Faculty, Staff and Student Publications

Authors

    Language

    English

    Publication Date

    4-1-2010

    Journal

    FEMS Immunology and Medical Microbiology

    DOI

    10.1111/j.1574-695X.2009.00637.x

    PMID

    20030715

    PMCID

    PMC2871062

    PubMedCentral® Posted Date

    July 2010

    PubMedCentral® Full Text Version

    Post-print

    Abstract

    Matrix metalloproteinase-9 (MMP-9) cleaves collagen, allowing leukocytes to traffic toward the vasculature and the lymphatics. When MMP-9 is unregulated by tissue inhibitor of metalloproteinase-1 (TIMP-1), this can lead to tissue destruction. Dendritic cells (DCs) infiltrate the oral mucosa increasingly in chronic periodontitis, characterized by infection with several pathogens including Porphyromonas gingivalis. In this study, human monocyte-derived DCs were pulsed with different doses of lipopolysaccharide of P. gingivalis 381 and of Escherichia coli type strain 25922, as well as whole live isogenic fimbriae-deficient mutant strains of P. gingivalis 381. Levels of induction of MMP-9 and TIMP-1, as well as interleukin-10 (IL-10), which reportedly inhibits MMP-9 induction, were measured by several approaches. Our results reveal that lipopolysaccharide of P. gingivalis, compared with lipopolysaccharide from E. coli type strain 25922, is a relatively potent inducer of MMP-9, but a weak inducer of TIMP-1, contributing to a high MMP-9/TIMP-1 ratio.Whole live P. gingivalis strain 381, major fimbriae mutant DPG-3 and double mutant MFB were potent inducers of MMP-9, but minor fimbriae mutant MFI was not. MMP-9 induction was inversely proportional to IL-10 induction. These results suggest that lipopolysaccharide and the minor and the major fimbriae of P. gingivalis may play distinct roles in induction by DCs of MMP-9, a potent mediator of local tissue destruction and leukocyte trafficking.

    Keywords

    Cells, Cultured, Dendritic Cells, Escherichia coli, Humans, Interleukin-10, Lipopolysaccharides, Matrix Metalloproteinase 9, Monocytes, Porphyromonas gingivalis, Tissue Inhibitor of Metalloproteinase-1, Up-Regulation

    Included in

    Dentistry Commons

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