Table of Contents Author Guidelines Submit a Manuscript
Advances in Urology
Volume 2009, Article ID 723831, 8 pages
http://dx.doi.org/10.1155/2009/723831
Research Article

Tumoral Prostate Shows Different Expression Pattern of Somatostatin Receptor 2 (SSTR2) and Phosphotyrosine Phosphatase SHP-1 (PTPN6) According to Tumor Progression

Laboratorio de Biologia Molecular, Facultad de Ciencias Exactas Aplicada Químicas y Naturales, Universidad Nacional de Misiones, N3300LQH Posadas, Argentina

Received 2 May 2008; Revised 1 February 2009; Accepted 16 February 2009

Academic Editor: Daniel W. Lin

Copyright © 2009 Ariel Ernesto Cariaga-Martinez 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. Gurel, T. Iwata, C. M. Koh, S. Yegnasubramanian, W. G. Nelson, and A. M. De Marzo, “Molecular alterations in prostate cancer as diagnostic, prognostic, and therapeutic targets,” Advances in Anatomic Pathology, vol. 15, no. 6, pp. 319–331, 2008. View at Publisher · View at Google Scholar
  2. S. Wirén and P. Stattin, “Androgens and prostate cancer risk,” Best Practice & Research Clinical Endocrinology & Metabolism, vol. 22, no. 4, pp. 601–613, 2008. View at Publisher · View at Google Scholar
  3. D. Djakiew, “Dysregulated expression of growth factors and their receptors in the development of prostate cancer,” The Prostate, vol. 42, no. 2, pp. 150–160, 2000. View at Publisher · View at Google Scholar
  4. B. J. Mayer, “Clues to the evolution of complex signaling machinery,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 28, pp. 9453–9454, 2008. View at Publisher · View at Google Scholar
  5. D. Qian and A. Weiss, “T cell antigen receptor signal transduction,” Current Opinion in Cell Biology, vol. 9, no. 2, pp. 205–212, 1997. View at Publisher · View at Google Scholar
  6. J. I. Healy and C. C. Goodnow, “Positive versus negative signaling by lymphocyte antigen receptors,” Annual Review of Immunology, vol. 16, pp. 645–670, 1998. View at Publisher · View at Google Scholar
  7. K. A. Siminovitch, A. M. Lamhonwah, A. K. Somani, R. Cardiff, and G. B. Mills, “Involvement of the SHP-1 tyrosine phosphatase in regulating B lymphocyte antigen receptor signaling, proliferation and transformation,” Current Topics in Microbiology and Immunology, vol. 246, pp. 291–297, 1999. View at Google Scholar
  8. L. A. J. O'Neill, “When signaling pathways collide: positive and negative regulation of toll-like receptor signal transduction,” Immunity, vol. 29, no. 1, pp. 12–20, 2008. View at Publisher · View at Google Scholar
  9. R. Roskoski Jr., “Src kinase regulation by phosphorylation and dephosphorylation,” Biochemical and Biophysical Research Communications, vol. 331, no. 1, pp. 1–14, 2005. View at Publisher · View at Google Scholar
  10. G. Pani, K. D. Fischer, I. Mlinaric-Rascan, and K. A. Siminovitch, “Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase,” Journal of Experimental Medicine, vol. 184, no. 3, pp. 839–852, 1996. View at Publisher · View at Google Scholar
  11. R. Roskoski Jr., “Signaling by Kit protein-tyrosine kinase—the stem cell factor receptor,” Biochemical and Biophysical Research Communications, vol. 337, no. 1, pp. 1–13, 2005. View at Publisher · View at Google Scholar
  12. P. Brazeau, W. Vale, R. Burgus et al., “Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormone,” Science, vol. 179, no. 4068, pp. 77–79, 1973. View at Publisher · View at Google Scholar
  13. Y. C. Patel, “Somatostatin and its receptor family,” Frontiers in Neuroendocrinology, vol. 20, no. 3, pp. 157–198, 1999. View at Publisher · View at Google Scholar
  14. Y. Taniyama, T. Suzuki, Y. Mikami, T. Moriya, S. Satomi, and H. Sasano, “Systemic distribution of somatostatin receptor subtypes in human: an immunohistochemical study,” Endocrine Journal, vol. 52, no. 5, pp. 605–611, 2005. View at Publisher · View at Google Scholar
  15. D. Ferone, P. M. van Hagen, C. Semino et al., “Somatostatin receptor distribution and function in immune system,” Digestive and Liver Disease, vol. 36, supplement 1, pp. S68–S77, 2004. View at Publisher · View at Google Scholar
  16. L. N. Møller, C. E. Stidsen, B. Hartmann, and J. J. Holst, “Somatostatin receptors,” Biochimica et Biophysica Acta, vol. 1616, no. 1, pp. 1–84, 2003. View at Publisher · View at Google Scholar
  17. N. Benali, P. Cordelier, D. Calise et al., “Inhibition of growth and metastatic progression of pancreatic carcinoma in hamster after somatostatin receptor subtype 2 (sst2) gene expression and administration of cytotoxic somatostatin analog AN-238,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 16, pp. 9180–9185, 2000. View at Publisher · View at Google Scholar
  18. F. Tagliati, M. C. Zatelli, A. Bottoni et al., “Role of complex cyclin D1/Cdk4 in somatostatin subtype 2 receptor-mediated inhibition of cell proliferation of a medullary thyroid carcinoma cell line in vitro,” Endocrinology, vol. 147, no. 7, pp. 3530–3538, 2006. View at Publisher · View at Google Scholar
  19. F. Lopez, J.-P. Estève, L. Buscail et al., “The tyrosine phosphatase SHP-1 associates with the sst2 somatostatin receptor and is an essential component of sst2-mediated inhibitory growth signaling,” The Journal of Biological Chemistry, vol. 272, no. 39, pp. 24448–24454, 1997. View at Publisher · View at Google Scholar
  20. P. D. Zapata, R. M. Ropero, A. M. Valencia et al., “Autocrine regulation of human prostate carcinoma cell proliferation by somatostatin through the modulation of the SH2 domain containing protein tyrosine phosphatase (SHP)-1,” The Journal of Clinical Endocrinology & Metabolism, vol. 87, no. 2, pp. 915–926, 2002. View at Publisher · View at Google Scholar
  21. S. E. Alvarez, L. R. Seguin, R. S. Villarreal, C. Nahmias, and G. M. Ciuffo, “Involvement of c-Src tyrosine kinase in SHP-1 phosphatase activation by Ang II AT2 receptors in rat fetal tissues,” Journal of Cellular Biochemistry, vol. 105, no. 3, pp. 703–711, 2008. View at Publisher · View at Google Scholar
  22. K. Bedecs, N. Elbaz, M. Sutren et al., “Angiotensin II type 2 receptors mediate inhibition of mitogen-activated protein kinase cascade and functional activation of SHP-1 tyrosine phosphatase,” Biochemical Journal, vol. 325, no. 2, pp. 449–454, 1997. View at Google Scholar
  23. N. Douziech, E. Calvo, Z. Coulombe et al., “Inhibitory and stimulatory effects of somatostatin on two human pancreatic cancer cell lines: a primary role for tyrosine phosphatase SHP-1,” Endocrinology, vol. 140, no. 2, pp. 765–777, 1999. View at Publisher · View at Google Scholar
  24. C. Bousquet, N. Delesque, F. Lopez et al., “sst2 somatostatin receptor mediates negative regulation of insulin receptor signaling through the tyrosine phosphatase SHP-1,” The Journal of Biological Chemistry, vol. 273, no. 12, pp. 7099–7106, 1998. View at Publisher · View at Google Scholar
  25. A.-M. Valencia, J. L. Oliva, G. Bodega et al., “Identification of a protein-tyrosine phosphatase (SHP1) different from that associated with acid phosphatase in rat prostate,” FEBS Letters, vol. 406, no. 1-2, pp. 42–48, 1997. View at Publisher · View at Google Scholar
  26. C. Wu, M. Sun, L. Liu, and G. W. Zhou, “The function of the protein tyrosine phosphatase SHP-1 in cancer,” Gene, vol. 306, no. 1-2, pp. 1–12, 2003. View at Publisher · View at Google Scholar
  27. G. Ferjoux, C. Bousquet, P. Cordelier et al., “Signal transduction of somatostatin receptors negatively controlling cell proliferation,” Journal of Physiology, vol. 94, no. 3-4, pp. 205–210, 2000. View at Publisher · View at Google Scholar
  28. P. D. Zapata, B. Colas, P. López-Ruiz et al., “Phosphotyrosine phosphatase SHP-1, somatostatin and prostate cancer,” Actas Urológicas Españolas, vol. 28, no. 4, pp. 269–285, 2004. View at Google Scholar
  29. Z. Z. Chong and K. Maiese, “The Src homology 2 domain tyrosine phosphatases SHP-1 and SHP-2: diversified control of cell growth, inflammation, and injury,” Histology and Histopathology, vol. 22, no. 11, pp. 1251–1267, 2007. View at Google Scholar
  30. H. W. Tsui, K. Hasselblatt, A. Martin, S. C.-H. Mok, and F. W. L. Tsui, “Molecular mechanisms underlying SHP-1 gene expression,” European Journal of Biochemistry, vol. 269, no. 12, pp. 3057–3064, 2002. View at Publisher · View at Google Scholar
  31. B. Bruecher-Encke, J. D. Griffin, B. G. Neel, and U. Lorenz, “Role of the tyrosine phosphatase SHP-1 in K562 cell differentiation,” Leukemia, vol. 15, no. 9, pp. 1424–1432, 2001. View at Publisher · View at Google Scholar
  32. V. Barresi, C. Alafaci, F. Salpietro, and G. Tuccari, “Sstr2A immunohistochemical expression in human meningiomas: is there a correlation with the histological grade, proliferation or microvessel density?” Oncology Reports, vol. 20, no. 3, pp. 485–492, 2008. View at Publisher · View at Google Scholar
  33. U. Kumar, S. I. Grigorakis, H. L. Watt et al., “Somatostatin receptors in primary human breast cancer: quantitative analysis of mRNA for subtypes 1–5 and correlation with receptor protein expression and tumor pathology,” Breast Cancer Research and Treatment, vol. 92, no. 2, pp. 175–186, 2005. View at Publisher · View at Google Scholar
  34. T. Zhou, X. Xiao, B. Xu, H. Li, and Y. Zou, “Overexpression of SSTR2 inhibited the growth of SSTR2-positive tumors via multiple signaling pathways,” Acta Oncologica, vol. 48, no. 3, pp. 401–410, 2009. View at Publisher · View at Google Scholar
  35. T. Oka, T. Yoshino, K. Hayashi et al., “Reduction of hematopoietic cell-specific tyrosine phosphatase SHP-1 gene expression in natural killer cell lymphoma and various types of lymphomas/leukemias: combination analysis with cDNA expression array and tissue microarray,” The American Journal of Pathology, vol. 159, no. 4, pp. 1495–1505, 2001. View at Google Scholar
  36. G. Halmos, A. V. Schally, B. Sun, R. Davis, D. G. Bostwick, and A. Plonowski, “High expression of somatostatin receptors and messenger ribonucleic acid for its receptor subtypes in organ-confined and locally advanced human prostate cancers,” The Journal of Clinical Endocrinology & Metabolism, vol. 85, no. 7, pp. 2564–2571, 2000. View at Publisher · View at Google Scholar
  37. A. A. Sinisi, A. Bellastella, D. Prezioso et al., “Different expression patterns of somatostatin receptor subtypes in cultured epithelial cells from human normal prostate and prostate cancer,” The Journal of Clinical Endocrinology & Metabolism, vol. 82, no. 8, pp. 2566–2569, 1997. View at Publisher · View at Google Scholar
  38. J. C. Reubi, B. Waser, J. C. Schaer, and R. Markwalder, “Somatostatin receptors in human prostate and prostate cancer,” The Journal of Clinical Endocrinology & Metabolism, vol. 80, no. 9, pp. 2806–2814, 1995. View at Publisher · View at Google Scholar
  39. S. A. Kaplan, “Expression of somatostatin receptor subtypes 2 and 4 in human benign prostatic hyperplasia and prostatic cancer,” The Journal of Urology, vol. 169, no. 4, p. 1621, 2003. View at Google Scholar
  40. R. Tatoud, A. Degeorges, G. Prévost et al., “Somatostatin receptors in prostate tissues and derived cell cultures, and the in vitro growth inhibitory effect of BIM-23014 analog,” Molecular and Cellular Endocrinology, vol. 113, no. 2, pp. 195–204, 1995. View at Publisher · View at Google Scholar
  41. M. Koppan, A. Nagy, A. V. Schally, J. M. Arencibia, A. Plonowski, and G. Halmos, “Targeted cytotoxic analogue of somatostatin AN-238 inhibits growth of androgen-independent dunning R-3327-AT-1 prostate cancer in rats at nontoxic doses,” Cancer Research, vol. 58, no. 18, pp. 4132–4137, 1998. View at Google Scholar
  42. A. Plonowski, A. V. Schally, A. Nagy, B. Sun, and K. Szepeshazi, “Inhibition of PC-3 human androgen-independent prostate cancer and its metastases by cytotoxic somatostatin analogue AN-238,” Cancer Research, vol. 59, no. 8, pp. 1947–1953, 1999. View at Google Scholar
  43. D. Ferone, E. Resmini, M. Boschetti et al., “Potential indications for somatostatin analogues: immune system and limphoproliferative disorders,” Journal of Endocrinological Investigation, vol. 28, supplement 11, pp. 111–117, 2005. View at Google Scholar
  44. C. C. Delibrias, J. E. Floettmann, M. Rowe, and D. T. Fearon, “Downregulated expression of SHP-1 in Burkitt lymphomas and germinal center B lymphocytes,” Journal of Experimental Medicine, vol. 186, no. 9, pp. 1575–1583, 1997. View at Publisher · View at Google Scholar
  45. C. Wu, Q. Guan, Y. Wang, Z. J. Zhao, and G. W. Zhou, “SHP-1 suppresses cancer cell growth by promoting degradation of JAK kinases,” Journal of Cellular Biochemistry, vol. 90, no. 5, pp. 1026–1037, 2003. View at Publisher · View at Google Scholar
  46. Q. Zhang, B. Lee, M. Korecka et al., “Differences in phosphorylation of the IL-2R associated JAK/STAT proteins between HTLV-I (+), IL-2-independent and IL-2-dependent cell lines and uncultured leukemic cells from patients with adult T-cell lymphoma/leukemia,” Leukemia Research, vol. 23, no. 4, pp. 373–384, 1999. View at Publisher · View at Google Scholar
  47. Q. Zhang, P. N. Raghunath, E. Vonderheid, N. Ødum, and M. A. Wasik, “Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T-cell lymphoma cells results from methylation of the SHP-1 promoter,” The American Journal of Pathology, vol. 157, no. 4, pp. 1137–1146, 2000. View at Google Scholar
  48. M. Thangaraju, K. Sharma, D. Liu, S.-H. Shen, and C. B. Srikant, “Interdependent regulation of intracellular acidification and SHP-1 in apoptosis,” Cancer Research, vol. 59, no. 7, pp. 1649–1654, 1999. View at Google Scholar
  49. T.-S. Migone, N. A. Cacalano, N. Taylor, T. Yi, T. A. Waldmann, and J. A. Johnston, “Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor; loss of SHP-1 expression in human T-lymphotropic virus type I-transformed T cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 7, pp. 3845–3850, 1998. View at Publisher · View at Google Scholar