Inhibition of Janus kinases by tyrosine phosphorylation inhibitor, Tyrphostin AG-490

Journal of Biomolecular Structure and Dynamics

Volumn 33, Issue 11, 2015, Pages 2368-2379

  Rashid, Sajid ^a   Bibi, Nousheen ^a   Parveen, Zahida ^a   Shafique, Shagufta ^a  

^a QUAID I AZAM UNIVERSITY   (Pakistan)

Author keywords

AG 490; JAKs; molecular docking; molecular dynamics simulation; PTK domain

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; JANUS KINASE 1; JANUS KINASE 2; JANUS KINASE 3; N BENZYL 2 CYANO 3 (3,4 DIHYDROXYPHENYL)ACRYLAMIDE; ALPHA-CYANO-(3,4-DIHYDROXY)-N-BENZYLCINNAMIDE; JANUS KINASE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR; TYRPHOSTIN;

ARTICLE; BINDING AFFINITY; COMPARATIVE STUDY; CONTROLLED STUDY; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENZYME INHIBITION; ENZYME STRUCTURE; MOLECULAR DOCKING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; METABOLISM; MOLECULAR GENETICS; QUANTITATIVE STRUCTURE ACTIVITY RELATION; SEQUENCE ALIGNMENT;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; JANUS KINASE 1; JANUS KINASE 2; JANUS KINASE 3; JANUS KINASES; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN KINASE INHIBITORS; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; SEQUENCE ALIGNMENT; TYRPHOSTINS;

EID: 84942981041     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2015.1050696     Document Type: Article

References (45)

1. Aaronson, D. S., Horvath, C. M. (2002). A road map for those who don't know JAK-STAT. Science, 296, 1653-1655.
2. Boggon, T. J., Li, Y., Manley, P. W., Eck, M. J. (2005). Crystal structure of the Jak3 kinase domain in complex with a staurosporine analog. Blood, 106, 996-1002.
3. Brown, G. R., Bamford, A. M., Bowyer, J., James, D. S., Rankine, N., Tang, E., Culbert, E. J. (2000). Naphthyl ketones: A new class of Janus kinase 3 inhibitors. Bioorganic & Medicinal Chemistry Letters, 10, 575-579.
4. Davoodi-Semiromi, A., Wasserfall, C. H., Xia, C. Q., Cooper-DeHoff, R. M., Wabitsch, M., Clare-Salzler, M., Atkinson, M. (2012). The tyrphostin agent AG490 prevents and reverses type 1 diabetes in NOD mice. PLoS ONE, 7, e36079.
5. Druker, B. J. (2003). Imatinib alone and in combination for chronic myeloid leukemia. Seminars in Hematology, 40, 50-58.
6. Duan, Y., Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang, W.,., Kollman, P. (2003). A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. Journal of Computational Chemistry, 24, 1999-2012.
7. Feng, J., Witthuhn, B. A., Matsuda, T., Kohlhuber, F., Kerr, I. M., Ihle, J. N. (1997). Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. Molecular and Cellular Biology, 17, 2497-2501.
8. Firmbach-Kraft, I., Byers, M., Shows, T., Dalla-Favera, R., Krolewski, J. J. (1990). Tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene, 5, 1329-1336.
9. Frank, G. D., Saito, S., Motley, E. D., Sasaki, T., Ohba, M., Kuroki, T.,., Eguchi, S. (2002). Requirement of Ca(2+) and PKCdelta for Janus kinase 2 activation by angiotensin II: Involvement of PYK2. Molecular Endocrinology, 16, 367-377.
10. Goncalves, S., Fernandez-Sanchez, R., Sanchez-Nino, M. D., Tejedor, A., Neria, F., Egido, J.,., Ortiz, A. (2010). Tyrphostins as potential therapeutic agents for acute kidney injury. Current Medicinal Chemistry, 17, 974-986.
11. Harpur, A. G., Andres, A. C., Ziemiecki, A., Aston, R. R., Wilks, A. F. (1992). JAK2, a third member of the JAK family of protein tyrosine kinases. Oncogene, 7, 1347-1353.
12. Hubbard, T. J., Aken, B. L., Ayling, S., Ballester, B., Beal, K., Bragin, E.,., Curwen, V. (2009). Ensembl 2009. Nucleic Acids Research, 37, D690-D697.
13. Humphrey, W., Dalke, A., Schulten, K. (1996). VMD: Visual molecular dynamics. Journal of Molecular Graphics, 14, 33-38.
14. Kalykaki, A., Agelaki, S., Kallergi, G., Xyrafas, A., Mavroudis, D., Georgoulias, V. (2014). Elimination of EGFR-expressing circulating tumor cells in patients with metastatic breast cancer treated with Gefitinib. Cancer Chemotherapy and Pharmacology, 73, 685-693.
15. Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H.,., Higgins, D. G. (2007). Clustal W and Clustal X version 2.0. Bioinformatics, 23, 2947-2948.
16. Lee, S. K., Lee, J. O., Kim, J. H., Jung, J. H., You, G. Y., Park, S. H., Kim, H. S. (2010). C-peptide stimulates nitrites generation via the calcium-JAK2/STAT1 pathway in murine macrophage Raw264.7 cells. Life Sciences, 86, 863-868.
17. Levitzki, A. (1990). Tyrphostins-potential antiproliferative agents and novel molecular tools. Biochemical Pharmacology, 40, 913-918.
18. Levitzki, A. (1994). Signal-transduction therapy. A novel approach to disease management. European Journal of Biochemistry, 226, 1-13.
19. Levitzki, A., Gazit, A. (1995). Tyrosine kinase inhibition: An approach to drug development. Science, 267, 1782-1788.
20. Levy, D. E., Darnell, J. E. (2002). Signalling: Stats: Transcriptional control and biological impact. Nature Reviews Molecular Cell Biology, 3, 651-662.
21. Li, W. X. (2008). Canonical and non-canonical JAK-STAT signaling. Trends in Cell Biology, 18, 545-551.
22. Li, P., Roberts, B. P., Chakravorty, D. K., Merz Jr., K. M. (2013). Rational design of particle mesh ewald compatible Lennard-Jones parameters for +2 metal cations in explicit solvent. Journal of Chemical Theory and Computation, 9, 2733-2748.
23. Lucet, I. S., Fantino, E., Styles, M., Bamert, R., Patel, O., Broughton, S. E.,., Rossjohn, J. (2006). The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor. Blood, 107, 176-183.
24. Luo, C., Laaja, P. (2004). Inhibitors of JAKs/STATs and the kinases: A possible new cluster of drugs. Drug Discovery Today, 9, 268-275.
25. McGuffin, L. J., Bryson, K., Jones, D. T. (2000). The PSIPRED protein structure prediction server. Bioinformatics, 16, 404-405.
26. Meng, E. C., Pettersen, E. F., Couch, G. S., Huang, C. C., Ferrin, T. E. (2006). Tools for integrated sequence-structure analysis with UCSF Chimera. BMC Bioinformatics, 7, 339.
27. Meydan, N., Grunberger, T., Dadi, H., Shahar, M., Arpaia, E., Lapidot, Z.,., Roifman, C. M. (1996). Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature, 379, 645-648.
28. Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30, 2785-2791.
29. Pardanani, A. (2008). JAK2 inhibitor therapy in myeloproliferative disorders: Rationale, preclinical studies and ongoing clinical trials. Leukemia, 22, 23-30.
30. Powis, G. (1994). Signalling pathways as target for anticancer drug development. Pharmacology & Therapeutics, 62, 57-95.
31. Rane, S. G., Reddy, E. P. (1994). JAK3: A novel JAK kinase associated with terminal differentiation of hematopoietic cells. Oncogene, 9, 2415-2423.
32. Santos, F. P., Kantarjian, H. M., Jain, N., Manshouri, T., Thomas, D. A., Garcia-Manero, G.,., Verstovsek, S. (2010). Phase 2 study of CEP-701, an orally available JAK2 inhibitor, in patients with primary or post-polycythemia vera/essential thrombocythemia myelofibrosis. Blood, 115, 1131-1136.
33. Santos, F. P., Verstovsek, S. (2011). JAK2 inhibitors: Whats the true therapeutic potential? Blood Reviews, 25, 53-63.
34. Schüttelkopf, A. W., van Aalten, D. M. (2004). PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallographica Section D: Biological Crystallography, 60, 1355-1363.
35. van Gurp, E., Weimar, W., Gaston, R., Brennan, D., Mendez, R., Pirsch, J.,., Chan, G. (2008). Phase 1 dose-escalation study of CP-690 550 in stable renal allograft recipients: Preliminary findings of safety, tolerability, effects on lymphocyte subsets and pharmacokinetics. American Journal of Transplantation, 8, 1711-1718.
36. Verstovsek, S., Kantarjian, H., Mesa, R. A., Pardanani, A. D., Cortes-Franco, J., Thomas, D. A.,., Tefferi, A. (2010). Safety and efficacy of INCB018424, a JAK1 and JAK2 inhibitor, in myelofibrosis. New England Journal of Medicine, 363, 1117-1127.
37. Verstovsek, S., Passamonti, F., Rambaldi, A., Barosi, G., Rosen, P. J., Rumi, E.,., Vannucchi, A. M. (2014). A phase 2 study of Ruxolitinib, an oral JAK1 and JAK2 inhibitor, in patients with advanced polycythemia vera who are refractory or intolerant to hydroxyurea. Cancer, 120, 513-520.
38. Wallace, A. C., Laskowski, R. A., Thornton, J. M. (1995). LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Engineering, Design and Selection, 8, 127-134.
39. Wilks, A. F. (1989). Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction. Proceedings of the National Academy of Sciences, 86, 1603-1607.
40. Wilks, A. F. (1990). Structure and function of the protein tyrosine kinases. Progress in Growth Factor Research, 2, 97-111.
41. Xiong, H., Zhang, Z. G., Tian, X. Q., Sun, D. F., Liang, Q. C., Zhang, Y. J.,., Fang, J. Y. (2008). Inhibition of JAK1, 2/STAT3 signaling induces apoptosis, cell cycle arrest, and reduces tumor cell invasion in colorectal cancer cells. Neoplasia, 10, 287-297.
42. Xuan, Y. T., Guo, Y., Han, H., Zhu, Y., Bolli, R. (2001). An essential role of the JAK-STAT pathway in ischemic preconditioning. Proceedings of the National Academy of Sciences, 98, 9050-9055.
43. Yamaoka, K., Saharinen, P., Pesu, M., Holt, V. E., Silvennoinen, O., OShea, J. J. (2004). The Janus kinases (Jaks). Genome Biology, 5, 253-259.
44. Zhang, L., Huang, D., Shen, D., Zhang, C., Ma, Y., Babcock, S. A.,., Ren, J. (2014). Inhibition of protein kinase C βII isoform ameliorates methylglyoxal advanced glycation endproduct-induced cardiomyocyte contractile dysfunction. Life Sciences, 94, 83-91. doi: 10.1016/j.lfs.2013.11.011
45. Zlenko, D. V. (2012). Diffusion factor calculation for TIP4P model of water. Biofizika, 57, 197-204.