English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Receptor-mediated endocytosis of extracellular ANG II has been suggested to play an important role in the regulation of proximal tubule cell (PTC) function. Using immortalized rabbit PTCs as an in vitro cell culture model, we tested the hypothesis that extracellular ANG II is taken up by PTCs through angiotensin type 1 receptor (AT(1); or AT(1a)) receptor-mediated endocytosis and that inhibition of ANG II endocytosis using a selective AT(1) receptor small-interfering RNA (siRNA; AT(1)R siRNA) or endocytotic inhibitors exerts a physiological effect on total and apical sodium and hydrogen exchanger isoform 3 (NHE-3) protein abundance. Western blots and live cell imaging with FITC-labeled ANG II confirmed that transfection of PTCs with a human specific AT(1)R siRNA for 48 h selectively knocked down AT(1) receptor protein by 76 +/- 5% (P &lt; 0.01), whereas transfection with a scrambled siRNA had little effect. In nontransfected PTCs, exposure to extracellular ANG II (1 nM) for 60 min at 37 degrees C increased intracellular ANG II accumulation by 67% (control: 566 +/- 55 vs. ANG II: 943 +/- 160 pg/mg protein, P &lt; 0.05) and induced mitogen-activated protein kinase extracellular signal-regulated kinase (ERK) 1/2 phosphorylation (163 +/- 15% of control, P &lt; 0.01). AT(1)R siRNA reduced ANG II endocytosis to a level similar to losartan, which blocks cell surface AT(1) receptors (557 +/- 37 pg/mg protein, P &lt; 0.05 vs. ANG II), or to colchicine, which disrupts cytoskeleton microtubules (613 +/- 12 pg/mg protein, P &lt; 0.05 vs. ANG II). AT(1)R siRNA, losartan, and colchicine all attenuated ANG II-induced ERK1/2 activation and total cell lysate and apical membrane NHE-3 abundance. The scrambled siRNA had no effect on ANG II endocytosis, ERK1/2 activation, or NHE-3 expression. These results suggest that AT(1) receptor-mediated endocytosis of extracellular ANG II may regulate proximal tubule sodium transport by increasing total and apical NHE-3 proteins.

american journal of physiology. cell physiology

Selective knockdown of AT<sub>1</sub>receptors by RNA interference inhibits Val<sup>5</sup>-ANG II endocytosis and NHE-3 expression in immortalized rabbit proximal tubule cells

Selective knockdown of AT1receptors by RNA interference inhibits Val5-ANG II endocytosis and NHE-3 expression in immortalized rabbit proximal tubule cells

Selective knockdown of AT₁receptors by RNA interference inhibits Val⁵-ANG II endocytosis and NHE-3 expression in immortalized rabbit proximal tubule cells