Binuclear terbium(III) complex as a probe for tyrosine phosphorylation

Chemistry - A European Journal

Volumn 16, Issue 17, 2010, Pages 5018-5025

  Akiba, Hiroki ^a   Sumaoka, Jun ^a   Komiyama, Makoto ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Kinases; Lanthanides; Luminescence; Phosphorylation; Tyrosine

Indexed keywords

BENZENE RING; BINDING ACTIVITIES; BINUCLEAR COMPLEXES; ENZYMATIC PHOSPHORYLATION; KINASES; LANTHANIDES; LIGHT ENERGY; LUMINESCENCE INTENSITY; MONONUCLEAR COMPLEXES; NEUTRAL AQUEOUS SOLUTION; ORDERS OF MAGNITUDE; REAL TIME MONITORING; TYROSINE KINASE; TYROSINE PHOSPHORYLATION;

AMINO ACIDS; BENZENE; BINDING ENERGY; LIGHT; LUMINESCENCE; METAL IONS; PEPTIDES; PHOSPHATASES; TERBIUM; TERBIUM ALLOYS;

PHOSPHORYLATION;

LANTHANIDE; ORGANOMETALLIC COMPOUND; PEPTIDE; PHOSPHOTRANSFERASE; TERBIUM; TYROSINE; WATER;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; LUMINESCENCE; METABOLISM; PHOSPHORYLATION; SYNTHESIS;

AMINO ACID SEQUENCE; HUMANS; LANTHANOID SERIES ELEMENTS; LUMINESCENCE; MOLECULAR STRUCTURE; ORGANOMETALLIC COMPOUNDS; PEPTIDES; PHOSPHORYLATION; PHOSPHOTRANSFERASES; TERBIUM; TYROSINE; WATER;

EID: 77951592420     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200903379     Document Type: Article

References (68)

1. a) T. Hunter, Cell 2000, 100, 113-127;
2. b) P. Cohen, Nat. Cell Biol. 2002, 4, E127-E130.
3. a) T. Hunter, Philos. Trans. R. Soc. London Ser. B 1998, 353, 583-605;
4. b) T. Hunter, Curr. Opin. Cell Biol. 2009, 21, 140-146.
5. a) S. Morandell, T. Stasyk, S. Skvortsov, S. Ascher, L. A. Huber, Proteomics 2008, 8, 4383-4401;
6. b) A. Guo, J. Villén, J. Kornhauser, K. L. Lee, M. P. Stokes, K. Rikova, A. Possemato, J. Nardone, G. Innocenti, R. Wetzel, Y. Wang, J. MacNeill, J. Mitchell, S. P. Gygi, J. Rush, R. D. Polakiewicz, M. J. Comb, Proc. Natl. Acad. Sci. USA 2008, 105, 692-697.
7. a) J. R. Engen, T. E. Wales, J. M. Hochrein, M. A. Meyn, S. B. Ozkan, I. Bahar, T. E. Smithgall, Cell. Mol. Life Sci. 2008, 65, 3058--3073;
8. b) S. J. Parsons, J. T. Parsons, Oncogene 2004, 23, 7906-7909;
9. c) W. Luo, R. J. Slebos, S. Hill, M. Li, J. Brábek, R. Amanchy, R. Chaerkady, A. Pandey, A.-J. L. Ham, S. K. Hanks, J. Proteome Res. 2008, 7, 3447-3460.
10. a) B. Schulenberg, R. Aggeler, J. M. Beechem, R. A. Capaldi, W. F. Patton, J. Biol. Chem. 2003, 278, 27251-27255;
11. b) B. Schulenberg, T. N. Goodman, R. Aggeler, R. A. Capaldi, W. F. Patton, Electrophoresis 2004, 25, 2526-2532.
12. a) T. Sakamoto, A. Ojida, I. Hamachi, Chem. Commun. 2009, 141-152;
13. b) A. Ojida, M. Inoue, Y. Mito-oka, I. Hamachi, J. Am. Chem. Soc. 2003, 125, 10184-10185;
14. c) A. Ojida, Y. Mito-oka, K. Sada, I. Hamachi, J. Am. Chem. Soc. 2004, 126, 2454-2463;
15. d) E. Kinoshita, M. Takahashi, H. Takeda, M. Shiro, T. Koike, Dalton Trans. 2004, 1189-1193;
16. e) E. Kinoshita, E. Kinoshita-Kikuta, K. Takiyama, T. Koike, Mol. Cell. Proteomics 2006, 5, 749-757;
17. f) T. Zhang, N. Y. Edwards, M. Bonizzoni, E. V. Anslyn, J. Am. Chem. Soc. 2009, 131, 11976-11984;
18. g) A. Riechers, F. Schmidt, S. Stadlbauar, B. König, Bioconjugate Chem. 2009, 20, 804-807.
19. a) F. S. Richardson, Chem. Rev. 1982, 82, 541-552;
20. b) I. Hemmilá, V.-M. Mukkala, Crit. Rev. Clin. Lab. Sci. 2001, 38, 441-519;
21. c) J.C. G. Bünzli, C. Piguet, Chem. Soc. Rev. 2005, 34, 1048-1077;
22. d) C. M. G. dos Santos, A. J. Harte, S. J. Quinn, T. Gunnlaugsson, Coord. Chem. Rev. 2008, 252, 2512-2527.
23. T. Gunnlaugsson, A. J. Harte, J. P. Leonard, M. Nieuwenhuyzen, Supramol. Chem. 2003, 15, 505-519.
24. a) S. J. A. Pope, B. P. Burton-Pye, R. Berridge, T. Khan, P. J. Skabara, S. Faulkner, Dalton Trans. 2006, 2907-2912;
25. b) M. L. Cable, J. P. Kirby, D. J. Levine, M. J. Manary, H. B. Gray, A. Ponce, J. Am. Chem. Soc. 2009, 131, 9562-9570;
26. c) R. S. Dickins, T. Gunnlaugsson, D. Parker, R. D. Peacock, Chem. Commun. 1998, 1643-1644.
27. a) M. D. Best, E. V. Anslyn, Chem. Eur. J. 2003, 9, 51-57;
28. b) M. Schäferling, O. S. Wolfbeis, Chem. Eur. J. 2007, 13, 4342-4349.
29. III complex responding to nucleoside triphosphates was used for kinetic analysis of enzymes: a) C. M. Spangler, C. Spangler, M. Göttle, Y. Shen, W.-J. Tang, R. Seifert, M. Schäferling, Anal. Biochem. 2008, 381, 86-93;
30. b) C. Spangler, C. M. Spangler, M. Spoerner, M. Schäferling, Anal. Bioanal. Chem. 2009, 394, 989-996.
31. a) P. Atkinson, Y. Bretonniere, D. Parker, Chem. Commun. 2004, 438-439;
32. b) P. Atkinson, Y. Bretonniere, D. Parker, G. Muller, Helv. Chim. Acta 2005, 88, 391-405.
33. Lanthanide complexes were directly conjugated to kinase substrate peptides and used to assess kinase activity : a) M. S. Tremblay, Q. Zhu, A. A. Marti, J. Dyer, M. Halim, S. Jockusch, N. J. Turro, D. Sames, Org. Lett. 2006, 8, 2723-2726;
34. b) M. S. Tremblay, M. Lee, D. Sames, Org. Lett. 2008, 10, 5-8.
35. D. P. Ringer, J. L. Etheredge, B. L. Dalrymple, J. S. Niedbalski, Biochem. Biophys. Res. Commun. 1990, 168, 267-273.
36. a) P. K.-L. Fu, C. Turro, J. Am. Chem. Soc. 1999, 121, 1-7;
37. b) D. P. Ringer, S. Burchett, D. E. Kizer, Biochemistry 1978, 17, 4818-4825;
38. c) M. D. Topal, J. R. Fresco, Biochemistry 1980, 19, 5531-5537.
39. H. Akiba, J. Sumaoka, M. Komiyama, ChemBioChem 2009, 10, 1773-1776.
40. Cationic binuclear lanthanide complexes were described for anion recognition: a) K. Nwe, C. M. Andolina, J. R. Morrow, J. Am. Chem. Soc. 2008, 130, 14861-14871;
41. b) A. J. Harte, P. Jensen, S. E. Plush, P. E. Kruger, T. Gunnlaugsson, Inorg. Chem. 2006, 45, 9465-9474.
42. CCDC 756622 contains the supplementary crystallographic data of Tb-DOTAM complex for this paper. These data can be obtained free of charge from The Cambridge Crystallographic Data Centre via www.ccdc.cam.ac.uk/data-request/cif.
43. III have similar structures: a) J. Vipond, M. Woods, P. Zhao, G. Tircsó, J. Ren, S. G. Bott, D. Ogrin, G. E. Kiefer, Z. Kovacs, A. D. Sherry, Inorg. Chem. 2007, 46, 2584-2595;
44. b) G. Bombieri, N. Marchini, S. Clattini, A. Mortillaro, S. Aime, Inorg. Chim. Acta 2006, 359, 3405-3411;
45. c) S. Amin, D. A. Voss, Jr., W. D. Horrocks, Jr., C. H. Lake, M. R. Churchill, J. R. Morrow, Inorg. Chem. 1995, 34, 3294-3300.
46. The notable background fluorescence of Trp was subtracted.
47. 1, as described in the text.
48. 2, probably owing to precipitation of the complex there.
49. A. Beeby, I. M. Clarkson, R. S. Dickins, S. Faulkner, D. Parker, L. Royle, A. S. de Sousa, J. A. G. Williams, M. Woods, J. Chem. Soc. Perkin Trans. 2 1999, 493-503.
50. As described in text, the solid Tb-DOTAM complex (without pTyr or PhOP) has one coordination water molecule, according to the Xray crystallography.
51. This result further confirms that the luminescence enhancement by PhOP is the result of energy transfer from the benzene ring of pTyr. The possibility that the removal of water molecules, which quench the luminescence, is responsible for the enhancement is unlikely.
52. III complex was reported: C.-H. Huang, J. R. Morrow, J. Am. Chem. Soc. 2009, 131, 4206-4207.
53. a) Z. Songyang, K. L. Carraway III, M. J. Eck, S. C. Harrison, R. A. Feldman, M. Mohammadi, J. Schlessinger, S. R. Hubbard, D. P. Smith, C. Eng, M. J. Lorenzo, B. A. J. Ponder, B. J. Mayer, L. C. Cantley, Nature 1995, 373, 536-539;
54. b) Z. Songyang, L. C. Cantley, Trends Biochem. Sci. 1995, 20, 470-475.
55. A. Kreegipuu, N. Blom, S. Brunak, J. Järv, FEBS Lett. 1998, 430, 45-50.
56. The phosphorylation of this Tyr is crucial for the activation of transcription, and also overactivated in cancer cells; see a) D. E. Levy, J. E. Darnell, Jr., Nat. Rev. Mol. Cell Biol. 2002, 3, 651-662;
57. b) H. Yu, R. Jove, Nat. Rev. Cancer 2004, 4, 97-105.
58. The phosphorylation of this Ser, combined with T308 phosphorylation, activates signalling pathways including MAPK pathway to induce many cellular actions, such as proliferation and cell growth: a) D. P. Brazil, B. A. Hemmings, Trends Biochem. Sci. 2001, 26, 657-664;
59. b) B. D. Manning, L. C. Cantley, Cell 2007, 129, 1261-1274.
60. a) J. Inglese, R. L. Johnson, A. Simeonov, M. Xia, W. Zheng, C. P. Austin, D. S. Auld, Nat. Chem. Biol. 2007, 3, 466-479;
61. b) R. M. Eglen, T. Reisine, Assay Drug Dev. Technol. 2009, 7, 22-43;
62. c) J. Comley, Drug Discovery World 2006, 7, 27-50.
63. a) D. S. Lawrence, Q. Wang, ChemBioChem 2007, 8, 373-378;
64. b) Y. Li, W. Xie, G. Fang, Anal. Bioanal. Chem. 2008, 390, 2049-2057;
65. c) M. D. Shults, B. Imperiali, J. Am. Chem. Soc. 2003, 125, 14248-14249;
66. d) Q. Wang, Z. Dai, S. M. Cahill, M. Blumenstein, D. S. Lawrence, J. Am. Chem. Soc. 2006, 128, 14016-14017;
67. e) T. Anai, E. Nakata, Y. Koshi, A. Ojida, I. Hamachi, J. Am. Chem. Soc. 2007, 129, 6232-6239;
68. f) H. Sahoo, A. Hennig, M. Florea, D. Roth, T. Enderle, W. M. Nau, J. Am. Chem. Soc. 2007, 129, 15927-15934.