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Membrane Components of Treponema denticola Trigger Proteinase Release from Human Polymorphonuclear Leukocytes

Departments of lPeriodontology, University of Helsinki, Finland

V.-J. Uitto

Oral Biology, University of British Columbia, 2199 Wesbrook Mall, Vancouver, BC, V6T 1Z3, Canada

M. Haapasalo

Department of Cariology, Institute of Dentistry, University of Oslo, Norway

K. Lounatmaa

Department of Electron Microscopy, University of Helsinki

Y.T. Konttinen

Fourth Department of Medicine, University Central Hospital, Helsinki, Finland

T. Salo

Department of Oral Surgery and Pathology, University of Oulu, Finland

D. Grenier

Groupe de Recherche en Ecologie Buccale, Universite Laval, Quebec, Canada

T. Sorsa

Departments of lPeriodontology, University of Helsinki, Finland

Tissue destruction during periodontitis is believed to be primarily brought about by leukocyte proteinases. We postulate that oral spirochetes cause discharge of polymorphonuclear leukocyte (PMN) lysosomal enzymes. Effects of Treponema denticola 53-kDa outer membrane protein, lipopolysaccharide (LPS), and peptidoglycan on degranulation of matrix metalloproteinases (MMP)-8 (collagenase) and -9 (gelatinase), cathepsin G, and elastase by human peripheral blood PMNs were studied by specific enzyme assays and Western blot analysis. T. denticola 53-kDa outer membrane protein was found to be a particularly efficient inducer of MMP-8 release. The induction was comparable with that of phorbol myristate acetate, a known inducer of PMN specific granule discharge. All of the treponemal substances, most notably the 53-kDa protein and LPS, induced release of MMP-9, a component of C-type granules. Both collagenase and gelatinase released from PMNs were mostly in active forms. Release of cathepsin G and elastase was also observed with the 53-kDa protein treatment. The other T. denticola substances did not induce release of these serine proteinases. Lactate dehydrogenase was not released from PMNs by the treatments, indicating that the degranulation was specific and not caused by toxic effects of the substances. This was confirmed by transmission electron microscopy of PMNs treated with the 53-kDa protein that showed rapid vacuole formation and cell shape changes but no disintegration of the cells. Thus, T. denticola may participate in the PMN-dependent extracellular matrix degradation during the course of periodontal inflammation by triggering the secretion and activation of matrix metalloproteinases.

Key Words: Treponema denticola, neutrophils • degranulation • proteinases • matrix metalloproteinases • periodontitis

Journal of Dental Research, Vol. 75, No. 12, 1986-1993 (1996)
DOI: 10.1177/00220345960750121101


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