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2004 | 51 | 3 |

Tytuł artykułu

Bidirectional regulation of renal cortical Naplus, Kplus-ATPase by protein kinase C

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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 reagents were 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. Low dose of PDBu (10- mol/kg per min) increased cortical Na+ ,K+ -ATPase activity by 34.2%, whereas high doses (10-9 and 10-8 mol/kg per min) reduced this activity by 22.7% and 35.0%, respectively. PDBu administration caused changes in Na+ ,K+ -ATPase Vmax without af­fecting K0.5 for Na+ , K+ and ATP as well as K for ouabain. The effects of PDBu were abolished by PKC inhibitors, staurosporine, GF109203X, and Go 6976. The inhibi­tory effect of PDBu was reversed by pretreatment with inhibitors of cytochrome P450-dependent arachidonate metabolism, ethoxyresorufin and 17-octadecynoic acid, inhibitors of phosphatidylinositol 3-kinase (PI3K), wortmannin and LY294002, and by actin depolymerizing agents, cytochalasin D and latrunculin B. These results suggest that PKC may either stimulate or inhibit renal cortical Na+ ,K+ -ATPase. The inhibitory effect is mediated by cytochrome P450-dependent arachidonate metabo­lites and PI3K, and is caused by redistribution of the sodium pump from the plasma membrane to the inactive intracellular pool.

Wydawca

-

Rocznik

Tom

51

Numer

3

Opis fizyczny

p.757-772,fig.,ref.

Twórcy

autor
  • Medical University, Jaczewskiego 8, 20-090 Lublin, Poland
autor
autor
autor

Bibliografia

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Bibliografia

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