RRC ID 38285
Author El-Beialy W, Galal N, Deyama Y, Yoshimura Y, Suzuki K, Tei K, Totsuka Y.
Title Regulation of human and pig renal Na(+),K (+)-ATPase activity by tyrosine phosphorylation of their alpha(1)-subunits.
Journal J. Membr. Biol.
Abstract Modulation of the physiologically influential Na(+),K(+)-ATPase is a complex process involving a wide variety of factors. To determine the possible effects of the protein tyrosine phosphatase (PTP) inhibitors dephostatin and Et-3,4-dephostatin on human and pig, renal cells and enzymatic extracts, we treated our samples (15 min-24 h) with those PTP inhibitors (0-100 microM). PTP inhibitors were found to possess a concentration-dependent inhibition of Na(+),K(+)-ATPase activity in both human and pig samples. The inhibition was similarly demonstrated on all cellular, microsomal fraction and purified Na(+),K(+)-ATPase levels. Despite rigorous activity recovery attempts, the PTP inhibitors' effects were sustained on Na(+),K(+)-ATPase activity. Western blotting experiments revealed the expression of both alpha(1)- and beta(1)-subunits in both human and pig tissues. alpha(1)-Subunits possessed higher tyrosine phosphorylation levels with higher concentrations of PTP inhibitors. Meanwhile, serine/threonine residues of both alpha(1)- and beta(1)-subunits demonstrated diminished phosphorylation levels upon dephostatin treatment. Accordingly, we provide evidence that Na(+),K(+)-ATPase can be regulated through tyrosine phosphorylation of primarily their alpha(1)-subunits, using PTP inhibitors.
Volume 233(1-3)
Pages 119-26
Published 2010-2
DOI 10.1007/s00232-010-9231-z
PMID 20130847
MeSH Animals Blotting, Western Catecholamines / pharmacology Cell Line, Tumor Flow Cytometry Humans Hydroquinones / pharmacology Kidney / enzymology* Nitroso Compounds / pharmacology Phosphorylation / drug effects Protein Subunits / metabolism* Protein Tyrosine Phosphatases / antagonists & inhibitors Sodium-Potassium-Exchanging ATPase / metabolism* Swine Tyrosine / metabolism*
IF 1.746
Times Cited 5
Human and Animal Cells