Response of recombinant calcineurin to metal ions, reduction-oxidation agents, and enzymatic modification

Protein Expression and Purification

Volumn 26, Issue 2, 2002, Pages 194-201

  Rhode, David J ^a   Imparl Radosevich, Jennifer ^b   Bartleson, Cheryl ^b   Spannaus Martin, Donna J ^a   Martin, Bruce L ^a,c  

^a UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

^b IOWA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; INSECTA; UNIDENTIFIED BACULOVIRUS;

ASCORBIC ACID; CALCINEURIN; DITHIOTHREITOL; METAL; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; BRAIN; CATTLE; CHEMISTRY; ENZYMOLOGY; METABOLISM; OXIDATION REDUCTION REACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ANIMALS; ASCORBIC ACID; BRAIN; CALCINEURIN; CATTLE; DITHIOTHREITOL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; METALS; OXIDATION-REDUCTION; RECOMBINANT PROTEINS;

EID: 0036421217     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00520-X     Document Type: Article

References (49)

1. F. Rusnak, P. Mertz, Calcineurin: Form and function, Physiol. Rev. 80 (2000) 1483-1521.
2. M.M. King, C.Y. Huang, The calmodulin-dependent activation and deactivation of the phosphoprotein phosphatase, calcineurin, and the effect of nucleotides, pyrophosphate, and divalent metal ions. Identification of calcineurin as a Zn and Fe metalloenzyme, J. Biol. Chem. 259 (1984) 8847-8856.
3. M.M. King, C.Y. Huang, Activation of calcineurin by nickel ions, Biochem. Biophys. Res. Commun. 114 (1983) 955-961.
4. 2+, J. Biol. Chem. 259 (1984) 8801-8807.
5. 2+ and transition metal ions, Eur. J. Biochem. 144 (1984) 447-452.
6. C.J. Pallen, J.H. Wang, Regulation of calcineurin by metal ions, J. Biol. Chem. 259 (1984) 6134-6141.
7. R.C. Gupta, R.L. Khandelwal, P.V. Sulakhe, Intrinsic phosphatase activity of bovine brain calcineurin requires a tightly bound trace metal, FEBS Lett. 169 (1984) 251-255.
8. D.J. Wolff, D.W. Sved, The divalent cation dependence of bovine brain calmodulin-dependent phosphatase, J. Biol. Chem. 260 (1985) 4195-4202.
9. J.P. GriNth, J.L. Kim, E.E. Kim, M.D. Sintchak, J.A. Thomson, M.J. Fitzgibbon, M.A. Fleming, P.R. Caron, K. Hsiao, M.A. Navia, X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex, Cell 82 (1995) 507-522.
10. C.R. Kissinger, H.E. Perge, D.R. Knighton, C.T. Lewis, L.A. Pelletier, A. Tempczyk, V.J. Kalish, K.D. Tucker, R.E. Showalter, E.W. Moomaw, L.N. Gastinel, N. Habuka, X. Chen, F. Maldonado, J.E. Barker, R. Bacquet, J.E. Villafranca, Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex, Nature 378 (1995) 641-644.
11. N. Sträter, 3 T. Kablunde, P. Tucker, H. Witzel, B. Krebs, Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site, Science 268 (1995) 1489-1492.
12. T. Klabunde, N. Strater, R. Frohlich, H. Witzel, B. Krebs, Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures, J. Mol. Biol. 259 (1996) 737-748.
13. Y. Hashimoto, B.A. Perrino, T.R. Soderling, Identification of an autoinhibitory domain in calcineurin, J. Biol. Chem. 265 (1990) 1924-1927.
14. B.A. Perrino, L.Y. Ng, T.R. Soderling, Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain, J. Biol. Chem. 270 (1995) 340-346.
15. B.A. Perrino, Y.-L. Fong, D.A. Brickey, Y. Saitoh, Y. Ushio, K. Fukanaga, E. Miyamoto, T.R. Soderling, Characterization of the phosphatase activity of a baculovirus-expressed calcineurin A isoform, J. Biol. Chem. 267 (1992) 15965-15969.
16. R.K. Sharma, W.A. Taylor, J.H. Wang, Use of calmodulin affinity chromatography for purification of specific calmodulin-dependent enzymes, Methods Enzymol. 102 (1983) 210-219.
17. 2+-dependent modulator protein, Adv. Cyclic Nucleotide Res. 10 (1979) 187-198.
18. 2+-induced hydrophobic site chromatography on calmodulin, application to purification of calmodulin by phenyl Sepharose affinity chromatography, Biochem. Biophys. Res. Commun. 104 (1982) 830-836.
19. R.K. Sharma, T.H. Wang, E. Wirch, J.H. Wang, Purification and properties of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase, J. Biol. Chem. 255 (1980) 5916-6923.
20. H. Takahara, H. Okamoto, K. Sugawara, Affinity chromatography of peptidylarginine deiminase from rabbit skeletal muscle on a column of soybean trypsin inhibitor (Kunitz)-Sepharose, J. Biochem. 99 (1986) 1417-1424.
21. M.M. Bradford, A rapid and sensitive method for the quantitation for microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
22. D.B. Bylund, E.G. Krebs, Effect of denaturation on the susceptibility of proteins to enzymic phosphorylation, J. Biol. Chem. 250 (1975) 6355-6361.
23. K.L. Hippen, S. Jakes, J. Richards, B.P. Jena, B.L. Beck, L.B. Tabatabai, T.S. Ingebritsen, Acidic residues are involved in substrate recognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1, Biochemistry 32 (1993) 12405-12412.
24. J.M. Imparl, T. Senshu, D.J. Graves, Studies of calcineurin-calmodulin interaction: Probing the role of arginine residues using peptidylarginine deiminase, Arch. Biochem. Biophys. 318 (1995) 370-377.
25. K. Nomura, Specificity and mode of action of the muscle-type protein-arginine deiminase, Arch. Biochem. Biophys. 293 (1992) 362-369.
26. 2+- and calmodulin-dependent protein phosphatase: Probable identity with calcineurin (CaM-BP80), FEBS Lett. 137 (1982) 80-84.
27. 2+/calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle, Eur. J. Biochem. 132 (1982) 289-295.
28. C.B. Klee, M.H. Krinks, A.S. Manalan, G.F. Draetta, D.L. Newton, Control of calcineurin protein phosphatase activity, Adv. Protein Phosphatases 1 (1985) 135-146.
29. P.F. Simonelli, H.-C. Li, Regulation of calmodulin-dependent phosphoprotein phosphatase (calcineurin) by the synergistic action of Ca(II), calmodulin, and Mg(II) or transition metal ions, Adv. Protein Phosphatases 1 (1985) 175-190.
30. K. Seki, H.-C. Chen, K.P. Huang, Dephosphorylation of protein kinase C substrates, neurogranin, neuromodulin, and MARCKS, by calcineurin and protein phosphatases 1 and 2A, Arch. Biochem. Biophys. 316 (1995) 673-679.
31. C.J. Ladner, J. Czech, J. Maurice, S.A. Lorens, J.M. Lee, Reduction of calcineurin enzymatic activity in Alzheimer's disease: Correlation with neuropathologic changes, J. Neuropathol. Exp. Neurol. 55 (1996) 924-931.
32. B.L. Martin, L.A. Jurado, Activation of calcineurin by the trivalent metal terbium, J. Protein Chem. 17 (1998) 473-478.
33. 2+, Biochemistry 36 (1997) 10185-10191.
34. 2+, Biochemistry 38 (1999) 3386-3392.
35. B.L. Martin, D.J. Rhode, Effect of substitution inert metal complexes on calcineurin. Arch, Biochem. Biophys. 366 (1999) 168-176.
36. 2+ and transition metal ions in the activation of calcineurin, Arch. Biochem. Biophys. 380 (2000) 71-76.
37. L. Yu, J. Golbeck, J. Yao, F. Rusnak, Spectroscopic and enzymatic characterization of the active site dinuclear metal center of calcineurin: Implications for a mechanistic role, Biochemistry 36 (1997) 10727-10734.
38. X. Wang, V.C. Culotta, C.B. Klee, Superoxide dismutase protects calcineurin from inactivation, Nature 383 (1996) 434-437.
39. L. Yu, J. Golbeck, J. Yao, F. Rusnak, Spectroscopic and enzymatic characterization of the active site dinuclear metal center of calcineurin: Implications for a mechanistic role, Biochemistry 36 (1997) 10727-10734.
40. M. Carballo, G. Marquez, M. Conde, J. Martin-Nieto, J. Monte-seirin, J. Conde, E. Pintado, F. Sobrino, Characterization of calcineurin in human neutrophils, J. Biol. Chem. 274 (1999) 93-100.
41. T.A. Reiter, R.T. Abraham, M. Choi, F. Rusnak, Redox regulation of calcineurin in T-lymphocytes, J. Biol. Inorg. Chem. 4 (1999) 632-644.
42. K. Furuke, M. Shiraishi, H.S. Mostowski, E.T. Bloom, Fas ligand induction in human NK cells is regulated by redox through a calcineurin-nuclear factors of activated T cell-dependent pathway, J. Immunol. 162 (1999) 1988-1993.
43. A. Ferri, R. Gabbianelli, A. Casciati, E. Paolucci, G. Rotilio, M.T. Carri, Calcineurin activity is regulated both by redox compounds and by mutant familial amytrophic lateral sclerosis-superoxide dismutase, J. Neurochem. 75 (2000) 606-613.
44. D. Sommer, K.L. Fakata, S.A. Swanson, P.M. Stemmer, Modulation of the phosphatase activity of calcineurin by oxidants and antioxidants in vitro, Eur. J. Biochem. 267 (2000) 2312-2322.
45. R. Bogumil, D. Namagaladze, D. Schaarschmidt, T. Schmachtel, S. Hellstern, R. Mutzel, V. Ullrich, Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide, Eur. J. Biochem. 267 (2000) 1407-1415.
46. B.L. Martin, Selective activation of the calmodulin activated phosphatase, calcineurin, by dipicolinic acid, Arch. Biochem. Biophys. 345 (1997) 332-338.
47. M.M. King, Modification of the calmodulin-stimulated phosphatase, calcineurin, by sulfhydryl reagents, J. Biol. Chem. 261 (1986) 4081-4084.
48. 2+ center at the enzyme active site, J. Biol. Chem. 277 (2002) 5962-5969.
49. M.M. King, L.P. Heiny, Chemical modification of the calmodulin-stimulated phosphatase, calcineurin, by phenylglyoxal, J. Biol. Chem. 262 (1987) 10658-10662.