediated primarily by AT1a receptors. However, megalin may also play a partial role in these responses to ANG II. |*Endocytosis/drug effects [MESH] |Angiotensin II Type 1 Receptor Blockers/pharmacology [MESH] |Angiotensin II/analogs & derivatives/*metabolism [MESH] |Animals [MESH] |Cells, Cultured [MESH] |Enzyme Activation [MESH] |Extracellular Signal-Regulated MAP Kinases/metabolism [MESH] |Fluorescein-5-isothiocyanate/analogs & derivatives/metabolism [MESH] |Kidney Tubules, Proximal/drug effects/*metabolism [MESH] |Ligands [MESH] |Losartan/pharmacology [MESH] |Low Density Lipoprotein Receptor-Related Protein-2/genetics/*metabolism [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |Mice, Knockout [MESH] |Phosphorylation [MESH] |RNA Interference [MESH] |Receptor, Angiotensin, Type 1/deficiency/drug effects/genetics/*metabolism [MESH] |Signal Transduction [MESH] |Sodium-Hydrogen Exchanger 3 [MESH] |Sodium-Hydrogen Exchangers/metabolism [MESH]Mechanisms of AT1a receptor-mediated uptake of angiotensin II by proxi(epmc).pdf DeepDyve Pubget Overpricing