Delayed Tooth Eruption in Membrane Type-1 Matrix Metalloproteinase Deficient Mice

References

• Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., et al. (1994). A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370:61–65.
   PubMed Web of Science ®Google Scholar
• Will, H., and Hinzmann, B. (1995). cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur. J. Biochem. 231:602–608.
   PubMedGoogle Scholar
• Takino, T., Sato, H., Shinagawa, A., and Seiki, M. (1995). Identifica- tion of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J. Biol. Chem. 270:23013–23020.
   PubMed Web of Science ®Google Scholar
• Puente, X.S., Pendas, A.M., Llano, E., Velasco, G., and Lopez-Otin, C. (1996). Molecular cloning of a novel membrane-type matrix metallopro- teinase from a human breast carcinoma. Cancer Res. 56:944–949.
   PubMed Web of Science ®Google Scholar
• Pei, D., and Weiss, S.J. (1996). Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271:9135–9140.
   PubMed Web of Science ®Google Scholar
• Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A., and Goldberg, G.I. (1995). Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270:5331–5338.
   PubMed Web of Science ®Google Scholar
• d’Ortho, M.P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., et al. (1997). Membrane-type matrix metalloproteinases 1 and 2 ex- hibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250:751–757.
   PubMedGoogle Scholar
• Buttner, F.H., Hughes, C.E., Margerie, D., Lichte, A., Tschesche, H., Caterson, B., et al. (1998). Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the ‘aggrecanase’ and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. Biochem. J. 333(Pt 1):159–165.
   PubMed Web of Science ®Google Scholar
• Fosang, A.J., Last, K., Fujii, Y., Seiki, M., and Okada, Y. (1998). Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggre- can interglobular domain. FEBS Lett. 430:186–190.
   PubMed Web of Science ®Google Scholar
• Hiraoka, N., Allen, E., Apel, I.J., Gyetko, M.R., and Weiss, S.J. (1998). Matrix metalloproteinases regulate neovascularization by acting as peri- cellular fibrinolysins. Cell 95:365–377.
   PubMed Web of Science ®Google Scholar
• Hotary, K., Allen, E., Punturieri, A., Yana, I., and Weiss, S.J. (2000). Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J. Cell Biol. 149:1309–1323.
   PubMed Web of Science ®Google Scholar
• Koshikawa, N., Giannelli, G., Cirulli, V., Miyazaki, K., and Quaranta, V. (2000). Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J. Cell Biol. 148:615–624.
   PubMed Web of Science ®Google Scholar
• Will, H., Atkinson, S.J., Butler, G.S., Smith, B., and Murphy, G. (1996). The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J. Biol. Chem. 271:17119–17123.
   PubMed Web of Science ®Google Scholar
• Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272:2446–2451.
   PubMed Web of Science ®Google Scholar
• Knauper, V., Will, H., Lopez-Otin, C., Smith, B., Atkinson, S.J., Stanton, H., et al. (1996). Cellular mechanisms for human procollagenase-3 (MMP-13)activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271: 17124–17131.
   Google Scholar
• Kinoh, H., Sato, H., Tsunezuka, Y., Takino, T., Kawashima, A., Okada, Y., et al. (1996). MT-MMP, the cell surface activator of proMMP-2 (pro- gelatinase A), is expressed with its substrate in mouse tissue during em- bryogenesis. J. Cell Sci. 109(Pt 5):953–959.
   PubMed Web of Science ®Google Scholar
• Sato, T., del Carmen, O.M., Hou, P., Heegaard, A.M., Kumegawa, M., Foged, N.T., et al. (1997). Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts. J. Cell Sci. 110(Pt 5):589–596.
   PubMed Web of Science ®Google Scholar
• Holmbeck, K., Bianco, P., Caterina, J., Yamada, S., Kromer, M., Kuznetsov, S.A., et al. (1999). MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to in- adequate collagen turnover. Cell 99:81–92.
   PubMed Web of Science ®Google Scholar
• Zhou, Z., Apte, S.S., Soininen, R., Cao, R., Baaklini, G.Y., Rauser, R.W., et al. (2000). Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I. Proc. Natl. Acad. Sci. USA 97:4052–4057.
   PubMed Web of Science ®Google Scholar
• Bartlett, J.D., and Simmer, J.P. (1999). Proteinases in developing dental enamel. Crit Rev. Oral Biol. Med. 10:425–441.
   PubMedGoogle Scholar
• Overall, C.M., and Limeback, H. (1988). Identification and characteriza- tion of enamel proteinases isolated from developing enamel. Amelogeni- nolytic serine proteinases are associated with enamel maturation in pig. Biochem. J. 256:965–972.
   PubMed Web of Science ®Google Scholar
• DenBesten, P.K., Heffernan, L.M., Treadwell, B.V., and Awbrey, B.J. (1989). The presence and possible functions of the matrix metallo- proteinase collagenase activator protein in developing enamel matrix. Biochem. J. 264:917–920.
   PubMed Web of Science ®Google Scholar
• Moradian-Oldak, J., Simmer, J.P., Sarte, P.E., Zeichner-David, M., and Fincham, A.G. (1994). Specific cleavage of a recombinant murine amelo- genin at the carboxy-terminal region by a proteinase fraction isolated from developing bovine tooth enamel. Arch. Oral Biol. 39:647–656.
   PubMed Web of Science ®Google Scholar
• DenBesten, P.K., and Heffernan, L.M. (1989). Separation by polyacry- lamide gel electrophoresis of multiple proteases in rat and bovine enamel. Arch. Oral Biol. 34:399–404.
   PubMed Web of Science ®Google Scholar
• Fukae, M., Kaneko, I., Tanabe, T., and Shimizu, M. (1991). Metallopro- teinases in the mineralized compartments of porcine dentine as detected by substrate-gel electrophoresis. Arch. Oral Biol. 36:567–573.
   PubMed Web of Science ®Google Scholar
• Fukae, M., Tanabe, T., and Yamada, M. (1994). Action of metallopro- teinases on porcine dentin mineralization. Calcif. Tiss. Int. 55:426–435.
   PubMed Web of Science ®Google Scholar
• Bartlett, J.D., Simmer, J.P., Xue, J., Margolis, H.C., and Moreno, E.C. (1996). Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ. Gene 183:123–128.
   PubMed Web of Science ®Google Scholar
• Bartlett, J.D., Ryu, O.H., Xue, J., Simmer, J.P., and Margolis, H.C. (1998). Enamelysin mRNA displays a developmentally defined pattern of expres- sion and encodes a protein which degrades amelogenin. Connect. Tiss. Res. 39:101–109.
   PubMed Web of Science ®Google Scholar
• Fukae, M., Tanabe, T., Uchida, T., Lee, S.K., Ryu, O.H., Murakami, C., et al. (1998). Enamelysin (matrix metalloproteinase-20): Localization in the developing tooth and effects of pH and calcium on amelogenin hydrol- ysis. J. Dent. Res. 77:1580–1588.
   PubMed Web of Science ®Google Scholar
• Martin-De Las, H.S., Valenzuela, A., and Overall, C.M. (2000). The matrix metalloproteinase gelatinase A in human dentine. Arch. Oral Biol. 45:757–765.
   PubMed Web of Science ®Google Scholar
• Satoyoshi, M., Kawata, A., Koizumi, T., Inoue, K., Itohara, S., Teranaka, T., et al. (2001). Matrix metalloproteinase-2 in dentin matrix mineraliza- tion. J. Endod. 27:462–466.
   PubMed Web of Science ®Google Scholar
• Caron, C., Xue, J., Sun, X., Simmer, J.P., and Bartlett, J.D. (2001). Gelati- nase A (MMP-2) in developing tooth tissues and amelogenin hydrolysis. J. Dent. Res. 80:1660–1664.
   PubMed Web of Science ®Google Scholar
• Palosaari, H., Wahlgren, J., Larmas, M., Ronka, H., Sorsa, T., Salo, T., et al. (2000). The expression of MMP-8 in human odontoblasts and dental pulp cells is down-regulated by TGF-beta1. J. Dent. Res. 79:77–84.
   PubMed Web of Science ®Google Scholar
• Hall, R., Septier, D., Embery, G., and Goldberg, M. (1999). Stromelysin- 1 (MMP-3) in forming enamel and predentine in rat incisor-coordinated distribution with proteoglycans suggests a functional role. Histochem. J. 31:761–770.
   PubMedGoogle Scholar
• Caron, C., Xue, J., and Bartlett, J.D. (1998). Expression and localization of membrane type 1 matrix metalloproteinase in tooth tissues. Matrix Biol. 17:501–511.
   PubMed Web of Science ®Google Scholar
• Marks, S.C., Jr., and Schroeder, H.E. (1996). Tooth eruption: Theories and facts. Anat. Rec. 245:374–393.
   PubMedGoogle Scholar
• Gregg, J.M. (1965). Immobilization of the erupting molar in the syrian hamster. J. Dent. Res. 44:1219–1226.
   Web of Science ®Google Scholar