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RESEARCH REPORT |
1 Department of Medicine/Invärtes medicin, Helsinki University Hospital, Biomedicum Helsinki, PO Box 700 (Haartmaninkatu 8), FIN-00029 HUS, Helsinki, Finland;
2 Institute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland;
3 Medico-social, Dental Clinic, Bogazici University, Istanbul, Turkey;
4 Department of Oral and Maxillofacial Diseases, HUCH, Institute of Dentistry, University of Helsinki, Box 41 FIN-00014 Helsinki, Finland;
5 University of Gazi, Faculty of Dentistry, Department of Periodontology, Ankara, Turkey;
6 TNO-Prevention and Health, Leiden, The Netherlands;
7 ORTON Orthopaedic Hospital of the Invalid Foundation, Helsinki, Finland; and
8 COXA Hospital for Joint Replacement, Tampere, Finland
* corresponding author, yrjo.konttinen{at}helsinki.fi
Activated matrix metalloproteinase-3 (MMP-3) can contribute to periodontal ligament destruction in adult periodontitis. Since MMP-3 has been reported to activate proMMP-8 and -9, it was speculated that gingival tissue fibroblast-derived MMP-3 might, in periodontitis, be responsible for activation of gingival crevicular fluid (GCF) neutrophil-derived proMMP-8 and -9. Immunohistochemistry disclosed MMP-3 in gingival fibroblasts in periodontitis. Cultured gingival fibroblasts released only pro-MMP-3 when stimulated with tumor necrosis factor-
. However, Western blot revealed partially activated MMP-3, MMP-8, and MMP-9 in periodontitis GCF. Active MMP-8 (p < 0.05) and MMP-9 (p < 0.05) correlated with the presence of active MMP-3. It seems that resident gingival fibroblasts produce pro-MMP-3 in GCF, where it becomes activated, probably by cathepsin G or elastase released by neutrophils. Active MMP-3 then activates neutrophil-derived pro-MMP-8 and -9. Different tissue compartments/cells exert co-operative actions in mutual local MMP activation cascades.
KEY WORDS: stromelysin collagenase gelatinase periodontitis
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