ArticleThe Journal of physiology1998
Protein kinase A induces recruitment of active Na+,K+-ATPase units to the plasma membrane of rat proximal convoluted tubule cells.
Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 77 citations in OpenAlex.
- Repurposed cAMP-Modulating Agents Enhance 5-Fluorouracil Response Through Membrane-Dependent Mechanisms.Membranes · 2026Review
- Role of the adenylate cyclase/cyclic AMP pathway in oxytocin-induced lacrimal gland myoepithelial cells contraction.Experimental eye research · 2023Article
- Cell death signaling inExperimental biology and medicine (Maywood, N.J.) · 2023Article
- Ecstasy metabolites and monoamine neurotransmitters upshift the NaArchives of toxicology · 2022Article
- PGE2 upregulates the Na+/K+ ATPase in HepG2 cells via EP4 receptors and intracellular calcium.PloS one · 2021Article
- Phosphorylation of rat kidney Na-K pump at Ser938 is required for rapid angiotensin II-dependent stimulation of activity and trafficking in proximal tubule cells.American journal of physiology. Cell physiology · 2016Article
- Glucose-dependent insulinotropic polypeptide-mediated signaling pathways enhance apical PepT1 expression in intestinal epithelial cells.American journal of physiology. Gastrointestinal and liver physiology · 2015Article
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- Interaction between Calcineurin and Ca/Calmodulin Kinase-II in Modulating Cellular Functions.Enzyme research · 2011Article
- Insulin regulates alveolar epithelial function by inducing Na+/K+-ATPase translocation to the plasma membrane in a process mediated by the action of Akt.Journal of cell science · 2010Article
- Role of calcineurin-mediated dephosphorylation in modulation of an inwardly rectifying K+ channel in human proximal tubule cells.The Journal of membrane biology · 2009Article
- Vasotocin has the potential to inhibit basolateral Na(+)/K (+)-pump current across isolated skin of tree frog in vitro, via its V(2)-type receptor/cAMP pathway.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2008Article
- Differential expression of Na+/K+-ATPase alpha-subunits in mouse hippocampal interneurones and pyramidal cells.The Journal of physiology · 2007Article
- SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Identification of a cytoskeleton-bound form of phospholemman with unique C-terminal immunoreactivity.The Journal of membrane biology · 2004Article
- The GTP-binding protein RhoA mediates Na,K-ATPase exocytosis in alveolar epithelial cells.Molecular biology of the cell · 2003Article
- Intracellular Na+ controls cell surface expression of Na,K-ATPase via a cAMP-independent PKA pathway in mammalian kidney collecting duct cells.Molecular biology of the cell · 2003Article
- Hypoxia-induced endocytosis of Na,K-ATPase in alveolar epithelial cells is mediated by mitochondrial reactive oxygen species and PKC-zeta.The Journal of clinical investigation · 2003Article
- Analysis of Na+,K+-ATPase motion and incorporation into the plasma membrane in response to G protein-coupled receptor signals in living cells.Molecular biology of the cell · 2003Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. The aim of this study was to investigate the mechanism of control of Na+,K+-ATPase activity by the cAMP-protein kinase A (PKA) pathway in rat proximal convoluted tubules. For this purpose, we studied the in vitro action of exogenous cAMP (10-3 M dibutyryl-cAMP (db-cAMP) or 8-bromo-cAMP) and endogenous cAMP (direct activation of adenylyl cyclases by 10-5 M forskolin) on Na+,K+-ATPase activity and membrane trafficking. 2. PKA activation stimulated both the cation transport and hydrolytic activity of Na+,K+-ATPase by about 40%. Transport activity stimulation was specific to the PKA signalling pathway since (1) db-cAMP stimulated the ouabain-sensitive 86Rb+ uptake in a time- and dose-dependent fashion; (2) this effect was abolished by addition of H-89 or Rp-cAMPS, two structurally different PKA inhibitors; and (3) this stimulation was not affected by inhibition of protein kinase C (PKC) by GF109203X. The stimulatory effect of db-cAMP on the hydrolytic activity of Na+,K+-ATPase was accounted for by an increased maximal ATPase rate (Vmax) without alteration of the efficiency of the pump, suggesting that cAMP-PKA pathway was implicated in membrane redistribution control. 3. To test this hypothesis, we used two different approaches: (1) cell surface protein biotinylation and (2) subcellular fractionation. Both approaches confirmed that the cAMP-PKA pathway was implicated in membrane trafficking regulation. The stimulation of Na+,K+-ATPase activity by db-cAMP was associated with an increase (+40%) in Na+, K+-ATPase units expressed at the cell surface which was assessed by Western blotting after streptavidin precipitation of biotinylated cell surface proteins. Subcellular fractionation confirmed the increased expression in pump units at the cell surface which was accompanied by a decrease (-30%) in pump units located in the subcellular fraction corresponding to early endosomes. 4. In conclusion, PKA stimulates Na+,K+-ATPase activity, at least in part, by increasing the number of Na+-K+ pumps in the plasma membrane in proximal convoluted tubule cells.
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