Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2009, Article ID 850940, 11 pages
http://dx.doi.org/10.1155/2009/850940
Research Article

Cathepsin G, a Neutrophil Protease, Induces Compact Cell-Cell Adhesion in MCF-7 Human Breast Cancer Cells

1Faculty of Pharmaceutical Sciences, Teikyo University, 1091-1 Sagamiko, Sagamihara, Kanagawa 229-0195, Japan
2Department of Molecular Virology and Oncology, Cancer Research Institute, Kanazawa University, 13-1 Takara-machi, Kanazawa 920-0934, Japan

Received 23 May 2009; Revised 6 August 2009; Accepted 21 August 2009

Academic Editor: Hidde Bult

Copyright © 2009 Tomoya Kudo 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. R. M. Senior, E. J. Campbell, J. A. Landis, F. R. Cox, C. Kuhn, and H. S. Koren, “Elastase of U-937 monocytelike cells. Comparisons with elastases derived from human monocytes and neutrophils and murine macrophagelike cells,” Journal of Clinical Investigation, vol. 69, no. 2, pp. 384–393, 1982. View at Google Scholar · View at Scopus
  2. R. M. Senior and E. J. Campbell, “Cathepsin G in human mononuclear phagocytes: comparisons between monocytes and U937 monocyte-like cells,” Journal of Immunology, vol. 132, no. 5, pp. 2547–2551, 1984. View at Google Scholar · View at Scopus
  3. E. J. Campbell, E. K. Silverman, and M. A. Campbell, “Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity,” Journal of Immunology, vol. 143, no. 9, pp. 2961–2968, 1990. View at Google Scholar · View at Scopus
  4. G. Salvesen, D. Farley, J. Shuman, A. Przybyla, C. Reilly, and J. Travis, “Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases,” Biochemistry, vol. 26, no. 8, pp. 2289–2293, 1987. View at Google Scholar · View at Scopus
  5. O. Wiedow and U. Meyer-Hoffert, “Neutrophil serine proteases: potential key regulators of cell signalling during inflammation,” Journal of Internal Medicine, vol. 257, no. 4, pp. 319–328, 2005. View at Google Scholar · View at Scopus
  6. H. Odeberg and I. Olsson, “Antibacterial activity of cationic proteins from human granulocytes,” Journal of Clinical Investigation, vol. 56, no. 5, pp. 1118–1124, 1975. View at Google Scholar · View at Scopus
  7. S. Yui, K. Tomita, T. Kudo, S. Ando, and M. Yamazaki, “Induction of multicellular 3-D spheroids of MCF-7 breast carcinoma cells by neutrophil-derived cathepsin G and elastase,” Cancer Science, vol. 96, no. 9, pp. 560–570, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. D. R. Welch, D. J. Schissel, R. P. Howrey, and P. A. Aeed, “Tumor-elicited polymorphonuclear cells, in contrast to “normal” circulating polymorphonuclear cells, stimulate invasive and metastatic potentials of rat mammary adenocarcinoma cells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 15, pp. 5859–5863, 1989. View at Google Scholar · View at Scopus
  9. H. Tazawa, F. Okada, T. Kobayashi et al., “Infiltration of neutrophils is required for acquisition of metastatic phenotype of benign murine fibrosarcoma cells: implication of inflammation-associated carcinogenesis and tumor progression,” American Journal of Pathology, vol. 163, no. 6, pp. 2221–2232, 2003. View at Google Scholar · View at Scopus
  10. M. Takeichi, “Cadherin cell adhesion receptors as a morphogenetic regulator,” Science, vol. 251, no. 5000, pp. 1451–1455, 1991. View at Google Scholar · View at Scopus
  11. M. Takeichi, “Cadherins: a molecular family essential for selective cell-cell adhesion and animal morphogenesis,” Trends in Genetics, vol. 3, pp. 213–217, 1987. View at Google Scholar · View at Scopus
  12. A. Nose, A. Nagafuchi, and M. Takeichi, “Expressed recombinant cadherins mediate cell sorting in model systems,” Cell, vol. 54, no. 7, pp. 993–1001, 1988. View at Google Scholar · View at Scopus
  13. M. S. Steinberg and M. Takeichi, “Experimental specification of cell sorting, tissue spreading, and specific spatial patterning by quantitative differences in cadherin expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 1, pp. 206–209, 1994. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Hirano, A. Nose, K. Hatta, A. Kawakami, and M. Takeichi, “Calcium-dependent cell-cell adhesion molecules (cadherins): subclass specificities and possible involvement of actin bundles,” Journal of Cell Biology, vol. 105, no. 6, pp. 2501–2510, 1987. View at Google Scholar · View at Scopus
  15. F. Matsuzaki, R.-M. Mege, S. H. Jaffe et al., “cDNAs of cell adhesion molecules of different specificity induce changes in cell shape and border formation in cultured S180 cells,” Journal of Cell Biology, vol. 110, no. 4, pp. 1239–1252, 1990. View at Google Scholar · View at Scopus
  16. A. Nagafuchi and M. Takeichi, “Cell binding function of E-cadherin is regulated by the cytoplasmic domain,” EMBO Journal, vol. 7, no. 12, pp. 3679–3684, 1988. View at Google Scholar · View at Scopus
  17. M. Ozawa, H. Barbault, and R. Kemler, “The cytoplasmic domain of the cell adhesion molecule uvomorulin assoicates with three independent proteins structurally related in different species,” EMBO Journal, vol. 8, no. 6, pp. 1711–1717, 1989. View at Google Scholar · View at Scopus
  18. M. Ozawa and R. Kemler, “Molecular organization of the uvomorulin-catenin complex,” Journal of Cell Biology, vol. 116, no. 4, pp. 989–996, 1992. View at Google Scholar · View at Scopus
  19. M. Ozawa, J. Engel, and R. Kemler, “Single amino acid substitutions in one Ca2+ binding site of uvomorulin abolish the adhesive function,” Cell, vol. 63, no. 5, pp. 1033–1038, 1990. View at Publisher · View at Google Scholar · View at Scopus
  20. D. L. Rimm, E. R. Koslov, P. Kebriaei, C. D. Cianci, and J. S. Morrow, “α 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 19, pp. 8813–8817, 1995. View at Publisher · View at Google Scholar · View at Scopus
  21. H. Aberle, S. Butz, J. Stappert, H. Weissig, R. Kemler, and H. Hoschuetzky, “Assembly of the cadherin-catenin complex in vitro with recombinant proteins,” Journal of Cell Science, vol. 107, no. 12, pp. 3655–3663, 1994. View at Google Scholar · View at Scopus
  22. T.-S. Jou, D. B. Stewart, J. Stappert, W. J. Nelson, and J. A. Marrs, “Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 11, pp. 5067–5071, 1995. View at Publisher · View at Google Scholar · View at Scopus
  23. C. L. Adams, Y.-T. Chen, S. J. Smith, and W. J. Nelson, “Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein,” Journal of Cell Biology, vol. 142, no. 4, pp. 1105–1119, 1998. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Takai, J. Miyoshi, W. Ikeda, and H. Ogita, “Nectins and nectin-like molecules: roles in contact inhibition of cell movement and proliferation,” Nature Reviews Molecular Cell Biology, vol. 9, no. 8, pp. 603–615, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  25. L. Rønnov-Jessen, O. W. Petersen, and M. J. Bissell, “Cellular changes involved in conversion of normal to malignant breast: importance of the stromal reaction,” Physiological Reviews, vol. 76, no. 1, pp. 69–125, 1996. View at Google Scholar · View at Scopus
  26. B. Gumbiner, B. Stevenson, and A. Grimaldi, “The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex,” Journal of Cell Biology, vol. 107, no. 4, pp. 1575–1587, 1988. View at Google Scholar · View at Scopus
  27. M. R. Kooistra, N. Dube, and J. L. Bos, “Rap1: a key regulator in cell-cell junction formation,” Journal of Cell Science, vol. 120, no. 1, pp. 17–22, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. C. Hogan, N. Serpente, P. Cogram et al., “Rap1 regulates the formation of E-cadherin-based cell-cell contacts,” Molecular and Cellular Biology, vol. 24, no. 15, pp. 6690–6700, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  29. E. C. Lerner, T.-T. Zhang, D. B. Knowles, Y. Qian, A. D. Hamilton, and S. M. Sebti, “Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines,” Oncogene, vol. 15, no. 11, pp. 1283–1288, 1997. View at Google Scholar · View at Scopus
  30. M. Jaggi, P. S. Rao, D. J. Smith et al., “E-cadherin phosphorylation by protein kinase D1/protein kinase Cμ is associated with altered cellular aggregation and motility in prostate cancer,” Cancer Research, vol. 65, no. 2, pp. 483–492, 2005. View at Google Scholar · View at Scopus
  31. M. Gschwendt, S. Dieterich, J. Rennecke, W. Kittstein, H.-J. Mueller, and F.-J. Johannes, “Inhibition of protein kinase Cμ by various inhibitors. Differentiation from protein kinase c isoenzymes,” FEBS Letters, vol. 392, no. 2, pp. 77–80, 1996. View at Publisher · View at Google Scholar · View at Scopus
  32. P. D. Davis, C. H. Hill, G. Lawton et al., “Inhibitors of protein kinase C. 1. 2,3-bisarylmaleimides,” Journal of Medicinal Chemistry, vol. 35, no. 1, pp. 177–184, 1992. View at Google Scholar · View at Scopus
  33. P. R. Hansen, “Role of neutrophils in myocardial ischemia and reperfusion,” Circulation, vol. 91, no. 6, pp. 1872–1885, 1995. View at Google Scholar · View at Scopus
  34. M. Molino, N. Blanchard, E. Belmonte et al., “Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G,” Journal of Biological Chemistry, vol. 270, no. 19, pp. 11168–11175, 1995. View at Publisher · View at Google Scholar · View at Scopus
  35. L. M. Coussens and Z. Werb, “Inflammation and cancer,” Nature, vol. 420, no. 6917, pp. 860–867, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  36. T. T. Onder, P. B. Gupta, S. A. Mani, J. Yang, E. S. Lander, and R. A. Weinberg, “Loss of E-cadherin promotes metastasis via multiple downstream transcriptional pathways,” Cancer Research, vol. 68, no. 10, pp. 3645–3654, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. P. Friedl, Y. Hegerfeldt, and M. Tusch, “Collective cell migration in morphogenesis and cancer,” International Journal of Developmental Biology, vol. 48, no. 5-6, pp. 441–449, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. P. Friedl and K. Wolf, “Tumour-cell invasion and migration: diversity and escape mechanisms,” Nature Reviews Cancer, vol. 3, no. 5, pp. 362–374, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  39. P. Friedl, “Prespecification and plasticity: shifting mechanisms of cell migration,” Current Opinion in Cell Biology, vol. 16, no. 1, pp. 14–23, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. S. S. Kantak and R. H. Kramer, “E-cadherin regulates anchorage-independent growth and survival in oral squamous cell carcinoma cells,” Journal of Biological Chemistry, vol. 273, no. 27, pp. 16953–16961, 1998. View at Publisher · View at Google Scholar · View at Scopus
  41. G. R. Sambrano, W. Huang, T. Faruqi, S. Mahrus, C. Craik, and S. R. Coughlin, “Cathepsin G activates protease-activated receptor-4 in human platelets,” Journal of Biological Chemistry, vol. 275, no. 10, pp. 6819–6823, 2000. View at Publisher · View at Google Scholar · View at Scopus