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RESEARCH REPORT |
1 Department of Biological and Medical Sciences, Faculty of Dentistry, University of British Columbia, 2199 Wesbrook mall, Vancouver, BC, V6T 1Z3, Canada;
2 Department of Oral and Maxillofacial Diseases, Surgical Hospital, HUCH, Helsinki, Finland;
3 Turku Centre for Biomaterials, University of Turku, FIN-20520, Turku, Finland;
4 National Public Health Institute, Anaerobe Reference Laboratory, FIN-00300 Finland; and
5 Department of Dermatology, Helsinki University Central Hospital, Meilahdentie 2, FIN-00250 Helsinki, Finland;
*corresponding author, jukka.uitto{at}helsinki.fi
Matrilysin is a matrix metalloproteinase expressed in exocrine and mucosal epithelium in many human tissues. Immunohistochemical staining showed that matrilysin is expressed in suprabasal cells of junctional epithelium facing the teeth and in epithelial cell rests of Malassez. No matrilysin expression was seen in the periodontal pocket tissue. In a tissue culture model mimicking junctional epithelium, matrilysin expression was also observed in suprabasal epithelial cells. Of 13 anaerobic oral bacterial species tested, F. nucleatum, F. necrophorum, P. endodontalis, and P. denticola stimulated matrilysin expression in porcine periodontal ligament epithelial cells from 2.5- to 5.7-fold, compared with untreated cells. The enzyme was localized in intracytoplasmic vesicles that also reacted with antibodies against lysosomal membrane protein h-lamp-1. The results indicate that matrilysin may play an important role in the normal physiology of junctional epithelium.
KEY WORDS: matrilysin matrix metalloproteinase human gingiva epithelial cell Fusobacterium spp. lysosomal membrane protein-1
-defensin
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