Abstract
This review provides a detailed description of matrix metalloproteinases (MMPs), focusing on those that are known to have critical roles in bone and periodontal disease. Periodontal disease is an inflammatory process initiated by anaerobic bacteria, which promote the host immune response in the form of a complex network of molecular pathways involving proinflammatory mediators such as cytokines, growth factors, and MMPs. MMPs are a family of 23 endopeptidases, collectively capable of degrading virtually all extracellular matrix (ECM) components. This study critically discusses the available research concerning the involvement of the MMPs in periodontal disease development and progression and presents possible therapeutic strategies. MMPs participate in morphogenesis, physiological tissue turnover, and pathological tissue destruction. Alterations in the regulation of MMP activity are implicated in the manifestation of oral diseases, and MMPs comprise the most important pathway in tissue destruction associated with periodontal disease. MMPs can be considered a risk factor for periodontal disease, and measurements of MMP levels may be useful markers for early detection of periodontitis and as a tool to assess prognostic follow-ups. Detection and inhibition of MMPs could, therefore, be useful in periodontal disease prevention or be an essential part of periodontal disease therapy, which, considering the huge incidence of the disease, may greatly improve oral health globally.
Highlights
Periodontitis is an inflammatory disorder that causes tissue and bone loss as a consequence of various interactions between the host immune response and pathogenic bacteria [1]
The aim of this review is to provide a detailed description of matrix metalloproteinases (MMPs) and of their critical role in bone and periodontal disease, discussing current knowledge regarding MMPs within the periodontal tissues in an attempt to better understand their role, nature, and functions in the extracellular matrix environment
A number of MMPs have been described in gingival tissues [26], the most widely reported MMPs in gingival crevicular fluid (GCF) are MMP-8, MMP-9, and MMP-13 [27,28,29,30], and among the three collagenases (MMP-1, MMP-8, and MMP-13), MMP-8 accounts for 80% of the total collagenase protein found in the GCF, with smaller relative amounts of MMP-13 and MMP-1 in chronic periodontitis [31]
Summary
Periodontitis is an inflammatory disorder that causes tissue and bone loss as a consequence of various interactions between the host immune response and pathogenic bacteria [1]. Collagen telopeptides, gelatin, elastin, fibronectin, laminin, aggrecan, decorin, perlecan, versican, a2-macroglobulin, IL-1b, pro-TNF-a, fibrinogen, pro-MMP-1, -3, -7, MMP-11. Whereas TIMPs are the primary inhibitors of MMPs in tissues, α2-macroglobulin is the primary regulator of MMP activity in body fluids This macroglobulin protein, abundant in plasma, is a general endopeptidase inhibitor that acts via enzyme entrapment and steric interference in large MMP substrate interactions, resulting in endocytosis of the α2-macroglobulin–MMP complex [10,25]. This process terminally eliminates the complex, rendering α2-macroglobulin important in irreversible MMP clearance; in contrast, TIMP-related MMP inhibition is reversible [11]. Most of these inhibitors chelate or replace the zinc ion at the active site and/or interact with the MMP propeptide fragment; some may prevent MMP access and inhibit activity by coating the substrate [21]
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