Modulation of cell-cell junctional complexes by matrix metalloproteinases.
The ameloblast cell layer of the enamel organ is in contact with the forming enamel as it develops into the hardest substance in the body. Ameloblasts move in groups that slide by one another as the enamel layer thickens. Each ameloblast is responsible for the formation of one enamel rod, and the rods are the mineralized trail that moving ameloblasts leave behind. Matrix metalloproteinases (MMPs) facilitate cell movement in various tissues during development, and in this review we suggest that the tooth-specific MMP, enamelysin (MMP20), facilitates ameloblast movements during enamel development. Mmp20 null mice have thin brittle enamel with disrupted rod patterns that easily abrades from the underlying dentin. Strikingly, the Mmp20 null mouse enamel organ morphology is noticeably dysplastic during late-stage development, when MMP20 is no longer expressed. We suggest that in addition to its role of cleaving enamel matrix proteins, MMP20 also cleaves junctional complexes present on ameloblasts to foster the cell movement necessary for formation of the decussating enamel rod pattern. Therefore, inactivation of MMP20 would result in tight ameloblast cell-cell attachments that may cause maturation-stage enamel organ dysplasia. The tight ameloblast attachments would also preclude the ameloblast movement necessary to form decussating enamel rod patterns.
Department of Mineralized Tissue Biology, Forsyth Institute, Harvard School of Dental Medicine, Cambridge, MA, USA. jdbartlett@forsyth.org
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JD
Bartlett
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Smith
D000565:Ameloblasts / Q000201:enzymology*; D000566:Amelogenesis / Q000502:physiology; D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002465:Cell Movement / Q000502:physiology; D004658:Enamel Organ / Q000201:enzymology; D007365:Intercellular Junctions / Q000201:enzymology*; D053519:Matrix Metalloproteinase 20 / Q000502:physiology*; D051379:Mice
D053519:Matrix Metalloproteinase 20; C507113:Mmp20 protein, mouse