Journal of Periodontal and Implant Science

Korean Academy of Periodontology (대한치주과학회)
권호 표지

Stromelysin-1 and Membrane type-MMP-1 Expressions in Human Chronic Periodontitis with Type 2 Diabetes Mellitus

단순 만성 치주염 환자와 제 2형 당뇨병을 동반한 만성 치주염 환자에서 Stromelysin-1와 Membrane type-MMP-1 Expressions

  • Ryu, Sang-Ho (Department of Periodontology, School of Dentistry, Kyungpook National University) ;
  • Park, Jin-Woo (Department of Periodontology, School of Dentistry, Kyungpook National University) ;
  • Suh, Jo-Young (Department of Periodontology, School of Dentistry, Kyungpook National University) ;
  • Lee, Jae-Mok (Department of Periodontology, School of Dentistry, Kyungpook National University)
  • 류상호 (경북대학교 치의학전문대학원 치주과학교실) ;
  • 박진우 (경북대학교 치의학전문대학원 치주과학교실) ;
  • 서조영 (경북대학교 치의학전문대학원 치주과학교실) ;
  • 이재목 (경북대학교 치의학전문대학원 치주과학교실)
  • Published : 2008.12.31
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Abstract

Purpose: The purposes of this study were to compare and quantify the expression of Stromelysin-1 and MT-MMP-1 in the gingival tissues of patients with type 2 diabetes mellitus(DM) and healthy adults with chronic periodontitis. Materials and Methods: Gingival tissue samples were obtained during periodontal surgery or tooth extraction. According to the patient's systemic condition & clinical criteria of gingiva, each gingival sample was devided into three groups. Group 1 (n=8) is clinically healthy gingiva without bleeding and no evidence of bone resorption or periodontal pockets, obtained from systemically healthy 8 patients. Group 2 (n=8) is inflammed gingiva from patients with chronic periodontitis. Group 3 (n=8) is inflammed gingiva from patients with chronic periodontitis associated with type 2 DM. Tissue samples were prepared and analyzed by Western blotting. The quantification of Stromelysin-1 and MT-MMP-1 were performed using a densitometer and statistically analyzed by one-way ANOVA followed by Tukey test. Results: In the analysis of expression levels, Stromelysin-1 and MT-MMP-1 expressions were similar in group 1 and 2. Stromelysin-1 and MT-MMP-1 expressions was more increased in group 3 than group 1, 2. The difference between group 3 and group 1, 2 was statistically significant. Also, in the interrelationship of Stromelysin-1 and MT-MMP-1 expressions, expressions of Stromelysin-1 and MT-MMP-1 showed increasing tendency in chronic periodontitis associated with type 2 DM and it seems that the MT-MMP-1 expressions were increasing in proportion to Stromelysin-1 expressions. Conclusion: It is suggested that Stromelysin-1 and MT-MMP-1 may be partly involved in the progression of periodontal inflammation associated with type 2 DM, as related to a metabolism of other factors, such as AGE, plasmin and other inflammatory mediators. Therefore, the expression levels of Stromelysin-1 and MT-MMP-1 can be inflammatory markers of periodontal inflammed tissue with type 2 DM.

Keywords

References

  1. Reynolds, J. J. Collagenases and tissue inhibitors of metalloproteinases : a functional balance in tissue degradation. Oral Diseases 1995;2:70-76 https://doi.org/10.1111/j.1601-0825.1996.tb00206.x
  2. M. S. Kumar, G. Vamsi, R. Sripriya, and P. K. Sehgal. Expression of matrix metalloproteinases(MMP-8 and -9) in chronic periodontitis patients with and without diabetes mellitus. J Periodontol 2006;77:1803-1808 https://doi.org/10.1902/jop.2006.050293
  3. Werb, Z. ECM and cell surface proteolysis : regulating cellular ecology. Cell 1997;91:439-442 https://doi.org/10.1016/S0092-8674(00)80429-8
  4. Domeij, H., Yucel-Lindberg, T. & Modeer, T. Signal pathways involved in the production of MMP-1 and Stromelysin-1 in human gingival fibroblasts. European Journal of Oral Science 2002;110:302-306 https://doi.org/10.1034/j.1600-0722.2002.21247.x
  5. Nakaya H., Oates, T. W., Hoang, A. M., Kamoi, K. & Cochran, D. L. Effects of IL-1 beta on matrix metalloproteinase 3 levels in human periodontal ligament cells. J Periodontol 1997;68:517-523 https://doi.org/10.1902/jop.1997.68.6.517
  6. Sorsa, T., Suomalainen, K. & Uitto, V. J. The role of gingival crevicular fluid and salivary interstitial collagenases in human periodontal diseases. Archives of Oral Biology 1990;35:193-196 https://doi.org/10.1016/0003-9969(90)90156-5
  7. H. Sato, T. Takino, Y. Okada et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994;370:61-65 https://doi.org/10.1038/370061a0
  8. M. Seiki. The cell surface: the stage for matrix metalloproteinase regulation of migration. Curr. Opin. Cell Biol. 2002;14:624-632 https://doi.org/10.1016/S0955-0674(02)00363-0
  9. R. Achong, I Nishimura, H. Ramachandran et al. Membrane Type(MT)1-matrix metalloproteinase(MMP) and MMP-2 expression in ligature-induced periodontitis in the rat. J Periodontol 2003;74:494-500 https://doi.org/10.1902/jop.2003.74.4.494
  10. Thorstensson H, Kuylenstiern J, Hugoson A. Medical status and complications in relation to periodontal disease experience in insulin-dependent diabetics. J Clin Periodontol 1996;23:194-202 https://doi.org/10.1111/j.1600-051X.1996.tb02076.x
  11. Terranova A. The effects of diabetes mellitus on wound healing. Plast Surg Nurs 1991;11:20-25 https://doi.org/10.1097/00006527-199121000-00006
  12. Grossi SG, Genco RJ. Periodontal disease and diabetes mellitus: A two-way relationship. Ann periodontol 1998;3: 51-61 https://doi.org/10.1902/annals.1998.3.1.51
  13. Bissada NF, Manouchehr-Pour M, Haddow M, Spagnuolo PJ. Neutrophil functional activity in juvenile and adult onset diabetic patients with mild and severe periodontitis. J Periodont Res 1982;17:500-502 https://doi.org/10.1111/j.1600-0765.1982.tb02038.x
  14. Amitage GC. Development of a classification system for periodontal diseases and conditions. Ann Periodontol 1999;4:1-6 https://doi.org/10.1902/annals.1999.4.1.1
  15. Muhlemann HR and Son S. Gingival sulcus bleeding a leading symptom in initial gingivitis. Helv Odontol Acta 1971;15:107
  16. Park HK and Lee JM. Interrelationship of matrix metalloproteinase-13 and elastase expression in human gingiva with chronic periodontitis associated to type 2 diabetes mellitus. Journal of Korean Academy of Periodontology. 2006;36:397-408 https://doi.org/10.5051/jkape.2006.36.2.397
  17. Cho JY, Xing S, Liu X et al. Expression and activity of human Na+/I-symporter in human glioma cells by adenovirus-mediateed gene delivery. Gene Therapy 2000;7: 740-749
  18. Portik-Dobos V, Anstadt MP, Hutchinson J, Bannan M and Ergul A. Evidence for a matrix metalloproteinase induction/activation system in arterial vasculature and decreased synthesis and activity in diabetes. Diabetes 2002;51:3063-3068 https://doi.org/10.2337/diabetes.51.10.3063
  19. Taylor GW, Burt BA, Becker MP et al. Non-insulin dependent diabetes mellitus and alveolar bone loss progression over 2 years. J Periodontol 1998;69:76-83 https://doi.org/10.1902/jop.1998.69.1.76
  20. The Diabetes Control and Complications Trial Research Group. The effect of intensive treatment of diabetes on the development and progression of long-term complication in insulin-dependent diabetes mellitus. N Engl J Med 1993;329:977-986 https://doi.org/10.1056/NEJM199309303291401
  21. Sara G., Grossi, Robert J. Genco, Periodontal disease and diabetes mellitus: A two-way relationship. Ann Periodontol 1998;3:51-61 https://doi.org/10.1902/annals.1998.3.1.51
  22. Wassenaar A., Verschoor T., Kievits F. et al. CD40 engagement modulates the production of matrix metalloproteinases by gingival fibroblasts. Clin Exp Immunol 1999;115:161-167 https://doi.org/10.1046/j.1365-2249.1999.00764.x
  23. Tervahartiala T, Konttinen YT, Ingman T. et al. Cathepsin G in gingival tissue and crevicular fluid in adult periodontitis. J Clin Periodontol 1996;23:68-75 https://doi.org/10.1111/j.1600-051X.1996.tb00537.x
  24. Jenne DE. Structure of the azurocidin, proteinase 3, and neutrophil elastase genes. Implications for inflammation and vasculitis. Am J Respir Crit Care Med 1994;150(6 Pt 2):s147-s154 https://doi.org/10.1164/ajrccm/150.6_Pt_2.S147
  25. Weiss SJ. Tissue destruction by neutrophils. N Engl J Med 1989;320:365-376 https://doi.org/10.1056/NEJM198902093200606
  26. A. Beklen, G. Tuter, T. Sorsa et al. Gingival tissue and crevicular fluid co-operation in adult periodontitis. J Dent Res 2006;85(1):59-63 https://doi.org/10.1177/154405910608500110
  27. Trengove NJ. Stacey MC. MacAuley S et al. Analysis of the acute and chronic wound environments: the role of proteases and the inhibitors. Wound Repair Regeneration 1999;7:442-52 https://doi.org/10.1046/j.1524-475X.1999.00442.x
  28. Ohuchi E, Imai K, Fujii Y. et al. Membrane type-1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 1997;272: 2446-2451 https://doi.org/10.1074/jbc.272.4.2446
  29. von Bredow DC, Cress AE, Howard EW, Bowden GT, Nagle RB. Activation of gelatinase-tissue-inhibitors-of- metalloproteinase complexes by matrilysin. Biochem J 1998;331(Pt 3):965-972 https://doi.org/10.1042/bj3310965
  30. B. Arza, M.F. Hoylaerts, J. Felez, D. Collen, H. R. Lijnen. Prostromelysin-1 (proStromelysin-1) stimulates plasminogen activation by tissue-type plasminogen activator. Eur J Biochem 2000;267:6378-6384 https://doi.org/10.1046/j.1432-1327.2000.01732.x
  31. Y. Okumura, H. Sato, M. Seiki, H. Kido. Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin: A possible cell surface activator. FEBS Letters 1997;402:181-184 https://doi.org/10.1016/S0014-5793(96)01523-2
  32. S. Monea, K. Lehti, J. Keski-oja, P. Mignatti. Plasmin activates pro-matrix metalloproteinase-2 with a membrane-type 1 matrix metalloproteinase-dependent mechanism. J cell physiol 2002;192:160-170 https://doi.org/10.1002/jcp.10126