Dental Tissues Remodeling by Matrix Metalloproteinases (MMPS) and Tissues Inhibitors of MMPS (TIMPS)
Michel Goldberg*
Professor Emeritus, Department of Oral Biology, Faculty of Fundamental and Biomedical Sciences, INSERM UMR-S1124, Paris Cité University, France, 45 rue des Saints Pères, 75006 Paris, France
*Corresponding Author: Michel Goldberg, Professeur Emeritus, Department de Biologie Orale, Faculté des Sciences Fondamentales et Biomédicales, INSERM UMR- S1124, Paris Cité University, France, 45 rue des Saints Pères, 75006 Paris, France; Tel : 06 62 67 67 09
Received: August 09, 2022 Published: August 23, 2022
Abstract
MMPs are proteolytic enzymes that degrade matrix and non-matrix proteins (serine proteases, furin, plasmin). Catalytic enzymes constitute a family of proteases calcium-dependent and zinc-containing endopeptidases, implicated in the remodeling of dental tissues. Others enzymes involved in extracellular matrix (ECM) degradation are the disintegrins and MMPs (ADAMs) and disintegrins with thrombospontin motifs (ADAMTs) playing role in the destruction of ECM and shedding of membranes-bound receptor molecules. MMPs are organized in 6 groups (collagenases, gelatinases, stromelysins, matrilysins, metalloelastase, and membrane-type MMPs) and non-classified MMPs (such as enamelysin, also named MMP20). TIMPs -1 to -4 are specific endogenous tissue inhibitors of metalloproteinases. Emmprin hydrolyses active cell surface and extracellular matrix proteins. Meprin α and meprin β, discovered as procollagen proteinases cleaving the globular C- and N-terminal procollagen implicates collagenases, degrading the triple-helical fibrillary collagen into distinctive ¾ and ¼ fragments. In addition to the initial signaling peptide, the propeptide domain is based on the substrate specificity, the catalytic domain and the hemopexin-like C-terminal domain linked to the catalytic domain by a flexible hinge region. Synthetized in the latent form of zymogen and secreted as proenzyme, they are activated by organomercurials and other proteases. Located in the forming and maturing enamel, in sound and carious dentin, and during the alveolar bone regeneration, MMPs, active at neutral pH, are implicated in the early mineralization of dental tissues, in prevention and development of the carious lesion and in dental tissues erosion. Degradonomic constitutes the functional roles of MMPs and TIMPs in survival, migration, and morphogenesis, the key processes in remodeling and dental development.
Keywords: Metalloproteinases (MMPs), tissue inhibitors of MMPs (TIMPs), collagenases, gelatinases, matrilysins, stromelysins, membrane-type MMPs, extracellular matrix cleavage, dentin, enamel, morphogenesis, carious lesions, and prevention
Citation: Goldberg M. “Dental Tissues Remodeling by Matrix Metalloproteinases (MMPS) and Tissues Inhibitors of MMPS (TIMPS)”. SVOA Dentistry 2022, 3:4, 203-212.
