The in vivo expression of the collagenolytic matrix metalloproteinases (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in adult and localized juvenile periodontitis.

Periodontal inflammation is characterized by irreversible degradation of periodontal ligament collagen fibers leading to loss of tooth attachment. Cultured gingival keratinocytes and fibroblasts express, in vitro, various matrix metalloproteinases (MMPs) which can degrade fibrillar collagens. We hypothesized that several MMPs are also synthesized in vivo by sulcular epithelium, and analyzed the collagenolytic MMPs (MMP-2, -8, -13, and -14) and matrilysin (MMP-7) in gingival tissue specimens and gingival crevicular fluid from adult and localized juvenile periodontitis patients by in situ hybridization, immunohistochemistry, and Western immunoblotting.

Down-regulation of trypsinogen-2 expression by chemically modified tetracyclines: association with reduced cancer cell migration.

Many types of human tumor express trypsinogen-2, which may be a significant factor in the activation of pro-MMPs and the invasiveness of tumors. Prevention of trypsinogen-2 expression in cancer cells might be of benefit in cancer therapy. We describe here chemicals capable of down-regulating the expression of trypsinogen-2.

Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients.

Matrix metalloproteinases (MMPs) and serine proteinases seem to be related to tissue destruction in periodontitis. The presence of MMPs in gingival crevicular fluid (GCF) and saliva, however, has not been studied comprehensively with the enzyme-linked immunosorbent assay (ELISA)-technique. We therefore examined the levels of MMP-1, -3, -8 and -9, and their endogenous inhibitor, tissue inhibitor of matrix metalloproteinases (TIMP-1), in GCF and saliva of patients with adult periodontitis (AP) and localized juvenile periodontitis (LJP).

Cathepsin G in gingival tissue and crevicular fluid in adult periodontitis.

The presence, localization and activities of cathepsin G in gingival tissue specimens and crevicular fluid (GCF) from 9 adult periodontitis patients and 6 controls with clinically healthy periodontium were studied by use of avidinbiotin-peroxidase complex method, Western and dot blotting, and spectrophotometric activity assay. In contrast to healthy gingival tissue specimens, gingival tissue specimens collected from adult periodontitis patients contained inflammatory cells in lamina propria, beneath the oral sulcular epithelium, 10-50% of which were cathepsin G positive polymorphonuclear neutrophilic leukocytes (PMNs) and monocyte/macrophage-like cells. Cathepsin G activities were increased in adult periodontitis GCF when compared to periodontally healthy controls' GCF (p < 0.

Proteolytic enzymes as indicators of periodontal health in gingival crevicular fluid of patients with Sjögren's syndrome.

The present study characterizes the periodontal status of patients with Sjögren's syndrome (SS) and measures collagenase, elastase and gelatinase in gingival crevicular fluid (GCF) from these patients compared with adult individuals with periodontitis and healthy controls. The periodontal status was assessed by the Gingival Bleeding Index (GBI), the Visible Plaque Index (VPI), and pocket depth. Activity measurements were performed for collagenase with SDS-PAGE/laser densitometry, for elastase spectrophotometrically using a synthetic N-succinyl-Ala-Ala-Val p-nitroanilide peptide substrate, and for gelatinase with zymography.