Matrix metalloproteinases (MMP-2 and MMP-9) of the oral cavity: cellular origin and relationship to periodontal status (original) (raw)
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Quintessence international (Berlin, Germany : 1985), 2007
To compare the levels of matrix metalloproteinase-2 and -9 (MMP-2 and MMP-9) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in patients with gingivitis and periodontitis and in healthy controls. Levels of MMP-2, MMP-9, and TIMP-1 were determined by ELISA in patients with healthy gingiva (n = 16), gingivitis (n = 18), and periodontitis (n = 25). The subjects with periodontitis were examined before and 1 month after basic periodontal therapy. Slightly higher concentrations of MMP-9 were observed in patients with periodontitis but without statistical significance. MMP-2 was found to be slightly diminished in these patients. The lowest concentrations of MMP inhibitor (TIMP-1) were observed in patients with periodontitis, in whom the concentrations increased after periodontal treatment. The reduction in TIMP-1 concentrations in disease situations suggests a breakdown of the balance between the amount of MMPs and their inhibitor.
AIMS Molecular Science
Matrix metalloproteinases (MMPs) are one of the most important endopeptidases in periodontal disease that generally degrade extracellular matrix (ECM) components of periodontal supporting tissues, leading to tooth loss. Among the MMP family, MMP-1,-8 and-13, which are also known as the collagenase group, play a vital role in the degradation of ECM collagen and noncollagen substances. Elevated levels of MMP-1,-8 and-13 are markedly significant within tissue, gingival crevicular fluid (GCF), and saliva of patients with periodontitis, which help to explain the progression pattern of the disease. This review provides an overview of MMP-1,-8, and-13 on their structures, functions and their critical role in periodontitis.
The role of matrix metalloproteinases in the oral environment
Acta Odontologica Scandinavica, 2007
This review focuses specifically on matrix metalloproteinases (MMPs) and their role in physiological and pathological extracellular matrix (ECM) remodeling and degradation processes in the oral environment. A group of enzymes capable of degrading almost all ECM proteins, MMPs contribute to both normal and pathological tissue remodeling. The expression of different MMPs may be upregulated in pathological conditions such as inflammation and tumor invasion. The balance between activated MMPs and tissue inhibitors of metalloproteinases (TIMPs) controls the extent of ECM remodeling. Prior to mineralization, MMPs may participate in the organization of enamel and dentin organic matrix, or they may regulate mineralization by controlling the proteoglycan turnover. There is evidence indicating that MMPs could be involved in the etiology of enamel fluorosis and amelogenesis imperfecta. They seem to play a part in dentinal caries progression, since they have a crucial role in dentin collagen breakdown in caries lesions. MMPs have been identified in pulpal and periapical inflammation and are strongly correlated with periodontal diseases, since they are the major players in collagen breakdown during periodontal tissue destruction. The use of MMP inhibitors could help the prevention and treatment of many MMPrelated oral diseases.
Matrix Metalloproteinases & Implication in Periodontitis- A Short Review
2013
Matrix metalloproteinases (MMPs) are a group of enzymes which are responsible for the degradation of extracellular matrix during normal tissue turnover and also during inflammatory processes. The expression and activity of MMPs in adult tissues is normally quite low, but increases significantly in various pathological conditions that may lead into unwanted tissue destruction,such as inflammatory diseases, tumour growth and metastasis. The role of MMP-8 in periodontitis is the well-known example of the unwanted tissue destruction related to increased activity of MMPs. Degradation of the extracellular matrix may involve four distinct pathways. A body of evidence suggests that matrix components may be dissolved by extracellular matrix metalloproteinase (MMP)-dependent or plasmin (Pln)-dependent cleavage reactions and that larger fragment of matrix may be disposed by a phagocytic pathway by way of cleavage by lysosomal proteinases. Mineralized matrices appear to be degraded by a complex...
International Journal of Molecular Sciences
Objectives: This review article aims to describe some of the roles of Matrix metalloproteinases (MMPs) in enamel, dentine, dental caries, hybrid layer degradation, pulp and periodontal tissues, throwing light on their current inhibitors. The article addresses the potential of MMPs to serve as biomarkers with diagnostic and therapeutic value. Design: The sections of this review discuss MMPs’ involvement in developmental, remodeling, degradational and turnover aspects of dental and periodontal tissues as well as their signals in the pathogenesis, progress of different lesions and wound healing of these tissues. The literature was searched for original research articles, review articles and theses. The literature search was conducted in PubMed and MEDLINE for articles published in the last 20 years. Results: 119 published papers, two textbooks and two doctoral theses were selected for preparing the current review. Conclusions: MMPs are significant proteases, of evident contribution in ...
Journal of Clinical Periodontology, 2009
Aim: Matrix metalloproteinases (MMP)‐13 can initiate bone resorption and activate proMMP‐9 in vitro, and both these MMPs have been widely implicated in tissue destruction associated with chronic periodontitis. We studied whether MMP‐13 activity and TIMP‐1 levels in gingival crevicular fluid (GCF) associated with progression of chronic periodontitis assessed clinically and by measuring carboxy‐terminal telopeptide of collagen I (ICTP) levels. We additionally addressed whether MMP‐13 could potentiate gelatinase activation in diseased gingival tissue.Materials and Methods: In this prospective study, GCF samples from subjects undergoing clinical progression of chronic periodontitis and healthy controls were screened for ICTP levels, MMP‐13 activity and TIMP‐1. Diseased gingival explants were cultured, treated or not with MMP‐13 with or without adding CL‐82198, a synthetic MMP‐13 selective inhibitor, and assayed by gelatin zymography and densitometric analysis.Results: Active sites demon...
Significance of metalloproteinases in the progression of the periodontal disease
Revista Odonto Ciência, 2015
Objectives: The objective of this study was to evaluate the immunohistochemical expression of matrix metalloproteinases (MMPs)-1,-2 and-9 in the progression of the periodontal disease. Materials and methods: Thirteen gingival biopsies with clinical diagnosis of gingivitis and 13 with periodontitis were obtained and processed by immunohistochemical method. Staining of MMPs was scored according to intensity, both in epithelium and in connective tissue, in absent staining (-) which was attributed the score 0; weak staining (+), score 1; and strong staining (++), score 2. Results: MMP-1 has expressed significantly more than the others MMPs in gingivitis both in the epithelium (p=0.0008) and connective tissue (p=0.0049). In periodontitis, both MMP-1 and MMP-9 has expressed significantly in the epithelium (p<0,0001) and in the connective tissue (p=0.0002). MMP-1 and MMP-9 presented more expression in periodontitis than in gingivitis but, MMP-1 only in connective tissue (p=0,03) and MMP-9 in the epithelium (p=0.003) and in the connective tissue (p=0.04). Conclusion: These results indicate MMP-1 have an important role in connective tissue degradation and bone loss and MMP-9, that has expressed more in periodontitis, may have some role in the progression of gingivitis to periodontitis by acting in bone resorption.
Gingival Crevicular Fluid Matrix Metalloproteinase-25 and -26 Levels in Periodontal Disease
Journal of Periodontology, 2006
BACKGROUND: The purpose of this study was to evaluate the levels, molecular forms and activation degree of matrix metalloproteinase-13 (MMP-13) in the gingival crevicular fluid (GCF) of patients with periodontal diseases and to correlate these findings with periodontal clinical parameters. METHODS: Sixty one subjects participated in this study as healthy (n ¼ 18), gingivitis (n ¼ 17), aggressive periodontitis (AgP; n ¼ 15) and chronic periodontitis (CP; n ¼ 11) groups. Clinical measurements and GCF samples were obtained from each subject. The molecular forms of MMP-13 in GCF samples were analyzed by Western immunoblotting method. Differences among the groups were assessed using non-parametric statistical analysis. RESULTS: In the CP group, levels of 29-30 kDa fragment of MMP-13, total MMP-13, and activated form of MMP-13 were significantly higher than in the healthy, gingivitis and AgP groups. GCF levels of all molecular forms of MMP-13 in AgP group were similar to those of healthy and gingivitis groups. Total and activated MMP-13 levels were positively correlated with all clinical parameters. 29-30 kDa fragment levels of MMP-13 were also positively correlated with papillary bleeding index and plaque index. CONCLUSION: These results indicate that elevated GCF MMP-13 levels may play an important role in the pathogenesis of CP. These data demonstrate, for the first time, pathologically activated and elevated MMP-13 in GCF. Oral Diseases (2006) 12, 573-579