Open AccessInactivation of tissue inhibitor of metalloproteinases‐1 (TIMP‐1) by Porphyromonas gingivalis
Author(s) -
Grenier Daniel,
Mayrand Denis
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10835.x
Subject(s) - porphyromonas gingivalis , matrix metalloproteinase , chemistry , microbiology and biotechnology , metalloproteinase , proteolytic enzymes , inflammation , tissue inhibitor of metalloproteinase , periodontal pathogen , proteolysis , biology , bacteria , biochemistry , enzyme , immunology , genetics
In response to periodontal inflammation, host cells release matrix metalloproteinases (MMPs) that contribute to periodontal tissue breakdown unless the tissue inhibitors of metalloproteinases (TIMPs) neutralize their activity. In this study, the capacity of Porphyromonas gingivalis to inactivate TIMP‐1 was investigated. Proteolytic digestion of TIMP‐1 was monitored by SDS–PAGE and Western immunoblotting. Planktonic cells and biofilms of P. gingivalis degraded TIMP‐1 with production of several lower molecular mass fragments. Incorporation of human serum in the assay mixture had no effect on the degradation of TIMP‐1 by P. gingivalis , whereas a cysteine proteinase inhibitor caused a complete inhibition. Using a fluorogenic assay, it was found that TIMP‐1 treated with P. gingivalis lost its capacity to inhibit MMP‐9 activity. This study revealed the potential of P. gingivalis to inactivate TIMP‐1 through proteolytic degradation. This phenomenon may contribute to increasing significantly the level of active MMPs in affected periodontal sites and subsequently favor tissue destruction.