Matrix metalloproteases (MMPs) are a family of zinc-dependent endopeptidases, produced by numerous cell types including fibroblasts, endothelial cells, osteoblasts, macrophages, lymphocytes and neutrophils, and capable of degrading different components of the extracellular matrix (ECM), but also cytokines, receptors and factors that regulate cell motility (1). MMPs represent the main proteolytic enzymes involved in the remodeling and degradation of the components of the extracellular matrix, in the modifications of interactions between cells, and those between cells and the ECM that regulate, for example, the processes of cell migration (2, 3). Due to these characteristics, the MMPs are involved in numerous physiological processes (angiogenesis, apoptosis, bone remodeling, wound repair, morphogenesis, inflammation, immune response) response to incongruous conservative and endodontic treatments (29-37, 46, 47) and pathological (periodontitis, arthritis, cancer, cardiovascular diseases, neurological diseases, osteoporosis etc.) (5). Metalloproteinase-8 (MMP-8) is an important indicator of tissue decomposition and is present in case of periodontitis in the gingiva and in the sulcular fluid. The concentration of MMP-8 in the sulcular fluid of patients with chronic or aggressive periodontitis is higher than that found in healthy patients (4, 6). MMP-8 was also significantly correlated with gingivitis index, plaque index, probing and clinical attack level. For this reason, the concentration of MMP-8 in the sulcular fluid could constitute a useful index to monitor periodontitis activity and be used to predict disease progression, also because of orthodontic treatments (38-45). Patients with periodontitis had elevated concentrations of MMP-8 salivary compared to patients with gingivitis and healthy tissues. Through this experimentation we wanted to demonstrate the real effectiveness of using this test as a means of preventing peri-implant pathology.

Implant-safe test in patients with peri-implantitis

Mummolo, S;Botticelli, G;Quinzi, V;Marzo, G
2020-01-01

Abstract

Matrix metalloproteases (MMPs) are a family of zinc-dependent endopeptidases, produced by numerous cell types including fibroblasts, endothelial cells, osteoblasts, macrophages, lymphocytes and neutrophils, and capable of degrading different components of the extracellular matrix (ECM), but also cytokines, receptors and factors that regulate cell motility (1). MMPs represent the main proteolytic enzymes involved in the remodeling and degradation of the components of the extracellular matrix, in the modifications of interactions between cells, and those between cells and the ECM that regulate, for example, the processes of cell migration (2, 3). Due to these characteristics, the MMPs are involved in numerous physiological processes (angiogenesis, apoptosis, bone remodeling, wound repair, morphogenesis, inflammation, immune response) response to incongruous conservative and endodontic treatments (29-37, 46, 47) and pathological (periodontitis, arthritis, cancer, cardiovascular diseases, neurological diseases, osteoporosis etc.) (5). Metalloproteinase-8 (MMP-8) is an important indicator of tissue decomposition and is present in case of periodontitis in the gingiva and in the sulcular fluid. The concentration of MMP-8 in the sulcular fluid of patients with chronic or aggressive periodontitis is higher than that found in healthy patients (4, 6). MMP-8 was also significantly correlated with gingivitis index, plaque index, probing and clinical attack level. For this reason, the concentration of MMP-8 in the sulcular fluid could constitute a useful index to monitor periodontitis activity and be used to predict disease progression, also because of orthodontic treatments (38-45). Patients with periodontitis had elevated concentrations of MMP-8 salivary compared to patients with gingivitis and healthy tissues. Through this experimentation we wanted to demonstrate the real effectiveness of using this test as a means of preventing peri-implant pathology.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/151904
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