Stabilization of Na,K-ATPase by ionic interactions

Biochimica et Biophysica Acta - Biomembranes

Volumn 1778, Issue 4, 2008, Pages 835-843

  Fodor, Elfrieda ^a   Fedosova, Natalya U ^b   Ferencz, Csilla ^a   Marsh, Derek ^c   Pali, Tibor ^a   Esmann, Mikael ^b  

^a INSTITUTE OF BIOCHEMISTRY   (Hungary)

^b AARHUS UNIVERSITY   (Denmark)

^c MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Denaturation; Differential scanning calorimetry; Electrostatic screening; Na,K ATPase; Pig kidney; Shark salt gland

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); HISTIDINE; LIPID;

ANIMAL TISSUE; ARTICLE; CENTRIFUGATION; CONTROLLED STUDY; CORRELATION ANALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME INACTIVATION; ENZYME STABILITY; HYDROSTATIC PRESSURE; IONIC STRENGTH; KIDNEY; LOW TEMPERATURE; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; SALT GLAND; SHARK; SWINE; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; ENZYME ACTIVATION; ENZYME STABILITY; HEAT; KIDNEY; MEMBRANES; MOLECULAR SEQUENCE DATA; OSMOLAR CONCENTRATION; SALTS; SHARKS; SODIUM-POTASSIUM-EXCHANGING ATPASE; SWINE;

CHONDRICHTHYES; SUIDAE;

EID: 41249091661     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.12.006     Document Type: Article

References (38)

1. Kaplan J.H. Biochemistry of Na,K-ATPase. Annu. Rev. Biochem. 71 (2002) 511-535
2. Therien A.G., Pu H.X., Karlish S.J.D., and Blostein R. Molecular and functional studies of the gamma subunit of the sodium pump. J. Bioenerg. Biomemb. 33 (2001) 407-414
3. 2+-ATPase of the sarcoplasmatic reticulum. Annu. Rev. Biophys. Chem. 73 (2004) 269-292
4. Hebert H., Purhonen P., Vorum H., Thomsen K., and Maunsbach A.B. Three-dimensional structure of renal Na,K-ATPase from cryo-electron microscopy of two-dimensional crystals. J. Mol. Biol. 314 (2001) 479-494
5. 2+-ATPase of sarcoplasmic reticulum reveals two thermodynamically independent domains. Biochemistry 29 (1990) 681-689
6. +-ATPase and its rearrangement during the catalytic cycle. J. Biol. Chem. 272 (1997) 1608-1614
7. +-exchanging ATPase. A scanning calorimetry study. Eur. J. Biochem. 268 (2001) 5027-5036
8. Møller J.V., Juul B., and LeMaire M. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286 (1996) 1-51
9. 2+-ATPase pump. Curr. Opin. Struct. Biol. 15 (2005) 387-393
10. +-dependent ATPase. Biochem. J. 211 (1983) 771-774
11. Jørgensen P.L., and Andersen J.P. Thermoinactivation and aggregation of αβ units in soluble and membrane-bound (Na,K)-ATPase. Biochemistry 25 (1986) 2889-2897
12. Arystarkhova E., Gibbons D.L., and Sweadner K.J. Topology of the Na,K-ATPase. Evidence for externalization of a labile transmembrane structure during heating. J. Biol. Chem. 270 (1995) 8785-8796
13. Goldshleger R., Tal D.M., and Karlish S.J.D. Topology of the α-subunit of Na,K-ATPase based on proteolysis. Lability of the topological organization. Biochemistry 34 (1995) 8668-8679
14. Stolz M., Lewitzki E., Schick E., Mutz M., and Grell E. Calorimetry of Na,K-ATPase. Ann. N.Y. Acad. Sci. 986 (2003) 245-246
15. Esmann M., Fedosova N.U., and Maunsbach A.B. Protonation-dependent inactivation of Na,K-ATPase by hydrostatic pressure developed at high-speed centrifugation. Biochim. Biophys. Acta 1468 (2000) 320-328
16. +)-ATPase from rectal glands of Squalus acanthias. The effect of preparative procedures on purity, specific and molar activity. Biochim. Biophys. Acta 567 (1979) 436-444
17. +)-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecyl sulphate. Biochim. Biophys. Acta 356 (1974) 36-52
18. Klodos I., Esmann M., and Post R.L. Large-scale preparation of sodium-potassium ATPase from kidney outer medulla. Kidney Int. 62 (2002) 2097-2100
19. +-ATPase: molar and specific activity, protein determination. Methods Enzymol. 156 (1988) 105-115
20. Fiske C.H., and Subbarow Y. The colorimetric determination of phosphorus. J. Biol. Chem. 66 (1925) 375-400
21. Cornelius F., Turner N., and Christensen H.R.Z. Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and presteady-state kinetics. Biochemistry 42 (2003) 8541-8549
22. +)-activated ATPase. XLIX. Content and role of cholesterol and other neutral lipids in highly purified rabbit kidney enzyme preparation. Biochim. Biophys. Acta 649 (1981) 541-549
23. Popot J.-L., and Engelman D.M. Membrane protein folding and oligomerization - the 2-stage model. Biochemistry 29 (1990) 4031-4037
24. Haltia T., and Freire E. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta 1228 (1995) 1-27
25. Haltia T., Semo N., Arrondo J.L.R., Goni F.M., and Freire E. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33 (1994) 9731-9740
26. Esmann M., Arora A., Maunsbach A.B., and Marsh D. Structural characterization of Na,K-ATPase from shark rectal glands by extensive trypsinization. Biochemistry 45 (2006) 954-963
27. Robinson R.A., and Stokes R.H. Electrolyte solutions. (second edition) (1986), Butterworth, London 571
28. Esmann M., and Marsh D. Spin label studies on the origin of the specificity of lipid-protein interactions in Na,K-ATPase membranes from Squalus acanthias. Biochemistry 24 (1985) 3572-3578
29. Esmann M., and Marsh D. Lipid-protein interactions with the Na,K-ATPase. Chem. Phys. Lipids 141 (2006) 94-104
30. Glynn I.M., and Karlish S.J.D. Occluded cations in active transport. Annu. Rev. Biochem. 59 (1990) 171-205
31. L.O. Jakobsen, Structural Studies of Cation and Nucleotide Binding Sites in Na,K-ATPase, PhD Dissertation, The Faculty of Health Sciences, University of Aarhus, Denmark (2004).
32. Donnet C., Arystarkhova E., and Sweadner K.J. Thermal denaturation of the Na,K-ATPase provides evidence for α-α oligomeric interaction and γ subunit association with the C-terminal domain. J. Biol. Chem. 276 (2001) 7357-7365
33. 2+-ATPase (SERCA1a) and prevents thermal inactivation. J. Biol. Chem. 279 (2004) 52382-52389
34. + affinity and decreased thermal stability. J. Biol. Chem. 280 (2005) 19003-19011
35. 254 in the A domain of the α-subunit revealed by intermolecular thiol cross-linking. J. Biol. Chem. 280 (2006) 27776-27782
36. Füzesi M., Gottschalk K.-E., Lindzen M., Shainskaya A., Küster B., Garty H., and Karlish S.J.D. Covalent cross-links between the γ-subunit (FXYD2) and α and β subunits of Na,K-ATPase - modelling the α-γ interaction. J. Biol. Chem. 280 (2005) 18291-18301
37. +-ATPase. Primary structure and spatial organization. FEBS Lett. 201 (1986) 237-245
38. Delano W.L. PyMOL molecular graphics system (2002). http://www.pymol.sourceforge.net (online)