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Pathology Research International
Volume 2011 (2011), Article ID 178265, 6 pages
http://dx.doi.org/10.4061/2011/178265
Review Article

PAR Genes: Molecular Probes to Pathological Assessment in Breast Cancer Progression

1Departments of Oncology, Hadassah-University Hospital P.O. Box 12000, Jerusalem 91120, Israel
2Departments of Pathology, Hadassah-University Hospital P.O. Box 12000, Jerusalem 91120, Israel

Received 15 September 2010; Accepted 4 January 2011

Academic Editor: Beiyun Chen

Copyright © 2011 Beatrice Uziely 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. S. Hanash, “Integrated global profiling of cancer,” Nature Reviews Cancer, vol. 4, no. 8, pp. 638–644, 2004. View at Google Scholar · View at Scopus
  2. C. Oakman, S. Bessi, E. Zafarana, F. Galardi, L. Biganzoli, and A. Di Leo, “Recent advances in systemic therapy: new diagnostics and biological predictors of outcome in early breast cancer,” Breast Cancer Research, vol. 11, no. 2, p. 205, 2009. View at Google Scholar · View at Scopus
  3. S. Paik, S. Shak, G. Tang et al., “A multigene assay to predict recurrence of tamoxifen-treated, node-negative breast cancer,” New England Journal of Medicine, vol. 351, no. 27, pp. 2817–2826, 2004. View at Publisher · View at Google Scholar · View at Scopus
  4. S. R. Coughlin, “Thrombin signalling and protease-activated receptors,” Nature, vol. 407, no. 6801, pp. 258–264, 2000. View at Publisher · View at Google Scholar · View at Scopus
  5. P. Arora, B. D. Cuevas, A. Russo, G. L. Johnson, and J. Trejo, “Persistent transactivation of EGFR and ErbB2/HER2 by protease-activated receptor-1 promotes breast carcinoma cell invasion,” Oncogene, vol. 27, no. 32, pp. 4434–4445, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. M. L. Nierodzik and S. Karpatkin, “Thrombin induces tumor growth, metastasis, and angiogenesis: evidence for a thrombin-regulated dormant tumor phenotype,” Cancer Cell, vol. 10, no. 5, pp. 355–362, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. F. R. Rickles and R. L. Edwards, “Activation of blood coagulation in cancer: trousseau's syndrome revisited,” Blood, vol. 62, no. 1, pp. 14–31, 1983. View at Google Scholar · View at Scopus
  8. E. Camerer, D. N. Duong, J. R. Hamilton, and S. R. Coughlin, “Combined deficiency of protease-activated receptor-4 and fibrinogen recapitulates the hemostatic defect but not the embryonic lethality of prothrombin deficiency,” Blood, vol. 103, no. 1, pp. 152–154, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. J. S. Palumbo, K. W. Kombrinck, A. F. Drew et al., “Fibrinogen is an important determinant of the metastatic potential of circulating tumor cells,” Blood, vol. 96, no. 10, pp. 3302–3309, 2000. View at Google Scholar · View at Scopus
  10. M. Riewald, V. V. Kravchenko, R. J. Petrovan et al., “Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1,” Blood, vol. 97, no. 10, pp. 3109–3116, 2001. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Su, Y. Li, Y. Luo et al., “Proteinase-activated receptor 2 expression in breast cancer and its role in breast cancer cell migration,” Oncogene, vol. 28, no. 34, pp. 3047–3057, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. M. E.W. Collier, C. Li, and C. Ettelaie, “Influence of exogenous tissue factor on estrogen receptor alpha expression in breast cancer cells: involvement of beta1-integrin, PAR2, and mitogen-activated protein kinase activation,” Molecular Cancer Research, vol. 6, no. 12, pp. 1807–1818, 2008. View at Publisher · View at Google Scholar
  13. S. Even-Ram, B. Uziely, P. Cohen et al., “Thrombin receptor overexpression in malignant and physiological invasion processes,” Nature Medicine, vol. 4, no. 8, pp. 909–914, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Grisaru-Granovsky, Z. Salah, M. Maoz, D. Pruss, U. Beller, and R. Bar-Shavit, “Differential expression of Protease activated receptor 1 (Par1) and pY397FAK in benign and malignant human ovarian tissue samples,” International Journal of Cancer, vol. 113, no. 3, pp. 372–378, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. S. C. Even-Ram, S. Grisaru-Granovsky, D. Pruss et al., “The pattern of expression of protease-activated receptors (PARs) during early trophoblast development,” Journal of Pathology, vol. 200, no. 1, pp. 47–52, 2003. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Boire, L. Covic, A. Agarwal, S. Jacques, S. Sherifi, and A. Kuliopulos, “PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells,” Cell, vol. 120, no. 3, pp. 303–313, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. M. A. Booden, L. B. Eckert, C. J. Der, and J. Trejo, “Persistent signaling by dysregulated thrombin receptor trafficking promotes breast carcinoma cell invasion,” Molecular and Cellular Biology, vol. 24, no. 5, pp. 1990–1999, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. C. Tellez, M. McCarty, M. Ruiz, and M. Bar-Eli, “Loss of activator protein-2alpha results in overexpression of protease-activated receptor-1 and correlates with the malignant phenotype of human melanoma,” Journal of Biological Chemistry, vol. 278, no. 47, pp. 46632–46642, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. Z. Salah, M. Maoz, G. Pizov, and R. Bar-Shavit, “Transcriptional regulation of human protease-activated receptor 1: a role for the early growth response-1 protein in prostate cancer,” Cancer Research, vol. 67, no. 20, pp. 9835–9843, 2007. View at Publisher · View at Google Scholar · View at Scopus
  20. Z. Salah, S. Haupt, M. Maoz et al., “p53 controls hPar1 function and expression,” Oncogene, vol. 27, no. 54, pp. 6866–6874, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. R. Saban, M. R. D'Andrea, P. Andrade-Gordon et al., “Mandatory role of proteinase-activated receptor 1 in experimental bladder inflammation,” BMC Physiology, vol. 7, p. 4, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. X. Su, E. Camerer, J. R. Hamilton, S. R. Coughlin, and M. A. Matthay, “Protease-activated receptor-2 activation induces acute lung inflammation by neuropeptide-dependent mechanisms,” Journal of Immunology, vol. 175, no. 4, pp. 2598–2605, 2005. View at Google Scholar · View at Scopus
  23. J. Trejo and S. R. Coughlin, “The cytoplasmic tails of protease-activated receptor-1 and substance P receptor specify sorting to lysosomes versus recycling,” Journal of Biological Chemistry, vol. 274, no. 4, pp. 2216–2224, 1999. View at Publisher · View at Google Scholar · View at Scopus
  24. L. Hein, K. Ishii, S. R. Coughlin, and B. K. Kobilka, “Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor,” Journal of Biological Chemistry, vol. 269, no. 44, pp. 27719–27726, 1994. View at Google Scholar · View at Scopus
  25. I. Cohen, M. Maoz, H. Turm et al., “Etk/Bmx regulates proteinase-activated-receptor1 (PAR1) in breast cancer invasion: signaling partners, hierarchy and physiological significance,” Plos One, vol. 5, no. 6, Article ID e11135, 2010. View at Publisher · View at Google Scholar
  26. C. T. Griffin, Y. Srinivasan, Y. W. Zheng, W. Huang, and S. R. Coughlin, “A role for thrombin receptor signaling in endothelial cells during embryonic development,” Science, vol. 293, no. 5535, pp. 1666–1670, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. A. J. Connolly, H. Lshihara, M. L. Kahn, R. V. Farese, and S. R. Coughlin, “Role of the thrombin receptor an development and evidence for a second receptor,” Nature, vol. 381, no. 6582, pp. 516–519, 1996. View at Google Scholar · View at Scopus
  28. Y. Qiu and H. J. Kung, “Signaling network of the Btk family kinases,” Oncogene, vol. 19, no. 49, pp. 5651–5661, 2000. View at Google Scholar · View at Scopus
  29. Y. Qiu, D. Robinson, T. G. Pretlow, and H. J. Kung, “Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 7, pp. 3644–3649, 1998. View at Google Scholar · View at Scopus
  30. Y. T. Tsai, YI. H. Su, S. S. Fang et al., “Etk, a Btk family tyrosine kinase, mediates cellular transformation by linking src to STAT3 activation,” Molecular and Cellular Biology, vol. 20, no. 6, pp. 2043–2054, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. E. Yang, A. Boire, A. Agarwal et al., “Blockade of PAR1 signaling with cell-penetrating pepducins inhibits Akt survival pathways in breast cancer cells and suppresses tumor survival and metastasis,” Cancer Research, vol. 69, no. 15, pp. 6223–6231, 2009. View at Publisher · View at Google Scholar · View at Scopus