Kinetics of phosphorylation of Na+K+-ATPase by protein kinase C

Lowndes, Joseph M.; Hokin-Neaverson, Mabel; Bertics, Paul J.

doi:10.1016/0167-4889(90)90069-p

Cited by 92 publications

(34 citation statements)

References 55 publications

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“…1 illustrates phosphorylation of reconstituted shark and pig kidney Na+,K+-ATPase tx-subunit by PKA in the absence of detergents. This is in contrast to results using purified membrane preparations of the enzymes where Triton X-100 is necessary in order to obtain phosphorylation by PKA [1][2][3]6]. Probably, the dissociation from the native membranous constraints and the subsequent dilution into the liposomes makes the PKA target site accessible.…”

Section: Methodsmentioning

confidence: 40%

“…There is a consensus in the literature that the Na+,K +-ATPase under certain conditions can be phosphorylated in vitro both by the cAMP dependent protein kinase, PKA, and by protein kinase C, PKC [1][2][3][4][5][6][7] and it has been hyphotesized that this forms the molecular basis for its regulation, however, a direct link to the physiological regulation of Na+,K+-ATPase in vivo is still missing. Conflicting results of the effects of protein kinase phosphorylation on enzyme function have been reported (cf.…”

Section: Introductionmentioning

confidence: 99%

“…[2,6]). For PKA phosphorylation this is especially true due to the requirement for detergents [1][2][3] which probably exposes the target site for PKA, but makes it inaccessible to functional studies due to inhibition of the Na+,K+-ATPase activity. This necessity for detergents also makes it difficult to assess the sidedness of PKA action.…”

Section: Introductionmentioning

confidence: 99%

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Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation

Cornelius

Logvinenko

1996

FEBS Letters

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Reconstituted Na+,K+-ATPase from either pig kidney or shark rectal glands was phosphorylated by cAMP dependent protein kinase, PKA. The stoichiometry was ~0.9 mole Pilmole tx-subunit in the pig kidney enzyme and ,-~ 0.2 tool Pilmol a-subunit in the shark enzyme. In shark Na+,K+-ATPase PKA phosphorylation increased the maximum hydro!~tic activity for cytoplasmic Na ÷ activation and extracellular K activation without affecting the apparent Km values. In contrast, no significant functional effect after PKA phosphorylation was observed in pig kidney Na+,K+-ATPase.

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Section: Methodsmentioning

confidence: 40%

Section: Introductionmentioning

confidence: 99%

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Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation

Cornelius

Logvinenko

1996

FEBS Letters

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“…Over the past years, it has been demonstrated that the a subunit can be phosphorylated by PKC in vitro and in intact cells (Lowndes et al, 1990;Bertorello et al, 1991;Chibalin et al, 1992;Beguin et al, 1994;Feschenko and Sweadner, 1995). In the case of the Bufo marinus al subunit (alTBM), the PKC phosphorylation site has been mapped to the Thr-15 and Ser-16, close to the NH2 terminus of the molecule (Beguin et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Phorbol 12-myristate 13-acetate down-regulates Na,K-ATPase independent of its protein kinase C site: decrease in basolateral cell surface area.

Beron

Forster

Béguin

et al. 1997

MBoC

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The effect of protein kinase C (PKC) stimulation on the pump current (Up) generated by the Na,K-ATPase was measured in A6 epithelia apically permeabilized with amphotericin B. Phorbol 12-myristate 13-acetate (PMA) produced a decrease in I carried by sodium pumps containing the endogenous Xenopus laevis or transfected BuJ'o marinus al subunits (-30% reduction within 25 min, maximum after 40 min) independent of the PKC phosphorylation site (T15A/S16A). In addition to this major effect of PMA, which was independent of the intracellular sodium concentration and was prevented by the PKC inhibitor bisindolylmaleimide GF 109203X (BIM), another BIM-resistant, PKC siteindependent decrease was observed when the Ip was measured at low sodium concentrations (total reduction -50% at 5 mM sodium). Using ouabain binding and cell surface biotinylation, stimulation of PKC was shown to reduce surface Na,K-ATPase by 14 to 20% within 25 min. The same treatment stimulated fluid phase endocytosis sevenfold and decreased by 16.5% the basolateral cell surface area measured by transepithelial capacitance measurements. In conclusion, PKC stimulation produces a decrease in sodium pump function which can be attributed, to a large extent, to a withdrawal of sodium pumps from the basolateral cell surface independent of their PKC site. This

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“…In recent years, an increasing number of publications (1)(2)(3)(4) have reported the short term regulation of kidney Na ϩ ,K ϩ -ATPase by hormones and intracellular second messengers that modulate proximal tubule sodium reabsorption. Renal Na ϩ ,K ϩ -ATPase activity is regulated by phosphorylation/dephosphorylation processes, and both cAMP-dependent protein kinase and protein kinase C (PKC) phosphorylate the Na ϩ ,K ϩ -ATPase (1)(2)(3)(4)(5)(6)(7)(8)(9)(10). We have demonstrated that Ser-18 of the ␣-subunit is essential for the inhibition of the Na ϩ -pump activity by dopamine and that both Ser-18 and Ser-11 are essential for the stimulation of this activity by PMA (10 -15).…”

mentioning

confidence: 99%

Agonist-dependent Regulation of Renal Na+, K+-ATPase Activity Is Modulated by Intracellular Sodium Concentration

Efendiev

Bertorello

Zandomeni

et al. 2002

Journal of Biological Chemistry

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We tested the hypothesis that the level of intracellular sodium modulates the hormonal regulation of the Na ؉ ,K ؉ -ATPase activity in proximal tubule cells. By using digital imaging fluorescence microscopy of a sodium-sensitive dye, we determined that the sodium ionophore monensin induced a dose-specific increase of intracellular sodium. A correspondence between the elevation of intracellular sodium and the level of dopamine-induced inhibition of Na ؉ ,K ؉ -ATPase activity was determined. At basal intracellular sodium concentration, stimulation of cellular protein kinase C by phorbol 12-myristate 13-acetate (PMA) promoted a significant increase in Na ؉ ,K ؉ -ATPase activity; however, this activation was gradually reduced as the concentration of intracellular sodium was increased to become a significant inhibition at concentrations of intracellular sodium higher than 16 mM. Under these conditions, PMA and dopamine share the same signaling pathway to inhibit the Na ؉ ,K ؉ -ATPase. The effects of PMA and dopamine on the Na ؉ ,K ؉ -ATPase activity and the modulation of these effects by different intracellular sodium concentrations were not modified when extracellular and intracellular calcium were almost eliminated. These results suggest that the level of intracellular sodium modulates whether hormones stimulate, inhibit, or have no effect on the Na ؉ ,K ؉ -ATPase activity leading to a tight control of sodium reabsorption.

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Kinetics of phosphorylation of Na+K+-ATPase by protein kinase C

Cited by 92 publications

References 55 publications

Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation

Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation

Phorbol 12-myristate 13-acetate down-regulates Na,K-ATPase independent of its protein kinase C site: decrease in basolateral cell surface area.

Agonist-dependent Regulation of Renal Na+, K+-ATPase Activity Is Modulated by Intracellular Sodium Concentration

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