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Matrix metalloproteinases in periodontal tissue remodelling.

Matrix metalloproteinases in periodontal tissue remodelling. Research Abstract Details 

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  • Matrix metalloproteinases in periodontal tissue remodelling. Abstract Text:

    Inflammation of the periodontium leads to connective tissue degradation and eventual tooth loss. The regulation of matrix metalloproteinases (MMPs) has been studied to determine their role in these processes and also during tissue remodelling. Analysis of gingival crevicular fluid has revealed the presence of collagenase and gelatinase that, in the acute stages of periodontal disease, are derived predominantly from polymorphonuclear leukocytes. These MMPs appear to be intimately associated with tissue destruction since the levels of the active forms of these enzymes obtained from either crevicular fluid or mouthrinse samples correlate with tissue destruction and, therefore, provide a sensitive means of demonstrating disease activity. Transforming growth factor-beta, an important regulator of connective tissue remodelling, has been implicated in the rapid remodelling of periodontal tissues. TGF-beta promotes tissue matrix formation by stimulating both the synthesis of matrix proteins (collagen, fibronectin and SPARC) and proteinase inhibitors (TIMP, PAI-1) and by decreasing the synthesis of MMPs, but not the 72 kDa-gelatinase. Nuclear run-on analyses have shown that TGF-beta reduces collagenase and stromelysin synthesis by suppressing gene transcription without altering mRNA stabilities. In contrast, the transcription of the gelatinase and TIMP genes was increased by TGF-beta, which also increased gelatinase mRNA stability. Remodelling of alveolar bone involves interaction between osteoblasts and osteoclasts. Osteoblasts, under the influence of osteotropic hormones (vit D3, PTH and retinoic acid), produce MMPs which appear to function in the removal of soft tissue that precludes access of osteoclasts to the mineralized tissue surface. Rat osteoblastic cells produce MMPs with activity on native collagen, native collagen 3/4-fragments and gelatin and, in addition, two forms of TIMP activity. The 3/4-collagen endopeptidase, purified to apparent homogeneity, also has significant collagenase and gelatinase activities and an amino terminal sequence almost identical to human 72 kDa-gelatinase. The production of this enzyme was stimulated by TGF-beta, which suppresses bone resorption, and by osteotropic hormones which stimulate bone resorption, supporting a bifunctional role for the gelatinase in connective tissue remodelling. Although there is strong evidence for the involvement of MMPs in the resorption of bone and in the inflammation-mediated destruction of periodontal tissues, the role of MMPs in the remodelling of mature soft connective tissues remains equivocal.

    Matrix metalloproteinases in periodontal tissue remodelling. Publishing Authors By Initials

    For similar peptides: intercellular signaling peptides and proteins: cytokines: transforming growth factor beta research abstracts see: peptides: intercellular signaling peptides and proteins: cytokines: transforming growth factor beta research

    PUBMED ID PMID:

    MEDLINE DATE:

    Matrix metalloproteinases in periodontal tissue remodelling. Journal Published:

    PUBLICATION TYPE: Review

    Journal: Matrix (Stuttgart, Germany). Supplement

    VOLUME: 1

    Page Numbers: 352-62

    Journal Abbreviation:

    ISSN: 0940-1199

    DAY: 26

    MONTH: 02

    YEAR: 1992

    Matrix metalloproteinases in periodontal tissue remodelling. Information

    Number of References: 64

    LANGUAGE: eng

    NlmUniqueID: 9312140

    Matrix metalloproteinases in periodontal tissue remodelling. Keywords Mesh Terms:

    KEYWORDS: Transforming Growth Factor beta

    MESH TERMS: physiology

    Chemical & Substance for Abstract: Matrix metalloproteinases in periodontal tissue remodelling. Information

    Substance Name: Matrix Metalloproteinase 8

    Registry Number: EC 3.4.24.34

    Grant and Affiliation Information for Matrix metalloproteinases in periodontal tissue remodelling.

    AFFILIATION: Faculty of Dentistry, University of Toronto, Ontario, Canada.

    Country: GERMANY

    GERMANY Research PublicationGERMANY Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Matrix Suppl

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

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