Stimulation of protein kinase C rapidly reduces intracellular Na+ concentration via activation of the Na+ pump in ok cells

Molecular Pharmacology

Volumn 52, Issue 1, 1997, Pages 88-97

  Pedemonte, Carlos H ^a   Pressley, Thomas A ^b   Cinelli, Angel R ^c   Lokhandwala, Mustafa F ^a  

^a UNIVERSITY OF HOUSTON   (United States)

^b TEXAS TECH UNIVERSITY   (United States)

^c STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); PROTEIN KINASE C;

ANIMAL CELL; ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVITY; EPITHELIUM CELL; FLUORESCENCE MICROSCOPY; IMAGE ANALYSIS; MEMBRANE POTENTIAL; NONHUMAN; PRIORITY JOURNAL; SODIUM CELL LEVEL; STEADY STATE;

EID: 0030840887     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.52.1.88     Document Type: Article

References (49)

1. Beach, R. E., S. J. Schwab, P. C. Brazy, and V. W. Dennis. Norepinephrine increases Na,K-ATPase and solute transport in rabbit proximal tubules. Am. J. Physiol. 252:F215-F220 (1987).
2. Garvin, J., and K. Sanders. Endothelin inhibits fluid and bicarbonate transport in part by reducing Na,K-ATPase activity in rat proximal tubule. J. Am. Soc. Nephrol. 2:976-982 (1991).
3. Liu, F. Y., and M. G. Cogan. Role of protein kinase C in proximal bicarbonate absorption and angiotensin signaling. Am. J. Physiol. 258:F927-F933 (1990).
4. Schuster, V. L., J. P. Kokko, and H. R. Jacobson. Angiotensin II directly stimulates sodium transport in rabbit proximal convoluted tubules. J. Clin. Invest. 73:507-515 (1984).
5. Wang, T., and Y. L. Chan. Time- and dose-dependent effects of protein kinase C on proximal bicarbonate transport. J. Membr. Biol. 117:131-139 (1990).
6. Simons, K., and S. D. Fuller. Cell surface polarity in epithelia. Annu. Rev. Cell Biol. 1:243-288 (1985).
7. Soltoff, S. P., and L. J. Mandel. Active ion transport in the renal proximal tubule. I. Transport and metabolic studies. J. Gen. Physiol. 84:601-622 (1984).
8. Aperia, A., U. Holtbakc, M.-L. Syren, L.-B. Svensson, J. Fryckstedt, and P. Greengard. Activation/deactivation of renal Na,K-ATPase: a final common pathway for regulation of natriuresis. FASEB J. 8:436-439 (1994).
9. Bertorello, A. M., and A. I. Katz. Short-term regulation of renal Na,K-ATPase activity: physiological relevance and cellular mechanisms. Am. J. Physiol. 265:F743-F755 (1993).
10. Ewart, H. S., and A. Klip. Hormonal regulation of the Na,K-ATPase: mechanisms underlying rapid and sustained changes in pump activity. Am. J. Physiol. 269:C295-C311 (1995).
11. Jorgensen, P. L. Structure, function and regulation of Na,K-ATPase. Kidney Int. 29:10-20 (1986).
12. Aperia, A., F. Ibarra, L. B. Svensson, C. Klee, and P. Greengard. Calcineurin mediates α-adrenergic stimulation of Na,K-ATPase activity in renal tubule cells. Proc. Natl. Acad. Sci. USA 89:7394-7397 (1992).
13. Middleton, J. P., W. A. Khan, G. Collinsworth, Y. A. Hannun, and R. M. Medford. Heterogeneity of protein kinase C-mediated rapid regulation of Na/K-ATPase in kidney epithelial cells. J. Biol. Chem. 268:15958-15964 (1993).
14. Minta, A, and R. Y. Tsien. Fluorescent indicators for cytosolic sodium. J. Biol. Chem. 15:19449-19457 (1989).
15. Price, E. M., and J. B. Lingrel. Structure-function relationships in the Na,K-ATPase a-subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme. Biochemistry 27:8400-8408 (1988).
16. Price, E. M., D. A. Rice, and J. B. Lingrel. Site-directed mutagenesis of a conserved, extracellular aspartic acid residue affects the ouabain sensitivity of sheep Na,K-ATPase. J. Biol. Chem. 264:21902-21906 (1989).
17. Lane, L. K., J. M. Feldmann, C. E. Flarsheim, and C. L. Rybczynski. Expression of rat α1 Na,K-ATPase containing substitutions of 'essential' amino acids in the catalytic center. J. Biol. Chem. 268:17930-17934 (1993).
18. Shanbaky, N. M., and T. A. Pressley. Mammalian al-subunit of Na,K-ATPase does not need its amino terminus to maintain cell viability. Am. J. Physiol 267:C590-C597 (1994).
19. Rose, J. K., L. Buonocore, and M. A. Whitt. A new cationic liposome reagent mediating nearly quantitative transfection of animal cells. Biotechniques 10:520-525 (1991).
20. Pedemonte, C. H. Inhibition of Na-pump expression by impairment of protein glycosylation is independent of the reduced sodium entry into the cell. J. Membr. Biol. 147:223-233 (1995).
21. Pedemonte, C. H., and J. H. Kaplan. Carbodiimide inactivation of Na,K-ATPase: a consequence of internal cross-linking and not carboxyl group modification. J. Biol. Chem. 261:3632-3639 (1986).
22. Contreras, R. G., G. Avila, C. Gutierrez, J. J. Bolivar, L. Gonzalez-Mariscal, A. Darzon, G. Beaty, E. Rodriguez-Boulan, and M. Cereijido. Repolarization of Na-K pumps during establishment of epithelial monolayers. Am. J. Physiol. 257:C896-C905 (1989).
23. Gesek, F. A., and A. C. Schoolwerth. Hormone responses of proximal Na-H exchanger in spontaneously hypertensive rats. Am. J. Physiol. 261:F526-F536 (1991).
24. + in individual fibroblasts and lymphocytes. J. Biol. Chem. 264:19458-19467 (1989).
25. Cinelli, A. R., S. R. Neff, and J. S. Kauer. Salamander olfactory bulb neuronal activity observed by video rate, voltage-sensitive dye imaging. I. Characterization of the recording system. J. Neurophys. 73:2017-2032 (1995).
26. Salzberg, B. M., A. Grinvald, L. B. Cohen, H. V. Davila, and W. N. Ross. Optical recording of neuronal activity in an invertebrate central nervous system: simultaneous monitoring of several neurons. J. Neurophysiol. 40:1281-1291 (1977).
27. Grinvald, A., L. B. Cohen, S. Lesher, and M. B. Boyle. Simultaneous optical monitoring of activity of many neurons in invertebrate ganglia using a 124-element photodiode array. J. Neurophysiol. 45:829-839 (1981).
28. 2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260:3440-3450 (1985).
29. Moore, E. D. W., and F. S. Fay. Isoproterenol stimulates rapid extrusion of sodium from isolated smooth muscle cells. Proc. Natl. Acad. Sci. USA 90:8058-8062 (1993).
30. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227:680-685 (1970).
31. Pedemonte, C. H., T. A. Pressley, M. F. Lokhandwala, and A. R. Cinelli. Regulation of Na,K-ATPase transport activity by protein kinase C. J. Membr. Biol. 155:219-227 (1997).
32. Nishizuka, Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9:484-496 (1995).
33. Malstrom, K., G. Stange, and H. Murer. Identification of proximal tubular transport functions in the established kidney cell line OK. Biochim. Biophys. Acta 902:269-277 (1987).
34. Beguin, P., A. T. Beggah, A. V. Chibalin, P. B. Kairuz., F. Jaisser, P. M. Mathews, B. C. Rossier., S. Coteccia, and K. Geering. Phosphorylation of the Na,K-ATPase α-subunit by protein kinase A and C in vitro and in intact cells. J. Biol. Chem. 269:24437-24445 (1994).
35. Beguin, P., M. C. Peitsch, and K. Geering. Alpha 1 but not alpha 2 or alpha 3 isoforms of Na,K-ATPase are efficiently phosphorylated in novel protein kinase C motif. Biochemistry 35:14098-14108 (1996).
36. Feschenko, M. S., and K. J. Sweadner. Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C. J. Biol. Chem. 270:14072-14077 (1995).
37. Fisone, G., S. X.-H. Cheng, A. C. Nairn, A. H. Czernik, H. C. Hemmings, Jr., J.-O. Hoog, A. M. Bertorello, R. Kaiser, T. Bergman, H. Jornvall, A. Aperia, and P. Greengard. Identification of the phosphorylation site for cAMP-dependent protein kinase on Na,K-ATPase and effects of site-directed mutagenesis. J. Biol. Chem. 269:9368-9373 (1994).
38. Nash, S. R., N. Godinot, and M G. Caron. Clonning and characterization of the opossum kidney cell D1 dopamine receptor: expression of identical D1A and D1B dopamine receptor mRNAs in opossum kidney and brain. Mol. Pharmacol. 44:918-925 (1993).
39. +] in MDCK cells: evidence for amiloride-but not voltage-sensitive Na channels. J. Am. Soc. Nephr. 6:340 (1995).
40. +] and by cAMP-sensitive amilorde-inhibitable Na channels in MDCK cells. J. Am. Soc. Nephr. 6:343 (1995).
41. + conductance in rat CCD. J. Am. Soc. Nephr. 6:351 (1995).
42. Geering, K., and B. C. Rossier. Purification and characterization of (Na+K)-ATPase from toad kidney. Biochim. Biophys. Acta 566:157-170 (1979).
43. +K)-adenosine triphosphatase activity on thyroid status. J. Biol. Chem. 251:7826-7833 (1976).
44. +K)-adenosine triphosphatase from human renal tissue. Biochim. Biophys. Acta 481:313-327 (1977).
45. Kirk, K. L., and D. C. Dawson. Passive cation permeability of turtle colon: evidence for a negative interaction between intracellular sodium and apical sodium permeability. Pflueg. Arch. Eur. J. Physiol. 403:82-89 (1985).
46. Feraille, E., M.-L. Carranza, B. Buffin-Meyer, M. Rousselot, A. Doucet, and H. Favre. Protein kinase C-dependent stimulation of Na,K-ATPase in rat proximal convoluted tubules. Am. J. Physiol. 268:C1277-C1283 (1995).
47. Carranza, M. L., E. Feraille, and H. Favre. Protein kinase C-dependent phopshorylation of Na,K-ATPase α-subunit in rat kidney cortical tubules. Am. J. Physiol. 271:C136-C143 (1996).
48. Aperia, A. Regulation of Na,K-ATPase activity by phosphorylation/ dephosphorylation may influence intracellular Na concentration and cell adhesiveness. Ann. N. Y. Acad. Sci., in press.
49. Vasilets, L. A., H. Fotis, and E. M. Gartner. Regulatory phosphorylation of the Na,K-ATPase by protein kinases characterization of the phosphorylation site for PKC in mammalian kidney α-subunits. Ann. N. Y. Acad. Sci., in press.