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Computational and Mathematical Methods in Medicine
Volume 2015, Article ID 683679, 9 pages
http://dx.doi.org/10.1155/2015/683679
Research Article

Optimization and Corroboration of the Regulatory Pathway of p42.3 Protein in the Pathogenesis of Gastric Carcinoma

1Zhengzhou Central Hospital, Zhengzhou, Henan 450007, China
2Department of Pharmacology, School of Basic Medicine, Zhengzhou University, Zhengzhou, Henan 450001, China
3Department of Oncology, The First Affiliated Hospital, College of Medicine of Xi’an Jiaotong University, Xi’an, Shaanxi 710061, China

Received 29 July 2014; Revised 17 October 2014; Accepted 24 October 2014

Academic Editor: Antonino Staiano

Copyright © 2015 Yibin Hao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. G. Zhang, J. F. Li, B. Q. Yu, Z. G. Zhu, B. Y. Liu, and M. Yan, “microRNA-21 promotes tumor proliferation and invasion in gastric cancer by targeting PTEN,” Oncology Reports, vol. 27, no. 4, pp. 1019–1026, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. G.-H. Zhao, T.-C. Li, L.-H. Shi et al., “Relationship between inactivation of p16 gene and gastric carcinoma,” World Journal of Gastroenterology, vol. 9, no. 5, pp. 905–909, 2003. View at Google Scholar · View at Scopus
  3. Y.-H. Seo, Y.-E. Joo, S.-K. Choi, J.-S. Rew, C.-S. Park, and S.-J. Kim, “Prognostic significance of p21 and p53 expression in gastric cancer,” The Korean Journal of Internal Medicine, vol. 18, no. 2, pp. 98–103, 2003. View at Google Scholar · View at Scopus
  4. B. Xiao, E.-D. Zhu, N. Li et al., “Increased miR-146a in gastric cancer directly targets SMAD4 and is involved in modulating cell proliferation and apoptosis,” Oncology Reports, vol. 27, no. 2, pp. 559–566, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. E. Rippa, G. la Monica, R. Allocca, M. F. Romano, M. de Palma, and P. Arcari, “Overexpression of gastrokine 1 in gastric cancer cells induces Fas-mediated apoptosis,” Journal of Cellular Physiology, vol. 226, no. 10, pp. 2571–2578, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. Y.-Y. Du, D.-Q. Dai, and Z. Yang, “Role of RECK methylation in gastric cancer and its clinical significance,” World Journal of Gastroenterology, vol. 16, no. 7, pp. 904–908, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. L. Zhang, Y. Hou, H. Ashktorab et al., “The impact of C-MYC gene expression on gastric cancer cell,” Molecular and Cellular Biochemistry, vol. 344, no. 1-2, pp. 125–135, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. C. Holmberg, B. Ghesquière, F. Impens et al., “Mapping proteolytic processing in the secretome of gastric cancer-associated myofibroblasts reveals activation of MMP-1, MMP-2, and MMP-3,” Journal of Proteome Research, vol. 12, no. 7, pp. 3413–3422, 2013. View at Publisher · View at Google Scholar · View at Scopus
  9. X. Xu, W. Li, X. Fan et al., “Identification and characterization of a novel p42.3 gene as tumor-specific and mitosis phase-dependent expression in gastric cancer,” Oncogene, vol. 26, no. 52, pp. 7371–7379, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. W. Sun, Expression Change and Biological Significance of P42.3 in Gastric Mucosal Lesion, Beijing Cancer Hospital, Beijing, China, 2012.
  11. J. Zhang, C. Lu, Z. Shang, R. Xing, L. Shi, and Y. Lv, “p42.3 gene expression in gastric cancer cell and its protein regulatory network analysis,” Theoretical Biology and Medical Modelling, vol. 9, no. 1, article 53, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. M. F. Shao, Threading Method Research on Protein Structure Prediction, Graduate School of Chinese Academy of Sciences, 2011.
  13. C. Sandeep, V. Ravindra, J. Basuthkar et al., “Protein structure quality assessment based on the distance profiles of consecutive backbone Cα atoms,” F1000 Research, vol. 2, p. 211, 2013. View at Publisher · View at Google Scholar
  14. Y. Li, A. Roy, and Y. Zhang, “HAAD: a quick algorithm for accurate prediction of hydrogen atoms in protein structures,” PLoS ONE, vol. 4, no. 8, Article ID e6701, 2009. View at Publisher · View at Google Scholar · View at Scopus
  15. I. Kato, K. Narita, and I. Fuke, “Topological considerations in protein structure. I. Disulfide linkage,” Biopolymers, vol. 4, no. 7, pp. 737–746, 1966. View at Publisher · View at Google Scholar · View at Scopus
  16. L. M. Gregoret, S. D. Rader, R. J. Fletterick, and F. E. Cohen, “Hydrogen bonds involving sulfur atoms in proteins,” Proteins: Structure, Function and Genetics, vol. 9, no. 2, pp. 99–107, 1991. View at Publisher · View at Google Scholar · View at Scopus
  17. M. N. Wass, L. A. Kelley, and M. J. E. Sternberg, “3DLigandSite: predicting ligand-binding sites using similar structures,” Nucleic Acids Research, vol. 38, no. 2, pp. W469–W473, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. E. Santonico, S. Panni, M. Falconi, L. Castagnoli, and G. Cesareni, “Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction,” BMC Biochemistry, vol. 8, article 29, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Koshiba, T. Kigawa, J. Iwahara, A. Kikuchi, and S. Yokoyama, “Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1),” FEBS Letters, vol. 442, no. 2-3, pp. 138–142, 1999. View at Publisher · View at Google Scholar · View at Scopus
  20. J. F. Harper, M. R. Sussman, G. E. Schaller, C. Putnam-Evans, H. Charbonneau, and A. C. Harmon, “A calcium-dependent protein kinase with a regulatory domain similar to calmodulin,” Science, vol. 252, no. 5008, pp. 951–954, 1991. View at Publisher · View at Google Scholar · View at Scopus
  21. A. M. Weljie and H. J. Vogel, “Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-α,” The Journal of Biological Chemistry, vol. 279, no. 34, pp. 35494–35502, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Nakamura, T. Takemura, L. Tan et al., “Small GTPase RAB45-mediated p38 activation in apoptosis of chronic myeloid leukemia progenitor cells,” Carcinogenesis, vol. 32, no. 12, pp. 1758–1772, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. M. Shintani, M. Tada, T. Kobayashi, H. Kajiho, K. Kontani, and T. Katada, “Characterization of Rab45/RASEF containing EF-hand domain and a coiled-coil motif as a self-associating GTPase,” Biochemical and Biophysical Research Communications, vol. 357, no. 3, pp. 661–667, 2007. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Sudhakar Babu, C. E. Bugg, and W. J. Cook, “Structure of calmodulin refined at 2.2 Å resolution,” Journal of Molecular Biology, vol. 204, no. 1, pp. 191–204, 1988. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Koller, B. Schnyder, and E. E. Strehler, “Structural organization of the human CaMIII calmodulin gene,” Biochimica et Biophysica Acta—Gene Structure and Expression, vol. 1087, no. 2, pp. 180–189, 1990. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Koller and E. E. Strehler, “Functional analysis of the promoters of the human CaMIII calmodulin gene and of the intronless gene coding for a calmodulin-like protein,” Biochimica et Biophysica Acta, vol. 1163, no. 1, pp. 1–9, 1993. View at Publisher · View at Google Scholar · View at Scopus
  27. H. J. Yuasa, J. A. Cox, and T. Takagi, “Genomic structure of the amphioxus calcium vector protein,” Journal of Biochemistry, vol. 126, no. 3, pp. 572–577, 1999. View at Publisher · View at Google Scholar · View at Scopus
  28. I. Théret, S. Baladi, J. A. Cox, H. Sakamoto, and C. T. Craescu, “Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement,” Biochemistry, vol. 39, no. 27, pp. 7920–7926, 2000. View at Publisher · View at Google Scholar · View at Scopus
  29. J. Jia, S. Tarabykina, C. Hansen, M. Berchtold, and M. Cygler, “Structure of apoptosis-linked protein ALG-2: insights into Ca2+-induced changes in penta-EF-hand proteins,” Structure, vol. 9, no. 4, pp. 267–275, 2001. View at Publisher · View at Google Scholar · View at Scopus
  30. J. Song, Q. Zhao, S. Thao, R. O. Frederick, and J. L. Markley, “Letter to the editor: solution structure of a calmodulin-like calcium-binding domain from Arabidopsis thaliana,” Journal of Biomolecular NMR, vol. 30, no. 4, pp. 451–456, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. E. McCormack and J. Braam, “Calmodulins and related potential calcium sensors of Arabidopsis,” New Phytologist, vol. 159, no. 3, pp. 585–598, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. M. W. Berchtold, C. W. Heizmann, and K. J. Wilson, “Primary structure of parvalbumin from rat skeletal muscle,” European Journal of Biochemistry, vol. 127, no. 2, pp. 381–389, 1982. View at Publisher · View at Google Scholar · View at Scopus
  33. T. C. Williams, D. C. Corson, K. Oikawa, W. D. McCubbin, C. M. Kay, and B. D. Sykes, “1H NMR spectroscopic studies of calcium-binding proteins. 3. Solution conformations of rat apo-α-parvalbumin and metal-bound rat α-parvalbumin,” Biochemistry, vol. 25, no. 7, pp. 1835–1846, 1986. View at Publisher · View at Google Scholar · View at Scopus
  34. D. M. Watterson, F. Sharief, and T. C. Vanaman, “The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain,” Journal of Biological Chemistry, vol. 255, no. 3, pp. 962–975, 1980. View at Google Scholar · View at Scopus
  35. K. Ogura, H. Kumeta, K. Takahasi et al., “Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin,” Genes to Cells, vol. 17, no. 3, pp. 159–172, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. J. L. Gifford, M. P. Walsh, and H. J. Vogel, “Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs,” Biochemical Journal, vol. 405, no. 2, pp. 199–221, 2007. View at Publisher · View at Google Scholar · View at Scopus
  37. A. C. Drohat, D. M. Baldisseri, R. R. Rustandi, and D. J. Weber, “Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy,” Biochemistry, vol. 37, no. 9, pp. 2729–2740, 1998. View at Publisher · View at Google Scholar · View at Scopus
  38. P. A. Hessian and L. Fisher, “The heterodimeric complex of MRP-8 (S100A8) and MRP-14 (S100A9) antibody recognition, epitope definition and the implications for structure,” European Journal of Biochemistry, vol. 268, no. 2, pp. 353–363, 2001. View at Publisher · View at Google Scholar · View at Scopus
  39. J. Liu, Q. Zheng, Y. Deng, C.-S. Cheng, N. R. Kallenbach, and M. Lu, “A seven-helix coiled coil,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 42, pp. 15457–15462, 2006. View at Publisher · View at Google Scholar · View at Scopus
  40. O. V. Moroz, A. A. Antson, G. N. Murshudov et al., “The three-dimensional structure of human S100A12,” Acta Crystallographica Section D: Biological Crystallography, vol. 57, no. 1, pp. 20–29, 2001. View at Publisher · View at Google Scholar · View at Scopus
  41. M. Sakaguchi, H. Sonegawa, H. Murata et al., “S100A11, an dual mediator for growth regulation of human keratinocytes,” Molecular Biology of the Cell, vol. 19, no. 1, pp. 78–85, 2008. View at Publisher · View at Google Scholar · View at Scopus
  42. S. Hiratsuka, A. Watanabe, H. Aburatani, and Y. Maru, “Tumour-mediated upregulation of chemoattractants and recruitment of myeloid cells predetermines lung metastasis,” Nature Cell Biology, vol. 8, no. 12, pp. 1369–1375, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. X. G. Liu, X. P. Wang, W. F. Li et al., “Ca2+-binding protein S100A11: a novel diagnostic marker for breast carcinoma,” Oncology Reports, vol. 23, no. 5, pp. 1301–1308, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. R. Yao, D. D. Davidson, A. Lopez-Beltran, G. T. MacLennan, R. Montironi, and L. Cheng, “The S100 proteins for screening and prognostic grading of bladder cancer,” Histology and Histopathology, vol. 22, no. 7–9, pp. 1025–1032, 2007. View at Google Scholar · View at Scopus
  45. S. W. Lee, C. Tomasetto, K. Swisshelm, K. Keyomarsi, and R. Sager, “Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 6, pp. 2504–2508, 1992. View at Publisher · View at Google Scholar · View at Scopus
  46. G. Feng, X. Xu, E. M. Youssef, and R. Lotan, “Diminished expression of S100A2, a putative tumor suppressor, at early stage of human lung carcinogenesis,” Cancer Research, vol. 61, no. 21, pp. 7999–8004, 2001. View at Google Scholar · View at Scopus
  47. I. D. Kyriazanos, M. Tachibana, D. K. Dhar et al., “Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus,” Oncology Reports, vol. 9, no. 3, pp. 503–510, 2002. View at Google Scholar · View at Scopus
  48. S. Gupta, T. Hussain, G. T. MacLennan, P. Fu, J. Patel, and H. Mukhtar, “Differential expression of S100A2 and S100A4 during progression of human prostate adenocarcinoma,” Journal of Clinical Oncology, vol. 21, no. 1, pp. 106–112, 2003. View at Publisher · View at Google Scholar · View at Scopus
  49. X. Su, Z. You, and Z. Zheng, “Effects of gene silencing in S100A2 and E-cadherin by RNA interference on gastric cancer cell proliferation and invasiveness,” Journal of China Medical University, vol. 41, no. 4, pp. 297–306, 2012. View at Google Scholar
  50. L. Ming, S. Xianzhong, and Y. Min, “Progress in Protein stuction prediction,” Biotechnology, vol. 19, no. 3, pp. 87–90, 2009. View at Google Scholar
  51. M. N. Lang, The Method and Application of Protein Stucture Alignment, Jilin University, 2009.