Bidirectional regulation of renal cortical Na+,K+-ATPase by protein kinaseC.
Journal Title: Acta Biochimica Polonica - Year 2004, Vol 51, Issue 3
Abstract
We examined the role of protein kinase C (PKC) in the regulation of Na+,K+-ATPase activity in the renal cortex. Male Wistar rats were anaesthetized and the investigated reagentswere infused into the abdominal aorta proximally to the renal arteries. A PKC-activating phorbol ester,phorbol 12,13-dibutyrate (PDBu), had a dose-dependent effect on cortical Na+,K+-ATPase activity. Lowdose of PDBu (10(-11) mol/kg per min) increased cortical Na+,K+-ATPase activity by 34.2%, whereas highdoses (10(-9) and 10(-8) mol/kg per min) reduced this activity by 22.7% and 35.0%, respectively. PDBuadministration caused changes in Na+,K+-ATPase Vmax without affecting K(0.5) for Na+, K+ and ATP as wellas Ki for ouabain. The effects of PDBu were abolished by PKC inhibitors, staurosporine, GF109203X, andGö 6976. The inhibitory effect of PDBu was reversed by pretreatment with inhibitors of cytochrome P450-dependentarachidonate metabolism, ethoxyresorufin and 17-octadecynoic acid, inhibitors of phosphatidylinositol3-kinase (PI3K), wortmannin and LY294002, and by actin depolymerizing agents, cytochalasin D and latrunculinB. These results suggest that PKC may either stimulate or inhibit renal cortical Na+,K+-ATPase. The inhibitoryeffect is mediated by cytochrome P450-dependent arachidonate metabolites and PI3K, and is caused by redistributionof the sodium pump from the plasma membrane to the inactive intracellular pool.
Authors and Affiliations
Grazyna Wójcicka, Ewelina Borkowska, Anna Jamroz-Wiśniewska, Andrzej Marciniak, Jerzy Bełtowski
Keywords
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