Table of Contents Author Guidelines Submit a Manuscript
Disease Markers
Volume 35 (2013), Issue 3, Pages 195–202
http://dx.doi.org/10.1155/2013/740201
Research Article

Overexpression of FXYD-3 Is Involved in the Tumorigenesis and Development of Esophageal Squamous Cell Carcinoma

1Department of Pathology, The First Hospital of Hebei Medical University, Shijiazhuang 050031, China
2Graduate School of Hebei Medical University, Shijiazhuang 050017, China
3Central Laboratory, The First Hospital of Hebei Medical University, Shijiazhuang 050031, China
4Clinical College of Hebei Medical University, Shijiazhuang 050031, China
5Applied Tumor Virology, University of Heidelberg, Heidelberg, Germany
6Division of Oncology, Department of Clinical and Experimental Medicine, Faculty of Health Sciences, Country Council of Östergötland, University of Linköping, 581 85 Linköping, Sweden

Received 2 January 2013; Revised 13 June 2013; Accepted 16 July 2013

Academic Editor: Yuk Ming Dennis Lo

Copyright © 2013 Zhen-Long Zhu 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. Z. B. Wu and G. H. Yang, Chinese Surgical Pathology, People's Health Press, Beijing, China, 2002.
  2. K. Geering, “FXYD3 proteins: new regulators of Na–K-ATPase,” American Journal of Physiology. Renal Physiology, vol. 29, pp. 241–250, 2006. View at Google Scholar
  3. S. Bibert, S. Roy, D. Schaer, E. Felley-Bosco, and K. Geering, “Structural and functional properties of two human FXYD3 (Mat-8) isoforms,” Journal of Biological Chemistry, vol. 281, no. 51, pp. 39142–39151, 2006. View at Publisher · View at Google Scholar · View at Scopus
  4. B. W. Morrison, J. Randall Moorman, G. C. Kowdley, Y. M. Kobayashi, L. R. Jones, and P. Leder, “Mat-8, a novel phospholemman-like protein expressed in human breast tumors, induces a chloride conductance in Xenopus oocytes,” Journal of Biological Chemistry, vol. 270, no. 5, pp. 2176–2182, 1995. View at Publisher · View at Google Scholar · View at Scopus
  5. H. Kayed, J. Kleeff, A. Kolb et al., “FXYD3 is overexpressed in pancreatic ductal adenocarcinoma and influences pancreatic cancer cell growth,” International Journal of Cancer, vol. 118, no. 1, pp. 43–54, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Grzmil, S. Voigt, P. Thelen, B. Hemmerlein, K. Helmke, and P. Burfeind, “Up-regulated expression of the MAT-8 gene in prostate cancer and its siRNA-mediated inhibition of expression induces a decrease in proliferation of human prostate carcinoma cells,” International Journal of Oncology, vol. 24, no. 1, pp. 97–105, 2004. View at Google Scholar · View at Scopus
  7. M. H. Vaarala, K. Porvari, A. Kyllönen, and P. Vihko, “Differentially expressed genes in two LNCaP prostate cancer cell lines reflecting changes during prostate cancer progression,” Laboratory Investigation, vol. 80, no. 8, pp. 1259–1268, 2000. View at Google Scholar · View at Scopus
  8. Z. Zhang, S.-T. Pang, K. A. Kasper et al., “FXYD3: a promising biomarker for urothelial carcinoma,” Biomarker Insights, vol. 6, pp. 17–26, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. C. Gazquez, M. J. Ribal, M. Marin-Aguilern et al., “Biomarkers vs conventional histological analysis to detect lymph node micremetastases in bladder cancer: a real improvement?” British Journal of Urology International, vol. 110, pp. 1310–1316, 2012. View at Publisher · View at Google Scholar
  10. S. Meding, B. Balluff, M. Elsner et al., “Tissue-based protemics reveals FXYD3, S100A11 and GSTM3 as novel markers for regional lymph node metastasis in colon cancer,” The Journal of Pathology, 2012. View at Publisher · View at Google Scholar
  11. R. Kiyamova, O. Garifukin, V. Gryshkova et al., “Preliminary study of thyroid and colon cancers-associated antigens and their cognate autoantibodies as potential cancer biomarkers,” Biomarkers, vol. 17, pp. 362–371, 2012. View at Google Scholar
  12. M. Marín-Aguilera, L. Mengual, M. J. Ribal et al., “Utility of urothelial mRNA markers in blood for staging and monitoring bladder cancer,” Urology, vol. 79, no. 1, pp. 240.e9–240.e15, 2012. View at Publisher · View at Google Scholar · View at Scopus
  13. J. Qin and C. Wu, “ILK: a pseudokinase in the cancer stage of cell-matrix adhesion and signaling,” Current Opinion in Cell Biology, vol. 24, pp. 607–613, 2012. View at Google Scholar
  14. E. Montanez, D. E. Karaköse, D. Tischner, A. Villunger, and R. Fässler, “PINCH-1 promotes Bcl-2-dependent survival signalling and inhibits JNK-mediated apoptosis in the primitive endoderm,” Journal of Cell Science, vol. 125, pp. 5233–5240, 2012. View at Google Scholar
  15. A. Rearden, “A new LIM protein containing an autoepitope homologous to ‘senescent cell antigen’,” Biochemical and Biophysical Research Communications, vol. 201, no. 3, pp. 1124–1131, 1994. View at Publisher · View at Google Scholar · View at Scopus
  16. C. Wu, “PINCH, N(i)ck and the ILK: network wiring at cell-matrix adhesions,” Trends in Cell Biology, vol. 15, no. 9, pp. 460–466, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. Y. Tu, F. Li, S. Goicoechea, and C. Wu, “The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells,” Molecular and Cellular Biology, vol. 19, no. 3, pp. 2425–2434, 1999. View at Google Scholar · View at Scopus
  18. D. Malan, A. Elischer, M. Hesse, S. A. Wickström, B. K. Fleischmann, and W. Bloch, “Deletion of integrin linked kinase in endothelial cells results in defective RTK signaling caused by caveolin 1 mislocalization,” Development, vol. 140, pp. 987–995, 2013. View at Google Scholar
  19. J. Wang-Rodriguez, A. D. Dreilinger, G. M. Alsharabi, and A. Rearden, “The signaling adapter protein PINCH is up-regulated in the stroma of common cancers, notably at invasive edges,” Cancer, vol. 95, no. 6, pp. 1387–1395, 2002. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Gao, G. Arbman, A. Rearden, and X.-F. Sun, “Stromal staining for PINCH is an independent prognostic indicator in colorectal cancer,” Neoplasia, vol. 6, no. 6, pp. 796–801, 2004. View at Publisher · View at Google Scholar · View at Scopus
  21. Z.-R. Zhao, Z.-Y. Zhang, D.-S. Cui et al., “Particularly interesting new cysteine-histidine rich protein expression in colorectal adenocarcinomas,” World Journal of Gastroenterology, vol. 12, no. 2, pp. 298–301, 2006. View at Google Scholar · View at Scopus
  22. M.-W. Wang, P. Gu, Z.-Y. Zhang et al., “Expression of PINCH protein in gliomas and its clinicopathological significance,” Oncology, vol. 72, no. 5-6, pp. 343–346, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. J.-T. Zhang, Q.-X. Li, D. Wang et al., “Up-regulation of PINCH in the stroma of oral squamous cell carcinoma predicts nodal metastasis,” Oncology Reports, vol. 14, no. 6, pp. 1519–1522, 2005. View at Google Scholar · View at Scopus
  24. B.-Y. Yan, D.-W. Wang, Z.-L. Zhu et al., “Overexpression of MAC30 in the cytoplasm of oral squamous cell carcinoma predicts nodal metastasis and poor differentiation,” Chemotherapy, vol. 56, no. 6, pp. 424–428, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. Z. Zhu, Y. Yang, Y. Zhang et al., “PINCH expression and its significance in esophageal squamous cell carcinoma,” Disease Markers, vol. 25, no. 2, pp. 75–80, 2008. View at Google Scholar · View at Scopus
  26. H.-Z. Zhang, X.-H. Li, X. Zhang et al., “PINCH protein expression in normal endometrium, atypical endometrial hyperplasia and endometrioid endometrial carcinoma,” Chemotherapy, vol. 56, no. 4, pp. 291–297, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. C. L. Scaife, J. Shea, L. Emerson et al., “Prognostic significance of PINCH signalling in human pancreatic ductal adenocarcinoma,” HPB, vol. 12, no. 5, pp. 352–358, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. R. F. Hwang, T. Moore, T. Arumugam et al., “Cancer-associated stromal fibroblasts promote pancreatic tumor progression,” Cancer Research, vol. 68, no. 3, pp. 918–926, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. L. H. Sobin and C. Wittekind, TNM Classification of the Esophagus, John Wiley & Sons, New York, NY, USA, 6th edition, 2002.
  30. M.-W. Wang, P. Gu, Z.-Y. Zhang et al., “FXYD3 expression in gliomas and its clinicopathological significance,” Oncology Research, vol. 18, no. 4, pp. 133–139, 2009. View at Google Scholar · View at Scopus
  31. K. J. Sweadner and E. Rael, “The FXYD gene family of small ion transport regulators or channels: cDNA sequence, protein signature sequence, and expression,” Genomics, vol. 68, no. 1, pp. 41–56, 2000. View at Publisher · View at Google Scholar · View at Scopus
  32. C. J. Palmer, B. T. Scott, and L. R. Jones, “Purification and complete sequence determination of the major plasma membrane substrate for cAMP-dependent protein kinase and protein kinase C in myocardium,” Journal of Biological Chemistry, vol. 266, no. 17, pp. 11126–11130, 1991. View at Google Scholar · View at Scopus
  33. R. W. Mercer, D. Biemesderfer, D. P. Bliss Jr., J. H. Collins, and B. Forbush III, “Molecular cloning and immunological characterization of the γ polypeptide, a small protein associated with the Na,K-ATPase,” Journal of Cell Biology, vol. 121, no. 3, pp. 579–586, 1993. View at Google Scholar · View at Scopus
  34. B. Attali, H. Latter, N. Rachamim, and H. Garty, “A corticosteroid-induced gene expressing an “IsK-like” K+ channel activity in Xenopus oocytes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 13, pp. 6092–6096, 1995. View at Publisher · View at Google Scholar · View at Scopus
  35. X. Fu and M. P. Kamps, “E2a-Pbx1 induces aberrant expression of tissue-specific and developmentally regulated genes when expressed in NIH 3T3 fibroblasts,” Molecular and Cellular Biology, vol. 17, no. 3, pp. 1503–1512, 1997. View at Google Scholar · View at Scopus
  36. F. Yamaguchi, K. Yamaguchi, Y. Tai, K. Sugimoto, and M. Tokuda, “Molecular cloning and characterization of a novel phospholemman-like protein from rat hippocampus,” Molecular Brain Research, vol. 86, no. 1-2, pp. 189–192, 2001. View at Publisher · View at Google Scholar · View at Scopus
  37. P. Béguin, G. Crambert, F. Monnet-Tschudi et al., “FXYD7 is a brain-specific regulator of Na,K-ATPase α1-β isozymes,” EMBO Journal, vol. 21, no. 13, pp. 3264–3273, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. J. Arimochi, A. Ohashi-Kobayashi, and M. Maeda, “Interaction of mat-8 (FXYD-3) with Na+/K+-ATPase in colorectal cancer cells,” Biological and Pharmaceutical Bulletin, vol. 30, no. 4, pp. 648–654, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. Z.-L. Zhu, Z.-R. Zhao, Y. Zhang et al., “Expression and significance of FXYD-3 protein in gastric adenocarcinoma,” Disease Markers, vol. 28, no. 2, pp. 63–69, 2010. View at Publisher · View at Google Scholar · View at Scopus
  40. J. Arimochi, A. Kobayashi, and M. Maeda, “Stable expression and visualization of Mat-8 (FXYD-3) tagged with a fluorescent protein in Chinese Hamster Ovary (CHO)-K1 cells,” Biotechnology Letters, vol. 27, no. 14, pp. 1017–1024, 2005. View at Publisher · View at Google Scholar · View at Scopus
  41. B. W. Morrison and P. Leder, “neu and ras initiate murine mammary tumors that share genetic markers generally absent in c-myc and int-2-initiated tumors,” Oncogene, vol. 9, no. 12, pp. 3417–3426, 1994. View at Google Scholar · View at Scopus
  42. H. Yamamoto, K. Okumura, S. Toshima et al., “FXYD3 protein involved in tumor cell proliferation is overproduced in human breast cancer tissues,” Biological and Pharmaceutical Bulletin, vol. 32, no. 7, pp. 1148–1154, 2009. View at Publisher · View at Google Scholar · View at Scopus
  43. K. Okudela, T. Yazawa, J. Ishii et al., “Down-regulation of FXYD3 expression in human lung cancers: its mechanism and potential role in carcinogenesis,” American Journal of Pathology, vol. 175, no. 6, pp. 2646–2656, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. S. Bibert, D. Aebischer, F. Desgranges et al., “A link between FXYD3 (Mat-8)-mediated Na,K-ATPase regulation and differentiation of caco-2 intestinal epithelial cells,” Molecular Biology of the Cell, vol. 20, no. 4, pp. 1132–1140, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. G. J. Gordon, W. G. Richards, D. J. Sugarbaker, M. T. Jaklitsch, and R. Bueno, “A prognostic test for adenocarcinoma of the lung from gene expression profiling data,” Cancer Epidemiology Biomarkers and Prevention, vol. 12, no. 9, pp. 905–910, 2003. View at Google Scholar · View at Scopus
  46. E. Widegren, S. Önnesjö, G. Arbman et al., “Expression of FXYD3 protein in relation to biological and clinicopathological variables in colorectal cancers,” Chemotherapy, vol. 55, no. 6, pp. 407–413, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. P. Anderle, V. Rakhmanova, K. Woodford, N. Zerangue, and W. Sadée, “Messenger RNA expression of transporter and ion channel genes in undifferentiated and differentiated Caco-2 cells compared to human intestines,” Pharmaceutical Research, vol. 20, no. 1, pp. 3–15, 2003. View at Publisher · View at Google Scholar · View at Scopus
  48. A. K. Rajasekaran and S. A. Rajasekaran, “Role of Na-K-ATPase in the assembly of tight junctions,” American Journal of Physiology. Renal Physiology, vol. 285, no. 3, pp. F388–F396, 2003. View at Google Scholar · View at Scopus
  49. R. G. Contreras, L. Shoshani, C. Flores-Maldonado, A. Lázaro, and M. Cereijido, “Relationship between Na+,K+-ATPase and cell attachment,” Journal of Cell Science, vol. 112, no. 23, pp. 4223–4232, 1999. View at Google Scholar · View at Scopus