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BioMed Research International
Volume 2014 (2014), Article ID 420830, 7 pages
http://dx.doi.org/10.1155/2014/420830
Research Article

Are Proteinase 3 and Cathepsin C Enzymes Related to Pathogenesis of Periodontitis?

1Department of Periodontology, School of Dentistry, Ege University, 35100 Izmir, Turkey
2Department of Pediatric Immunology, School of Medicine, Ege University, 35100 Izmir, Turkey

Received 13 February 2014; Accepted 15 April 2014; Published 19 May 2014

Academic Editor: Georgios E. Romanos

Copyright © 2014 Oya Türkoğlu 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. D. F. Kinane, D. R. Demuth, S. Gorr, G. N. Hajishengallis, and M. H. Martin, “Human variability in innate immunity,” Periodontology 2000, vol. 45, no. 1, pp. 14–34, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. B. A. Dale and L. P. Fredericks, “Antimicrobial peptides in the oral environment: expression and function in health and disease,” Current Issues in Molecular Biology, vol. 7, no. 2, pp. 119–133, 2005. View at Google Scholar · View at Scopus
  3. S. Ji, J. Hyun, E. Park, B. L. Lee, K. K. Kim, and Y. Choi, “Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils,” Journal of Periodontal Research, vol. 42, no. 5, pp. 410–419, 2007. View at Publisher · View at Google Scholar · View at Scopus
  4. G. Nussbaum and L. Shapira, “How has neutrophil research improved our understanding of periodontal pathogenesis?” Journal of Clinical Periodontology, vol. 38, no. 11, pp. 49–59, 2011. View at Publisher · View at Google Scholar · View at Scopus
  5. H. Hasturk, A. Kantarci, and T. E. van Dyke, “Oral inflammatory diseases and systemic inflammation: role of the macrophage,” Frontiers in Immunology, vol. 3, article 118, 2012. View at Publisher · View at Google Scholar
  6. Y. Zheng, F. Niyonsaba, H. Ushio et al., “Cathelicidin LL-37 induces the generation of reactive oxygen species and release of human α-defensins from neutrophils,” The British Journal of Dermatology, vol. 157, no. 6, pp. 1124–1131, 2007. View at Publisher · View at Google Scholar · View at Scopus
  7. R. Bals and J. M. Wilson, “Cathelicidins—a family of multifunctional antimicrobial peptides,” Cellular and Molecular Life Sciences, vol. 60, no. 4, pp. 711–720, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. O. E. Sørensen, P. Follin, A. H. Johnsen et al., “Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3,” Blood, vol. 97, no. 12, pp. 3951–3959, 2001. View at Publisher · View at Google Scholar · View at Scopus
  9. R. C. Kao, N. G. Wehner, K. M. Skubitz, B. H. Gray, and J. R. Hoidal, “Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters,” Journal of Clinical Investigation, vol. 82, no. 6, pp. 1963–1973, 1988. View at Google Scholar · View at Scopus
  10. E. J. Campbell, M. A. Campbell, and C. A. Owen, “Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition,” Journal of Immunology, vol. 165, no. 6, pp. 3366–3374, 2000. View at Google Scholar · View at Scopus
  11. N. V. Rao, N. G. Wehner, B. C. Marshall, W. R. Gray, B. H. Gray, and J. R. Hoidal, “Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase: structural and functional properties,” The Journal of Biological Chemistry, vol. 266, no. 15, pp. 9540–9548, 1991. View at Google Scholar · View at Scopus
  12. P. Renesto, L. Halbwachs-Mecarelli, P. Nusbaum, P. Lesavre, and M. Chignard, “Proteinase 3: a neutrophil proteinase with activity on platelets,” Journal of Immunology, vol. 152, no. 9, pp. 4612–4617, 1994. View at Google Scholar · View at Scopus
  13. J. J. Yang, R. Kettriz, R. J. Falk, J. C. Jennette, and M. L. Gaido, “Apoptosis of endothelial cells induced by the neutrophil serine proteases proteinase 3 and elastase,” The American Journal of Pathology, vol. 149, no. 5, pp. 1617–1626, 1996. View at Google Scholar
  14. C. Coeshott, C. Ohnemus, A. Pilyavskaya et al., “Converting enzyme-independent release of tumor necrosis factor α and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 11, pp. 6261–6266, 1999. View at Google Scholar · View at Scopus
  15. B. Korkmaz, T. Moreau, and F. Gauthier, “Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions,” Biochimie, vol. 90, no. 2, pp. 227–242, 2008. View at Publisher · View at Google Scholar · View at Scopus
  16. C. T. N. Pham, “Neutrophil serine proteases fine-tune the inflammatory response,” International Journal of Biochemistry and Cell Biology, vol. 40, no. 6-7, pp. 1317–1333, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Sugawara, A. Uehara, T. Nochi et al., “Neutrophil proteinase 3-mediated induction of bioactive IL-18 secretion by human oral epithelial cells,” Journal of Immunology, vol. 167, no. 11, pp. 6568–6575, 2001. View at Google Scholar · View at Scopus
  18. G. H. Nuckolls and H. C. Slavkin, “Paths of glorious proteases,” Nature Genetics, vol. 23, no. 4, pp. 378–380, 1999. View at Publisher · View at Google Scholar · View at Scopus
  19. S. F. de Haar, D. C. Jansen, T. Schoenmaker, H. de Vree, V. Everts, and W. Beertsen, “Loss-of-function mutations in cathepsin C in two families with Papillon-Lefèvre syndrome are associated with deficiency of serine proteinases in PMNs,” Human Mutation, vol. 23, no. 5, p. 524, 2004. View at Google Scholar · View at Scopus
  20. C. T. N. Pham and T. J. Ley, “Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 15, pp. 8627–8632, 1999. View at Publisher · View at Google Scholar · View at Scopus
  21. C. T. N. Pham, J. L. Ivanovich, S. Z. Raptis, B. Zehnbauer, and T. J. Ley, “Papillon-Lefèvre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans,” Journal of Immunology, vol. 173, no. 12, pp. 7277–7281, 2004. View at Google Scholar · View at Scopus
  22. S. F. de Haar, P. S. Hiemstra, M. T. J. M. van Steenbergen, V. Everts, and W. Beertsen, “Role of polymorphonuclear leukocyte-derived serine proteinases in defense against Actinobacillus actinomycetemcomitans,” Infection and Immunity, vol. 74, no. 9, pp. 5284–5291, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. T. Lundgren, R. S. Parhar, S. Renvert, and D. N. Tatakis, “Impaired cytotoxicity in Papillon-Lefèvre syndrome,” Journal of Dental Research, vol. 84, no. 5, pp. 414–417, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. J. L. Meade, E. A. de Wynter, P. Brett et al., “A family with Papillon-Lefèvre syndrome reveals a requirement for cathepsin C in granzyme B activation and NK cell cytolytic activity,” Blood, vol. 107, no. 9, pp. 3665–3668, 2006. View at Publisher · View at Google Scholar · View at Scopus
  25. P. S. Hart, Y. Zhang, E. Firatli et al., “Identification of cathepsin C mutations in ethnically diverse Papillon-Lefèvre syndrome patients,” Journal of Medical Genetics, vol. 37, no. 12, pp. 927–932, 2000. View at Google Scholar · View at Scopus
  26. C. Hewitt, D. McCormick, G. Linde et al., “The role of cathepsin C in Papillon-Lefèvre syndrome, prepubertal periodontitis, and aggressive periodontitis,” Human Mutation, vol. 23, no. 3, pp. 222–228, 2004. View at Publisher · View at Google Scholar
  27. B. Noack, H. Görgens, T. Hoffmann et al., “Novel mutations in the cathepsin C gene in patients with pre-pubertal aggressive periodontitis and Papillon-Lefèvre syndrome,” Journal of Dental Research, vol. 83, no. 5, pp. 368–370, 2004. View at Google Scholar · View at Scopus
  28. B. Noack, H. Görgens, U. Hempel et al., “Cathepsin C gene variants in aggressive periodontitis,” Journal of Dental Research, vol. 87, no. 10, pp. 958–963, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. M. Soell, R. Elkaim, and H. Tenenbaum, “Cathepsin C, matrix metalloproteinases, and their tissue inhibitors in gingiva and gingival crevicular fluid from periodontitis-affected patients,” Journal of Dental Research, vol. 81, no. 3, pp. 174–178, 2002. View at Google Scholar · View at Scopus
  30. K. Komine, T. Kuroishi, A. Ozawa et al., “Cleaved inflammatory lactoferrin peptides in parotid saliva of periodontitis patients,” Molecular Immunology, vol. 44, no. 7, pp. 1498–1508, 2007. View at Publisher · View at Google Scholar · View at Scopus
  31. O. Laugisch, M. Schacht, A. Guentsch et al., “Periodontal pathogens affect the level of protease inhibitors in gingival crevicular fluid,” Molecular Oral Microbiology, vol. 27, no. 1, pp. 45–56, 2012. View at Publisher · View at Google Scholar · View at Scopus
  32. O. Türkoǧlu, A. Berdeli, G. Emingil, and G. Atilla, “A novel p.S34N mutation of CAMP gene in patients with periodontal disease,” Archives of Oral Biology, vol. 56, no. 6, pp. 573–579, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. O. Türkoǧlu, G. Kandiloǧlu, A. Berdeli, G. Emingil, and G. Atilla, “Antimicrobial peptide hCAP-18/LL-37 protein and mRNA expressions in different periodontal diseases,” Oral Diseases, vol. 17, no. 1, pp. 60–67, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. G. A. Quigley and J. W. Hein, “Comparative cleansing efficiency of manual and power brushing,” Journal of the American Dental Association, vol. 65, pp. 26–29, 1962. View at Google Scholar · View at Scopus
  35. J. Ainamo and I. Bay, “Problems and proposals for recording gingivitis and plaque,” International Dental Journal, vol. 25, no. 4, pp. 229–235, 1975. View at Google Scholar · View at Scopus
  36. U. P. Saxer and H. R. Mühlemann, “Motivation and education,” Schweizerische Monatsschrift für Zahnheilkunde, vol. 85, no. 9, pp. 905–919, 1975. View at Google Scholar · View at Scopus
  37. G. C. Armitage, “Development of a classification system for periodontal diseases and conditions,” Annals of Periodontology, vol. 4, no. 1, pp. 1–6, 1999. View at Google Scholar · View at Scopus
  38. S. D. Kobayashi, K. R. Braughton, A. R. Whitney et al., “Bacterial pathogens modulate an apoptosis differentiation program in human neutrophils,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 19, pp. 10948–10953, 2003. View at Publisher · View at Google Scholar · View at Scopus
  39. B. G. Loos, U. van der Velden, and M. L. Laine, “Susceptibility,” in Clinical Periodontology and Implant Dentistry, J. Lindhe, N. P. Lang, and T. Karring, Eds., vol. 1, pp. 328–346, Blackwell Publishing, Singapore, 2008. View at Google Scholar
  40. H. J. Wright, J. B. Matthews, I. L. C. Chapple, N. Ling-Mountford, and P. R. Cooper, “Periodontitis associates with a type 1 IFN signature in peripheral blood neutrophils,” Journal of Immunology, vol. 181, no. 8, pp. 5775–5784, 2008. View at Google Scholar · View at Scopus
  41. I. H. K. Dias, J. B. Matthews, I. L. C. Chapple, H. J. Wright, C. R. Dunston, and H. R. Griffiths, “Activation of the neutrophil respiratory burst by plasma from periodontitis patients is mediated by pro-inflammatory cytokines,” Journal of Clinical Periodontology, vol. 38, no. 1, pp. 1–7, 2011. View at Publisher · View at Google Scholar · View at Scopus
  42. M. Holzhausen, J. R. Cortelli, V. A. da Silva, G. C. N. Franco, S. C. Cortelli, and N. Vergnolle, “Protease-activated receptor-2 (PAR2) in human periodontitis,” Journal of Dental Research, vol. 89, no. 9, pp. 948–953, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. S. S. Socransky, A. D. Haffajee, M. A. Cugini, C. Smith, and R. L. Kent Jr., “Microbial complexes in subgingival plaque,” Journal of Clinical Periodontology, vol. 25, no. 2, pp. 134–144, 1998. View at Google Scholar · View at Scopus
  44. L. Yin, B. Swanson, J. An et al., “Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2,” Journal of Oral Microbiology, vol. 2, article 5070, 2010. View at Publisher · View at Google Scholar
  45. P. M. M. Marsh, Oral Microbiology, Chapman & Hall, New York, NY, USA, 1992.
  46. R. Claesson, E. Johansson, and J. Carlsson, “Oxygen-dependent modulation of release and activity of polymorphonuclear leukocyte granule products,” Oral Microbiology and Immunology, vol. 9, no. 2, pp. 81–87, 1994. View at Google Scholar · View at Scopus
  47. G. L. Mandell, “Bactericidal activity of aerobic and anaerobic polymorphonuclear neutrophils,” Infection and Immunity, vol. 9, no. 2, pp. 337–341, 1974. View at Google Scholar · View at Scopus
  48. O. Türkoğlu, G. Emingil, N. Kütükçüler, and G. Atilla, “Evaluation of gingival crevicular fluid adrenomedullin and human neutrophil peptide 1–3 levels of patients with different periodontal diseases,” Journal of Periodontology, vol. 81, no. 2, pp. 284–291, 2010. View at Publisher · View at Google Scholar
  49. O. Türkoğlu, G. Emingil, N. Kütükçüler, and G. Atilla, “Gingival crevicular fluid levels of cathelicidin LL-37 and interleukin-18 in patients with chronic periodontitis,” Journal of Periodontology, vol. 80, no. 6, pp. 969–976, 2009. View at Publisher · View at Google Scholar
  50. Y. Abiko, M. Nishimura, and T. Kaku, “Defensins in saliva and the salivary glands,” Medical Electron Microscopy, vol. 36, no. 4, pp. 247–252, 2003. View at Publisher · View at Google Scholar · View at Scopus