Expression and localization of membrane type 1 matrix metalloproteinase in tooth tissues

Faculty of Dentistry, Laval University, Quebec, Canada.
Matrix Biology (Impact Factor: 5.07). 12/1998; 17(7):501-11. DOI: 10.1016/S0945-053X(98)90098-1
Source: PubMed


Matrix metalloproteinases (MMPs) have been detected in forming dental enamel and are thought to play an important role during enamel biomineralization. Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a membrane bound member of the MMP gene family that has previously been shown to be expressed by cells associated with bone and cartilage formation (osteoclasts, osteoblasts and chondrocytes). Thus, we asked if MT1-MMP was also expressed by the cells responsible for the formation of enamel and dentin. A porcine MT1-MMP cDNA composed of 3284 bp was isolated from an enamel organ-specific cDNA library. Multiple tissue Northern blot analysis revealed that the MT1-MMP message was expressed highly in the enamel organ and pulp organ when compared to the expression levels observed in other non-mineralizing tissues. Northern blot analysis of stage-specific enamel organs (early secretory, late secretory, or maturation stage) and their corresponding pulp organs revealed that MT1-MMP expression increased as the dentin matured. In the enamel organs, however, the MT1-MMP message level became reduced only during the late secretory stage. Immunohistochemical analysis showed that MT1-MMP was present on the surface of the cells (ameloblasts and odontoblasts) responsible for dentin and enamel formation. Thus, MT1-MMP is highly expressed in developing tooth tissues and may play a role in the biomineralization of enamel and dentin.

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    • "Since the first description of MT1-MMP (Sato et al. 1994) in the 1990s, studies have reported its effects in general (Holmbeck et al. 1999, 2005) and in teeth development (Beertsen et al. 2003, 2002; Bartlett et al. 2003; Caron et al. 1998; Yoshiba et al. 2003). MT1-MMP has been reported in normal molar teeth during all stages of dental development from the bud, cap and early bell stages. "
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    ABSTRACT: MT1-MMP (membrane type matrix metalloproteinase-1) has been considered an important membrane-type matrix metalloproteinase involved in the remodeling process in tissue and organ development, including the processes of the tooth and root growth and dental eruption. Therefore, the aims of this study were to evaluate MT1-MMP expression in the odontogenic region, as well as the eruption rate and morphology of the lower-left rat incisor, where the eruption process was interrupted for 14 days by a steel wire attached from the center of the incisor labial face and braced to the first molar. In the interrupted eruption group, the eruption rate was significantly reduced, producing drastic morphological alterations in the tooth germ and socket area. The MT1-MMP expression was widespread in the dental follicle, in both groups studied (normal and interrupted eruption groups); however a significant decrease in immunostaining was observed in the interrupted eruption group. Results indicate that MT1-MMP may have an important role in the process of dental eruption.
    Journal of molecular histology 09/2011; 42(6):505-11. DOI:10.1007/s10735-011-9356-0 · 1.82 Impact Factor
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    • "Therefore if the incisor is in continuous eruption an intense MMP activity in dental follicle tissue of the odontogenic region is expected. This approached was partially confirmed regarding a membrane bound metalloproteinase denominated MT1-MMP by Beertsen et al. (2002, 2003), Caron et al. (1998), Bartlett et al. (2003) which demonstrated that MT1-MMP is involved in both eruption and root elongation. In addition, our recent results (Gomes et al. 2010) show that in rat incisor MT1-MMP and TIMP-2 are increased after a shorting treatment, suggesting that these molecules may be involved in the cell proliferation and consequently in the increase in eruption rate. "
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    ABSTRACT: MMP-9 and MMP-2 are metalloproteinases which degrade the denatured collagen fibers. However, there is no report about roles of these MMPs in the odontogenic region of the adult rat incisor tooth under different eruption conditions. Male Wistar rats were divided in a normofunctional group (NF) in which their lower teeth remained in a normal eruption. In a hypofunctional group (HP) rats underwent shortening of their lower left incisor tooth every 2 days during 12 days. The eruption rate as well as the expression and activities of MMP-9 and MMP-2 were evaluated using imunohistochemistry and zymography. Although the shortening increased the eruption rate, no changes in the MMP-9 and MMP-2 were observed. We conclude that in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor.
    Journal of molecular histology 02/2011; 42(2):153-9. DOI:10.1007/s10735-011-9318-6 · 1.82 Impact Factor
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    • "Approximately 30 µg of total RNA extracted from 6-month-old porcine pulp and enamel organs was characterized by Northern blot analysis as described previously (Caron et al., 1998). The pulp and enamel organ were at the secretory (third molar), early maturation (second molar), and maturation (third premolar) stages of development (Robinson et al., 1987). "
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    ABSTRACT: Fluorosed enamel can be porous, mottled, discolored, hypomineralized, and protein-rich if the enamel matrix is not completely removed. Proteolytic processing by matrix metalloproteinase-20 (MMP20) and kallikrein-4 (KLK4) is critical for enamel formation, and homozygous mutation of either protease results in hypomineralized, protein-rich enamel. Herein, we demonstrate that the lysosomal proteinase cathepsin K is expressed in the enamel organ in a developmentally defined manner that suggests a role for cathepsin K in degrading re-absorbed enamel matrix proteins. We therefore asked if fluoride directly inhibits the activity of MMP20, KLK4, dipeptidyl peptidase I (DPPI) (an in vitro activator of KLK4), or cathepsin K. Enzyme kinetics were studied with quenched fluorescent peptides with purified enzyme in the presence of 0-10 mM NaF, and data were fit to Michaelis-Menten curves. Increasing concentrations of known inhibitors showed decreases in enzyme activity. However, concentrations of up to 10 mM NaF had no effect on KLK4, MMP20, DPPI, or cathepsin K activity. Our results show that fluoride does not directly inhibit enamel proteolytic activity.
    Journal of dental research 11/2010; 90(4):489-94. DOI:10.1177/0022034510390043 · 4.14 Impact Factor
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