320
Views
5
CrossRef citations to date
0
Altmetric
Laboratory Study

Mechanisms of PKC-Dependent Na+ K+ ATPase Phosphorylation in the Rat Kidney with Chronic Renal Failure

, , , , , , , & show all
Pages 13-22 | Published online: 07 Jul 2009

REFERENCES

  • Hayslett JP. Functional adaptation to reduction in renal mass. Physiol. Rev 1979; 59: 137–164
  • Hayslett JP, Kashgarian M, Epstein FH. Functional correlates of compensatory renal hypertrophy. J. Clin. Invest 1968; 47: 774–799
  • Schon DA, Silva P, Hayslett JP. Mechanism of potassium excretion in renal insufficiency. Am. J. Physiol 1974; 227: 1323–1330
  • Wen S-F, Wong NL, Evanson RL, Lockhart EA, Dirks JJ. Micropuncture studies of sodium transport in the remnant kidney of the dog. Clin. Invest 1973; 52: 386–397
  • Lubowitz H, Purkerson ML, Rolf DB, Weisser F, Bricker NS. Effect of nephron loss on proximal tubular bicarbonate reabsorption in the rat. Am. J. Physiol 1971; 220: 457–461
  • Schltze RG, Weisser F, Bricker NS. The influence of uremia on fractional sodium reabsorption by the proximal tubule of rats. Kidney Int 1972; 2: 59–65
  • Wong NL, Quamme GA, Dirks JH. Tubular handling of bicarbonate in dogs with experimental renal failure. Kidney Int 1984; 25: 912–918
  • Buerkert J, Martin D, Prasad J, Chambless S, Klahr S. Response of deep nephrons and the terminal collecting duct to a reduction in renal mass. Am. J. Physiol 1979; 236: F454–F464
  • Finkelstein FO, Hayslett JP. Role of medullary structures in the functional adaptation of renal insufficiency. Kidney Int 1974; 6: 419–425
  • Jacobson M, Rodriguez H, Hogan W, Klahr S. Mechanism of activation of renal Na+-K+-ATPase in the rat: effects of reduction of renal mass. Am. J. Physiol 1980; 239: F281–F288
  • Bertuccio CA, Ibarra FR, Toledo JE, Arrizurieta EE, Martin RS. Endogenous vasopressin regulates Na+-K+-ATPase and Na+-K+-Cl−-cotransporter rbsc-1 in rat outer medulla. Am. J. Physiol 2002; 282: F256–F270
  • Tumlin JA, Hoban CA, Medford RM, Sands JM. Expression of Na-K-ATPase alpha- and beta-subunit mRNA and protein isoforms in the rat nephron. Am J Physiol 1994; 266: F240–F245
  • Bofill P, Goecke IA, Bonilla S, Alvo M, Marusic ET. Tissue-specific modulation of Na, K-ATPase alpha-subunit gene expression in uremic rats. Kidney Int 1994; 45(3)672–678
  • Therien AG, Nestor NB, Ball WJ, Blostein R. Tissue-specific versus isoform-specific differences in cation activation kinetics of the Na, K-ATPase. J. Biol. Chem 1996; 271(22)7104–7112
  • Cheng X, Fisone G, Aizman O, Aizman R, Levenson R, Greengard P, Aperia A. PKA-mediated phosphorylation and inhibition of Na+, K+-ATPase in response to β-adrenergic hormone. Am. J. Physiol 1997; 273: C893–C901
  • Chibalin AV, Ogimoto G, Pedemonte CH, Pressley TA, Katz AI, Feraille E, Berggren PO, Bertorello AM. Dopamine-induced endocytosis of Na+, K+-ATPase is initiated by phosphorylation of Ser-18 in the rat alpha subunit and is responsible for the decreased activity in epithelial cells. J. Biol. Chem 1999; 274: 1920–1927
  • Feschenko MS, Sweadner KJ. Phosphorylation of Na+ K+ ATPase by protein kinase C at Ser-18 occurs in intact cells but does not result in direct inhibition of ATP hydrolysis. J. Biol. Chem 1997; 272: 17726–17733
  • Vasilets LA. Regulatory phosphorylation of the Na+ K+ ATPase from mammalian kidneys and Xenopus oocytes by protein kinases. Characterization of the phosphorylation site for PKC. Ann. N. Y. Acad. Sci 1997; 834: 585–587
  • Asghar M, Kansra V, Hussain T, Lokhandwala MF. Hyperphosphorylation of Na-pump contributes to defective renal dopamine response in old rats. J. Am. Soc. Nephrol 2001; 12: 226–232
  • Bertuccio CA, Cheng SX, Arrizurieta EE, Martín RS, Ibarra FR. Mechanisms of Na+, K+-ATPase phosphorylation by PKC in the medullary thick ascending limb of Henle in the rat. Pflügers Arch 2003; 447: 87–96
  • Arrizurieta de Muchnick EE, Wiersba CR, Paz RA. Contribución de los nefrones yuxtamedulares al balance de agua y sodio en la rata. Medicina (Bs As) 1977; 37(Suppl. 2)145–153
  • Hilger HH, Klumper JD, Ullrich KJ. Water resorption and ion transport through collecting tubule cells of mammalian kidney: microanalytic studies. Pflugers Arch 1958; 267(3)218–237
  • Morel F, Chabardes D, Imbert-Teboul M. Vasopressin action sites along the nephron. J Physiol (Paris) 1981; 77(4–5)615–620
  • Bertuccio C, Ibarra FR, Toledo J, Paz L, Arrizurieta EE, Martin RS. cAMP regulation in thick ascending limb of Henle in rats with chronic renal failure. A microdissection study. Acta Phys. Scand 1998; 64: 107–114
  • Kim GH, Ecelbarger C, Knepper MA, Packer RK. Regulation of thick ascending limb ion transporter abundance in response to altered acid/base intake. J Am Soc Nephrol 1999; 10(5)935–942
  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J. Biol. Chem 1951; 193: 265–267
  • Ibarra FR, Cheng SX, Agren M, Svensson LB, Aizman O, Aperia A. Intracellular sodium modulates the state of protein kinase C phosphorylation of rat proximal tubule Na+, K+-ATPase. Acta Physiol Scand 2002; 175(2)165–171
  • Feschenko MS, Sweadner KJ. Structural basis for species-specific differences in the phosphorylation of Na-K-ATPase by protein kinase C. J. Biol. Chem 1995; 270: 14072–14077
  • Cheng X, Aizman O, Nairn AC, Greengard AC, Aperia A. Ca2+ determines the effects of protein kinase A and C on activity of rat renal Na+, K+-ATPase. J. Physiol 1999; 518: 37–46
  • Li D, Cheng SX, Fisone G, Caplan M, Ohtomo Y, Aperia A. Effects of okadaic acid, calyculin A and PDBu on state of phosphorylation of rat renal Na+, K+-ATPase. Am. J. Physiol 1998; 275: F863–869
  • Lucking K, Nielsen JM, Pedersen PA, Jorgensen PL. Na-K-ATPase isoform (alpha 3, alpha 2, alpha 1) abundance in kidney estimated by competitive RT-PCR and ouabain binding. Am. J. Physiol 1996; 271: F253–F260
  • Knepper MA, Rector FC, Jr. Urinary concentration and dilution. The Kidney, BM Brenner, FC Rector, Jr. Saunders, Philadelphia, PA 1995; 532–570
  • Fernández-Llama P, Andrews P, Ecelbarger CA, Nielsen S, Knepper MA. Concentrating defect in experimental nephrotic syndrome: Altered expression of aquaporins and thick ascending limb Na+ transporters. Kidney Int 1998; 54(1)170
  • Ibarra F, Aperia A, Svensson L-B, Eklöf A-C, Greengard P. Bidirectional regulation of Na+, K+-ATPase activity by dopamine and an α-adrenergic agonist. Proc. Natl. Acad. Sci 1993; 90: 21–24
  • Belusa R, Wag ZM, Matsubara T, Sahlgren B, Dulubova I, Nairn AC, Ruoslahti E, Greengard P, Aperia A. Mutation of the protein kinase C phosphorylation site on rat alpha1 Na+-K+-ATPase alters regulation of intracellular Na+ and PH and influences cell shape and adhesiveness. J. Biol. Chem 1997; 272: 20179–20184
  • Vasilets LA, Postina R, Kirichenko SN. Mutations of the alpha-1 subunit of the rat Na-K-ATPase to negatively charged amino acid residues mimic the functional effect of PKC-mediated phosphorylation. FEBS Letters 1999; 455: 8–12
  • Asghar M, Hussain T, Lokhandwala MF. Higher basal serine phosphorylation of D1A receptors in proximal tubules of old Fischer 344 rats. Am J Physiol 2002; 283: F350–F355
  • Horiuchi A, Albrecht FE, Eisner GM, Jose PA, Felder RA. Renal dopamine receptors and pre- and post-cAMP-mediated Na+ transport defect in spontaneously hypertensive rats. Am. J. Physiol 1992; 263: F1105–F1111
  • Bertuccio CA, Ibarra FR, Pignataro O, Toledo J, Arrizurieta EE, Martin RS. Cellular adaptation of the rat medullary thick ascending limb to chronic renal failure. Medicina (Buenos Aires) 1995; 55: 329–333
  • Cheng X-J, Höög J-O, Nairn AC, Greengard P, Aperia A. Regulation of rat Na+- K+- ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. Am J Physiol Cell Physiol 1997; 273: 1981–1986
  • Silva IV, Caruso-Neves C, Azeredo IM, Carvalho TL, Lara LS, de Mello MC, Lopes AG. Urea inhibition of renal Na+ K+ ATPase activity is reversed by cAMP. Arch. Biochem. Biophys 2002; 406: 183–189

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.