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Gingival crevicular stromelysin, collagenase and tissue inhibitor of metalloproteinases levels in healthy and diseased sites
Author(s) -
Haerian A.,
Adonogianaki E.,
Mooney J.,
Docherty J. P.,
Kinane D. F.
Publication year - 1995
Publication title -
journal of clinical periodontology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.456
H-Index - 151
eISSN - 1600-051X
pISSN - 0303-6979
DOI - 10.1111/j.1600-051x.1995.tb00797.x
Subject(s) - collagenase , matrix metalloproteinase , periodontitis , gingivitis , extracellular matrix , tissue inhibitor of metalloproteinase , extracellular , bleeding on probing , interstitial collagenase , chemistry , medicine , biology , pathology , enzyme , dentistry , biochemistry
. The ability of stromelysin (SL). fibroblast‐type collagenase (FIB‐CL) and tissue inhibitor of metalloproteinases (TIMP). to differentiate between healthy, gingivitis and periodontitis sites was investigated. SL and FIB‐CL are members of a family of enzymes which are capable of degrading most of the extracellular matrix macromolecules. Extracellular control of these enzymes is performed by TIMR 40 patients each provided 3 GCF samples from healthy, gingivitis and periodontitis sites. GCF samples were collected by means of sterile paper strips. GCF samples were eluted into 500 /A of assay buffer and assays for SL, FIB‐CL and TIMP were performed by a sandwich EL1SA. The mean amounts of SL and TIMP in diseased sites (gingivitis and periodontitis) were significantly higher than the mean amount of these GCF components in healthy sites (MANOVA p values were: 0.006 for SL and 0.001 for TIMP). GCF SL and TIMP differentiated healthy from diseased sites. Both SL and TIMP showed moderate correlation with clinical indices. FIB‐CL was detectable in only 20.8/o of all sites and did not correlate with disease status.