ArticleAmerican journal of physiology. Renal physiology2008
PTH-mediated regulation of Na+-K+-ATPase requires Src kinase-dependent ERK phosphorylation.
Article in American journal of physiology. Renal physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Na/K-ATPase in the renal proximal tubule cell: classic & novel roles in sodium handling.Frontiers in physiology · 2026Review
- Endogenous Cardiac Steroids in Bipolar Disorder: State of the Art.International journal of molecular sciences · 2022Review
- Role of endogenous ouabain in the etiology of bipolar disorder.International journal of bipolar disorders · 2021Review
- Effect of photobiomodulation therapy on neuronal injuries by ouabain: the regulation of Na, K-ATPase; Src; and mitogen-activated protein kinase signaling pathway.BMC neuroscience · 2019Article
- Effects of phospho- and calciotropic hormones on electrolyte transport in the proximal tubule.F1000Research · 2017Review
- Low dose ouabain stimulates NaK ATPase α1 subunit association with angiotensin II type 1 receptor in renal proximal tubule cells.Biochimica et biophysica acta · 2016Article
- Protein-DNA Interactions at the Opossum Npt2a Promoter are Dependent upon NHERF-1.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2016Article
- Nitric oxide regulation of Na, K-ATPase activity in ocular ciliary epithelium involves Src family kinase.Journal of cellular physiology · 2014Article
- DIDS inhibits Na-K-ATPase activity in porcine nonpigmented ciliary epithelial cells by a Src family kinase-dependent mechanism.American journal of physiology. Cell physiology · 2013Article
- Disruption of parathyroid hormone and parathyroid hormone-related peptide receptor phosphorylation prolongs ERK1/2 MAPK activation and enhances c-fos expression.American journal of physiology. Endocrinology and metabolism · 2012Article
- Sodium depletion enhances renal expression of (pro)renin receptor via cyclic GMP-protein kinase G signaling pathway.Hypertension (Dallas, Tex. : 1979) · 2012Article
- A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development.Molecular & cellular proteomics : MCP · 2011Article
- Ouabain stimulates Na-K-ATPase through a sodium/hydrogen exchanger-1 (NHE-1)-dependent mechanism in human kidney proximal tubule cells.American journal of physiology. Renal physiology · 2010Article
- Steroidogenic acute regulatory-related lipid transfer domain protein 5 localization and regulation in renal tubules.American journal of physiology. Renal physiology · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Parathyroid hormone (PTH) inhibits Na+-K+-ATPase activity by serine phosphorylation of the alpha1-subunit through ERK-dependent phosphorylation and translocation of protein kinase Calpha (PKCalpha). On the basis of previous studies, we postulated that PTH regulates sodium pump activity through Src kinase, PLC, and calcium-dependent ERK phosphorylation. In the present work utilizing opossum kidney cells, a model of renal proximal tubule, PTH-stimulated ERK phosphorylation and membrane translocation of PKCalpha were prevented by inhibition of Src kinase, PLC, and calcium entry. Pharmacological inhibition of PLA2 did not prevent PTH-stimulated ERK phosphorylation but completely prevented PKCalpha translocation. Silencing the expression of cytosolic or calcium-independent PLA2 also prevented PTH-mediated phosphorylation of Na+-K+-ATPase alpha1-subunit and PKCalpha without blocking ERK phosphorylation. Inhibition of Na+-K+-ATPase activity by the PLA2 metabolites arachidonic acid and 20-hydroxyeicosatetraenoic acid was prevented by specific inhibition of PKCalpha but not by U0126, a MEK-1 inhibitor. Transient transfection of constitutively active MEK-1 cDNA induced phosphorylation of Na+-K+-ATPase alpha1-subunit and PKCalpha, which was prevented by PLA2 inhibition. We conclude that PTH stimulates Na+-K+-ATPase phosphorylation and decreases the activity of Na+-K+-ATPase by a sequential activation of a signaling pathway involving Src kinase, PLC, ERK, PLA2, and PKCalpha.
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