Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2014 (2014), Article ID 971409, 12 pages
http://dx.doi.org/10.1155/2014/971409
Research Article

Neutrophil Cathepsin G, but Not Elastase, Induces Aggregation of MCF-7 Mammary Carcinoma Cells by a Protease Activity-Dependent Cell-Oriented Mechanism

Laboratory of Host Defense, Department of Pharma-Sciences, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan

Received 3 September 2013; Revised 20 December 2013; Accepted 7 February 2014; Published 2 April 2014

Academic Editor: Simi Ali

Copyright © 2014 Satoru Yui 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. M. Canel, A. Serrels, M. C. Frame, and V. G. Brunton, “E-cadherin-integrin crosstalk in cancer invasion and metastasis,” Journal of Cell Science, vol. 126, no. 2, pp. 393–401, 2013. View at Google Scholar
  2. E. C. Woodhouse, R. F. Chuaqui, and L. A. Liotta, “General mechanisms of metastasis,” Cancer, vol. 80, no. 8, pp. 1529–1537, 1997. View at Google Scholar · View at Scopus
  3. G. P. H. Gui, J. R. Puddefoot, G. P. Vinson, C. A. Wells, and R. Carpenter, “Altered cell-matrix contact: a prerequisite for breast cancer metastasis?” British Journal of Cancer, vol. 75, no. 5, pp. 623–633, 1997. View at Google Scholar · View at Scopus
  4. G. L. Nicolson, “Cancer metastasis: tumor cell and host organ properties important in metastasis to specific secondary sites,” Biochimica et Biophysica Acta, vol. 948, no. 2, pp. 175–224, 1988. View at Google Scholar · View at Scopus
  5. U. Cavallaro and G. Christofori, “Cell adhesion in tumor invasion and metastasis: loss of the glue is not enough,” Biochimica et Biophysica Acta, vol. 1552, no. 1, pp. 39–45, 2001. View at Publisher · View at Google Scholar · View at Scopus
  6. I. J. Fidler, “The relationship of embolic homogeneity, number, size and viability to the incidence of experimental metastasis,” European Journal of Cancer, vol. 9, no. 3, pp. 223–227, 1973. View at Google Scholar · View at Scopus
  7. L. A. Liotta, J. Kleinerman, and G. M. Saidel, “The significance of hematogenous tumor cell clumps in the metastatic process,” Cancer Research, vol. 36, no. 3, pp. 889–894, 1976. View at Google Scholar · View at Scopus
  8. J. S. Tomlinson, M. L. Alpaugh, and S. H. Barsky, “An intact overexpressed E-cadherin/α,β-catenin axis characterizes the lymphovascular emboli of inflammatory breast carcinoma,” Cancer Research, vol. 61, no. 13, pp. 5231–5241, 2001. View at Google Scholar · View at Scopus
  9. S. W. Russell, G. Y. Gillespie, C. B. Hansen, and C. G. Cochrane, “Inflammatory cells in solid murine neoplasms. II. Cell types found throughout the course of Moloney sarcoma regression or progression,” International Journal of Cancer, vol. 18, no. 3, pp. 331–338, 1976. View at Google Scholar · View at Scopus
  10. F. Balkwill and A. Mantovani, “Inflammation and cancer: back to Virchow?” The Lancet, vol. 357, no. 9255, pp. 539–545, 2001. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Brigati, D. M. Noonan, A. Albini, and R. Benelli, “Tumors and inflammatory infiltrates: friends or foes?” Clinical and Experimental Metastasis, vol. 19, no. 3, pp. 247–258, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. E. Di Carlo, G. Forni, P. Lollini, M. P. Colombo, A. Modesti, and P. Musiani, “The intriguing role of polymorphonuclear neutrophils in antitumor reactions,” Blood, vol. 97, no. 2, pp. 339–345, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. H. Piccard, R. J. Muschel, and G. Opdenakker, “On the dual roles and polarized phenotypes of neutrophils in tumor development and progression,” Critical Reviews in Oncology/Hematology, vol. 82, no. 3, pp. 296–309, 2012. View at Publisher · View at Google Scholar · View at Scopus
  14. 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 Scopus
  15. T. Kudo, H. Kigoshi, T. Hagiwara, T. Takino, M. Yamazaki, and S. Yui, “Cathepsin G, a neutrophil protease, induces compact cell-cell adhesion in MCF-7 human breast cancer cells,” Mediators of Inflammation, vol. 2009, Article ID 850940, 11 pages, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. C. A. Owen and E. J. Campbell, “The cell biology of leukocyte-mediated proteolysis,” Journal of Leukocyte Biology, vol. 65, no. 2, pp. 137–150, 1999. View at Google Scholar · View at Scopus
  17. C. T. N. Pham, “Neutrophil serine proteases: specific regulators of inflammation,” Nature Reviews Immunology, vol. 6, no. 7, pp. 541–550, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. S. L. Newman, L. Gootee, J. E. Gabay, and M. E. Selsted, “Identification of constituents of human neutrophil azurophil granules that mediate fungistasis against Histoplasma capsulatum,” Infection and Immunity, vol. 68, no. 10, pp. 5668–5672, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. W. M. Shafer, F. Hubalek, M. Huang, and J. Pohl, “Bactericidal activity of a synthetic peptide (CG 117-136) of human lysosomal cathepsin G is dependent on arginine content,” Infection and Immunity, vol. 64, no. 11, pp. 4842–4845, 1996. View at Google Scholar · View at Scopus
  20. I. Hahn, A. Klaus, A.-K. Janze et al., “Cathepsin G and neutrophil elastase play critical and nonredundant roles in lung-protective immunity against Streptococcus pneumoniae in mice,” Infection and Immunity, vol. 79, no. 12, pp. 4893–4901, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. M. A. Selak and J. B. Smith, “Cathepsin G binding to human platelets. Evidence for a specific receptor,” Biochemical Journal, vol. 266, no. 1, pp. 55–62, 1990. View at Google Scholar · View at Scopus
  22. 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,” The Journal of Biological Chemistry, vol. 275, no. 10, pp. 6819–6823, 2000. View at Publisher · View at Google Scholar · View at Scopus
  23. R. Sun, P. Iribarren, N. Zhang et al., “Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor,” The Journal of Immunology, vol. 173, no. 1, pp. 428–436, 2004. View at Google Scholar · View at Scopus
  24. A. Uehara, K. Muramoto, H. Takada, and S. Sugawara, “Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2,” The Journal of Immunology, vol. 170, no. 11, pp. 5690–5696, 2003. View at Google Scholar · View at Scopus
  25. E. Glusa and C. Adam, “Endothelium-dependent relaxation induced by cathepsin G in porcine pulmonary arteries,” British Journal of Pharmacology, vol. 133, no. 3, pp. 422–428, 2001. View at Google Scholar · View at Scopus
  26. A. Sabri, S. G. Alcott, H. Elouardighi et al., “Neutrophil cathepsin G promotes detachment-induced cardiomyocyte apoptosis via a protease-activated receptor-independent mechanism,” The Journal of Biological Chemistry, vol. 278, no. 26, pp. 23944–23954, 2003. View at Publisher · View at Google Scholar · View at Scopus
  27. L. Iacoviello, V. Kolpakov, L. Salvatore et al., “Human endothelial cell damage by neutrophil-derived cathepsin G role of cytoskeleton rearrangement and matrix-bound plasminogen activator inhibitor-1,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 15, no. 11, pp. 2037–2046, 1995. View at Publisher · View at Google Scholar
  28. R. Morimoto-Kamata, S. Mizoguchi, T. Ichisugi, and S. Yui, “Cathepsin G induces cell aggregation of human breast cancer MCF-7 via a 2-step mechanism: enzymatic activity-independent binding to the cell surface and enzymatic activity-dependent induction of the cell aggregation,” Mediators of Inflammation, vol. 2012, Article ID 456462, 13 pages, 2012. View at Publisher · View at Google Scholar
  29. 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
  30. J. A. McDonald and D. G. Kelley, “Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments,” The Journal of Biological Chemistry, vol. 255, no. 18, pp. 8848–8858, 1980. View at Google Scholar · View at Scopus
  31. T. Vartio, H. Seppä, and A. Vaheri, “Susceptibility of soluble and matrix fibronectins to degradation by tissue proteinases, mast cell chymase and cathepsin G,” The Journal of Biological Chemistry, vol. 256, no. 1, pp. 471–477, 1981. View at Google Scholar · View at Scopus
  32. A. Bonnefoy and C. Legrand, “Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase,” Thrombosis Research, vol. 98, no. 4, pp. 323–332, 2000. View at Publisher · View at Google Scholar · View at Scopus
  33. P. A. Underwood and F. A. Bennett, “A comparison of the biological activities of the cell-adhesive proteins vitronectin and fibronectin,” Journal of Cell Science, vol. 93, no. 4, pp. 641–649, 1989. View at Google Scholar · View at Scopus
  34. M. Takeichi, “The cadherins: cell-cell adhesion molecules controlling animal morphogenesis,” Development, vol. 102, no. 4, pp. 639–655, 1988. View at Google Scholar · View at Scopus
  35. K. Nakajima, J. C. Powers, B. M. Ashe, and M. Zimmerman, “Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site,” The Journal of Biological Chemistry, vol. 254, no. 10, pp. 4027–4032, 1979. View at Google Scholar
  36. C. A. Owen and E. J. Campbell, “Neutrophil proteinases and matrix degradation. The cellbiology of pericellular proteolysis,” Seminars in Cell Biology, vol. 6, no. 6, pp. 367–376, 1995. View at Google Scholar · View at Scopus
  37. K. Zen, Y.-L. Guo, L.-M. Li, Z. Bian, C.-Y. Zhang, and Y. Liu, “Cleavage of the CD11b extracellular domain by the leukocyte serprocidins is critical for neutrophil detachment during chemotaxis,” Blood, vol. 117, no. 18, pp. 4885–4894, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. S. Z. Raptis, S. D. Shapiro, P. M. Simmons, A. M. Cheng, and C. T. N. Pham, “Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering,” Immunity, vol. 22, no. 6, pp. 679–691, 2005. View at Publisher · View at Google Scholar · View at Scopus