Redox-based probes as tools to monitor oxidized protein tyrosine phosphatases in living cells

European Journal of Medicinal Chemistry

Volumn 88, Issue , 2014, Pages 28-33

  Garcia, Francisco J ^a   Carroll, Kate S ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Bioconjugation; Nucleophile based therapeutics; Phosphatases; Reactive oxygen species; Redox biology; Redox based probes

Indexed keywords

5,5 DIMETHYL 1,3 CYCLOHEXANEDIONE; ELECTROPHILE; GLUTATHIONE PEROXIDASE 3; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NUCLEOPHILE; PROTEIN TYROSINE PHOSPHATASE; SULFIDE; ALKYNE; INSULIN RECEPTOR; MOLECULAR LIBRARY; REACTIVE OXYGEN METABOLITE;

ANIMAL CELL; ARTICLE; BLOTTING; CHO CELL LINE; CONJUGATION; COS 1 CELL LINE; ENZYME ACTIVITY; FEMALE; GLUCOSE TRANSPORT; IMMUNOPRECIPITATION; IN VITRO STUDY; MOLECULAR PROBE; NONHUMAN; NUCLEOPHILICITY; OXIDATION; OXIDATION REDUCTION STATE; PATHOPHYSIOLOGY; PHYSIOLOGICAL PROCESS; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; ANIMAL; ANTAGONISTS AND INHIBITORS; BIOCATALYSIS; BIOSYNTHESIS; CELL CULTURE; CHEMICAL STRUCTURE; CHEMISTRY; CHLOROCEBUS AETHIOPS; CRICETULUS; HUMAN; METABOLISM; MOLECULAR LIBRARY; OXIDATION REDUCTION REACTION; PHARMACOLOGY; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

ALKYNES; ANIMALS; BIOCATALYSIS; CELLS, CULTURED; CERCOPITHECUS AETHIOPS; CHO CELLS; COS CELLS; CRICETULUS; HUMANS; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PROTEIN TYROSINE PHOSPHATASES; REACTIVE OXYGEN SPECIES; RECEPTOR, INSULIN; SMALL MOLECULE LIBRARIES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84911471670     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.06.040     Document Type: Article

References (38)

1. M. Giorgio, M. Trinei, E. Migliaccio, P.G. Pelicci, Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat. Rev. Mol. Cell. Biol. 8 (2007) 722-728.
2. H. de Groot, A. Littauer, Hypoxia, reactive oxygen, and cell injury, Free Radic. Biol. Med. 6 (1989) 541-551.
3. M. Sundaresan, Z.X. Yu, V.J. Ferrans, K. Irani, T. Finkel, Requirement for generation of H2O2 for platelet-derived growth factor signal transduction, Science 270 (1995) 296-299.
4. E.A. Veal, A.M. Day, B.A. Morgan, Hydrogen peroxide sensing and signaling, Mol. Cell. 26 (2007) 1-14.
5. C.E. Paulsen, K.S. Carroll, Orchestrating redox signaling networks through regulatory cysteine switches, ACS Chem. Biol. 5 (2010) 47-62.
6. J.N. Andersen, P.G. Jansen, S.M. Echwald, O.H. Mortensen, T. Fukada, R. Del Vecchio, N.K. Tonks, N.P. Moller, A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage, Faseb J. 18 (2004) 8-30.
7. J. den Hertog, A. Ostman, F.D. Bohmer, Protein tyrosine phosphatases: regulatory mechanisms, Febs. J. 275 (2008) 831-847.
8. J.J. Tanner, Z.D. Parsons, A.H. Cummings, H. Zhou, K.S. Gates, Redox regulation of protein tyrosine phosphatases: structural and chemical aspects, Antioxid. Redox Signal. 15 (2011) 77-97.
9. A. Ostman, J. Frijhoff, A. Sandin, F.D. Bohmer, Regulation of protein tyrosine phosphatases by reversible oxidation, J. Biochem. 150 (2011) 345-356.
10. R. Karisch, B.G. Neel, Methods to monitor classical protein-tyrosine phosphatase oxidation, Febs. J. 280 (2013) 459-475.
11. T.C. Meng, T. Fukada, N.K. Tonks, Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo, Mol. Cell. 9 (2002) 387-399.
12. B. Boivin, S. Zhang, J.L. Arbiser, Z.Y. Zhang, N.K. Tonks, A modified cysteinyllabeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells, Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 9959-9964.
13. C. Persson, T. Sjoblom, A. Groen, K. Kappert, U. Engstrom, U. Hellman, C.H. Heldin, J. den Hertog, A. Ostman, Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases, Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 1886-1891.
14. R. Karisch, M. Fernandez, P. Taylor, C. Virtanen, J.R. St-Germain, L.L. Jin, I.S. Harris, J. Mori, T.W. Mak, Y.A. Senis, A. Ostman, M.F. Moran, B.G. Neel, Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome", Cell 146 (2011) 826-840.
15. L.V. Benitez, W.S. Allison, The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins, J. Biol. Chem. 249 (1974) 6234-6243.
16. C.E. Paulsen, K.S. Carroll, Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery, Chem. Rev. 113 (2013) 4633-4679.
17. S.E. Leonard, F.J. Garcia, D.S. Goodsell, K.S. Carroll, Redox-based probes for protein tyrosine phosphatases, Angew. Chem. Int. Ed. Engl. 50 (2011) 4423-4427.
18. A. Haque, J.N. Andersen, A. Salmeen, D. Barford, N.K. Tonks, Conformationsensing antibodies stabilize the oxidized form of PTP1B and inhibit its phosphatase activity, Cell 147 (2011) 185-198.
19. G. Charron, M.M. Zhang, J.S. Yount, J. Wilson, A.S. Raghavan, E. Shamir, H.C. Hang, Robust fluorescent detection of protein fatty-acylation with chemical reporters, J. Am. Chem. Soc. 131 (2009) 4967-4975.
20. W. Wang, S. Hong, A. Tran, H. Jiang, R. Triano, Y. Liu, X. Chen, P. Wu, Sulfated ligands for the copper(I)-catalyzed azide-alkyne cycloaddition, Chem. Asian J. 6 (2011) 2796-2802.
21. A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, N.K. Tonks, D. Barford, Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate, Nature 423 (2003) 769-773.
22. R.L. van Montfort, M. Congreve, D. Tisi, R. Carr, H. Jhoti, Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B, Nature 423 (2003) 773-777.
23. Y.H. Seo, K.S. Carroll, Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 16163-16168.
24. S.L. McGovern, E. Caselli, N. Grigorieff, B.K. Shoichet, A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening, J. Med. Chem. 45 (2002) 1712-1722.
25. T.P. Shiau, D.A. Erlanson, E.M. Gordon, Selective reduction of peptide isothiazolidin- 3-ones, Org. Lett. 8 (2006) 5697-5699.
26. S. Liu, B. Zhou, H. Yang, Y. He, Z.X. Jiang, S. Kumar, L. Wu, Z.Y. Zhang, Aryl vinyl sulfonates and sulfones as active site-directed and mechanism-based probes for protein tyrosine phosphatases, J. Am. Chem. Soc. 130 (2008) 8251-8260.
27. S.R. Lee, K.S. Kwon, S.R. Kim, S.G. Rhee, Reversible inactivation of proteintyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor, J. Biol. Chem. 273 (1998) 15366-15372.
28. T.C. Meng, D.A. Buckley, S. Galic, T. Tiganis, N.K. Tonks, Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B, J. Biol. Chem. 279 (2004) 37716-37725.
29. K. Mahadev, H. Motoshima, X. Wu, J.M. Ruddy, R.S. Arnold, G. Cheng, J.D. Lambeth, B.J. Goldstein, The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction, Mol. Cell. Biol. 24 (2004) 1844-1854.
30. K. Mahadev, X. Wu, A. Zilbering, L. Zhu, J.T. Lawrence, B.J. Goldstein, Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes, J. Biol. Chem. 276 (2001) 48662-48669.
31. B.J. Goldstein, A. Bittner-Kowalczyk, M.F. White, M. Harbeck, Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by proteintyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein, J. Biol. Chem. 275 (2000) 4283-4289.
32. A. Salmeen, J.N. Andersen, M.P. Myers, N.K. Tonks, D. Barford, Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B, Mol. Cell. 6 (2000) 1401-1412.
33. L. Xie, S.Y. Lee, J.N. Andersen, S. Waters, K. Shen, X.L. Guo, N.P. Moller, J.M. Olefsky, D.S. Lawrence, Z.Y. Zhang, Cellular effects of small molecule PTP1B inhibitors on insulin signaling, Biochemistry 42 (2003) 12792-12804.
34. A.R. Saltiel, C.R. Kahn, Insulin signalling and the regulation of glucose and lipid metabolism, Nature 414 (2001) 799-806.
35. A.P. Combs, Recent advances in the discovery of competitive protein tyrosine phosphatase 1B inhibitors for the treatment of diabetes, obesity, and cancer, J. Med. Chem. 53 (2010) 2333-2344.
36. A.J. Barr, Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development, Future Med. Chem. 2 (2010) 1563-1576.
37. S. Liu, L.F. Zeng, L. Wu, X. Yu, T. Xue, A.M. Gunawan, Y.Q. Long, Z.Y. Zhang, Targeting inactive enzyme conformation: aryl diketoacid derivatives as a new class of PTP1B inhibitors, J. Am. Chem. Soc. 130 (2008) 17075-17084.
38. T.H. Truong, K.S. Carroll, Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation, Biochemistry 51 (2012) 9954-9965.