2008
DOI: 10.1152/ajpcell.00475.2007
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Regulation of apical NHE3 trafficking by ouabain-induced activation of the basolateral Na+-K+-ATPase receptor complex

Abstract: The long-term effects of ouabain on transepithelial Na+ transport involve transcriptional downregulation of apical Na+/H+ exchanger isoform 3 (NHE3). The aim of this study was to determine whether ouabain could acutely regulate NHE3 via a posttranscriptional mechanism in LLC-PK1 cells. We observed that the basolateral, but not apical, application of ouabain for 1 h significantly reduced transepithelial Na+ transport. This effect was not due to changes in the integrity of tight junctions or increases in the int… Show more

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Cited by 55 publications
(104 citation statements)
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“…Although disruption of the Na/K-ATPase⅐c-Src signaling (as in PY-17 and C2-9 cells) attenuated ouabain-stimulated protein carbonylation, studies with SYF/SYF ϩ c-Src cells and Src kinase inhibitor PP2 are consistent with our previous observations that ouabain stimulates a c-Src-dependent regulation of RPT Na/K-ATPase and NHE3 (13,21). Interestingly, GO-stimulated protein carbonylation was also attenuated in SYF cells, suggesting that the Na/K-ATPase⅐c-Src signaling complex is capable of functioning as a receptor complex for extracellular H 2 O 2 .…”
Section: Discussionsupporting
confidence: 90%
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“…Although disruption of the Na/K-ATPase⅐c-Src signaling (as in PY-17 and C2-9 cells) attenuated ouabain-stimulated protein carbonylation, studies with SYF/SYF ϩ c-Src cells and Src kinase inhibitor PP2 are consistent with our previous observations that ouabain stimulates a c-Src-dependent regulation of RPT Na/K-ATPase and NHE3 (13,21). Interestingly, GO-stimulated protein carbonylation was also attenuated in SYF cells, suggesting that the Na/K-ATPase⅐c-Src signaling complex is capable of functioning as a receptor complex for extracellular H 2 O 2 .…”
Section: Discussionsupporting
confidence: 90%
“…In LLC-PK1 cells, a low concentration of ouabain (up to 100 nM, about 1/10th of IC 50 ) does not inhibit 86 Rb ϩ uptake nor alter intracellular Na ϩ concentration when administered for up to 15 min (13, 47), but it does inhibit 86 Rb ϩ and Na ϩ uptake when administered for longer periods as we reported previously (13,47,48), due to ouabain-induced Na/K-ATPase endocytosis via Na/KATPase signaling (11,13,21,47,48). In LLC-PK1 cells, ouabain (1 h)-induced inhibition of transepithelial 22 Na ϩ flux is mostly dependent on the coordinated regulation of Na/K-ATPase and NHE3 through Na/K-ATPase signaling (13,21,47). Ouabain induced redistribution of Na/K-ATPase and NHE3 in LLC-PK1 cells, with a resultant reduction in cell surface levels of both transporters to depress apical Na ϩ entry through NHE3 (and other Na ϩ -coupled Na ϩ transporters) and basolateral Na ϩ extrusion through Na/K-ATPase.…”
Section: Discussionsupporting
confidence: 63%
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