RESEARCH ARTICLE
Proteolytic Activities of Oral Bacteria on ProMMP-9 and the Effect of Synthetic Proteinase Inhibitors
Guang Jie Bao1, Kirsti Kari2, Taina Tervahartiala2, Timo Sorsa2, Jukka H. Meurman2 , *
Article Information
Identifiers and Pagination:
Year: 2008Volume: 2
First Page: 96
Last Page: 102
Publisher ID: TODENTJ-2-96
DOI: 10.2174/1874210600802010096
Article History:
Received Date: 14/1/2008Revision Received Date: 5/6/2008
Acceptance Date: 5/6/2008
Electronic publication date: 9/7/2008
Collection year: 2008
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
Tissue reactions to bacteria lead to proinflammatory reactions involving matrix metalloproteinases (MMPs). Synthetic protease inhibitors may offer new possibilities to regulate bacterial proteases. We investigated proteolytic activities of certain periodontal bacteria, their effects on the latent proMMP-9, and the effects of synthetic MMP inhibitors and a serine protease inhibitor Pefabloc. The strains studied were Porphyromonas gingivalis, Prevotella intermedia, Peptostreptoccus micros, Prevotella nigrescens, Fusobacterium nucleatum, and 5 Aggregatibacter actinomycetemcomitans serotypes. Their gelatinolytic activities and the effects of certain synthetic MMP inhibitors and Pefabloc were analyzed by zymography. Bacterial effects on proMMP-9 conversion were investigated by Western immunoblot. All investigated periodontal bacteria produced gelatinolytic cell-bound and extracellular proteinases which could fragment latent proMMP-9, suggesting co-operative processing cascades in oral tissue remodeling. A. actinomycetemcomitans produced the weakest gelatinolytic activity. Synthetic proteinase inhibitors exhibited slight but clear reductive effects on the bacterial proteolytic activities. We conclude that targeted anti-proteolytic treatment modalities against bacterial-host proteolytic cascades can be developed.
