The role of enamelysin (mmp-20) in tooth development: systematic review
DOI:
https://doi.org/10.17533/udea.rfo.v27n1a8Keywords:
Enamel development, Tooth development, Enamelysin, Amelogenesis, mmp-20, Amelogenesis imperfecta, MMP-20Abstract
Introduction: ameloblasts are cells responsible for the production and mineralization of the organic matrix of enamel through several stages: pre-secretory, secretory, transition, and maturation. The organic matrix components are produced in the secretory phase. In the maturation phase, the organic component is removed and the mineralization process starts. This process requires the involvement of matrix metalloproteinase 20 (MMP-20), also called enamelysin. Several studies have shown the presence of MMP-20 in tooth development and its relationship to alterations in enamel formation. The objective was: to classify the different studies and laboratory techniques used to demonstrate the involvement of enamelysin in tooth development and its relation to pathologies during enamel formation. Methods: a systematic review was conducted with the following bibliographic databases: PubMed, Science-Direct, Hinari, and SciELO, in order to classify the different studies related to the involvement of MMP-20 in tooth development and the methods to detect its expression, between the years of 2009 and 2014. Results and conclusions: in vitro models show that MMP-20 has specific cleavage sites for enamel matrix proteins. This process is altered by chemical composition, ions, and the presence of hydroxyapatite. Enamel morphology is altered in the knockout models. In human studies, MMP-20 has been associated with increased susceptibility to dental caries, enamel thickness, and dental agenesis.
Downloads
References
Kaufman MH. Atlas of mouse development. Ámsterdam: Elsevier, 1992.
Bartlett JD. Dental enamel development: proteinases and their enamel matrix substrates. ISRN Dent 2013; 2013:684607. doi: 10.1155/2013/684607.
Gómez de Ferraris M, Campos -Muñoz A. Histología y embriología bucodental 2a ed. Madrid: Editorial Médica Panamericana, 2002.
Evrosimovska B, Velickovski B, Dimova C, Veleska-Stefkovska D. Matrix metalloproteinases (with accent to collagenases). J Cell and Anim Biol 2011; 5(7): 113-120.
Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92(8): 827-839.
Begue-Kirn C, Krebsbach PH, Bartlett JD, Butler WT. Dentin sialoprotein, dentin phosphoprotein, enamelysin and ameloblastin: tooth-specific molecules that are distinctively expressed during murine dental differentiation. Eur J Oral Sci 1998; 106(5): 963-970.
Fukae M, Shimizu M. Studies on the proteins of developing bovine enamel. Arch Oral Biol 1974; 19 (5): 381-386.
Grant GM, Giambernardi TA, Grant AM, Klebe RJ. Overview of expression of matrix metalloproteinases (MMP-17, MMP-18, and MMP-20) in cultured human cells. Matrix Biol 1999; 18(2): 145-148.
Takata T, Zhao M, Nikai H, Uchida T, Wang T. Ghost cells in calcifying odontogenic cyst express enamel-related proteins. Histochem J 2000; 32(4): 223-229.
Takata T, Zhao M, Uchida T, Wang T, Aoki T, Bartlett JD et al. Immunohistochemical detection and distribution of enamelysin (MMP-20) in human odontogenic tumors. J Dent Res 2000; 79(8): 1608-1613.
Vaananen A, Srinivas R, Parikka M, Palosaari H, Bartlett JD, Iwata K et al. Expression and regulation of MMP-20 in human tongue carcinoma cells. J Dent Res 2001; 80(10):1884-1889.
Kim JW, Simmer JP, Hart TC, Hart PS, Ramaswami MD, Bartlett JD et al. MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. J Med Genet 2005; 42(3): 271-275
Santos MC, Line SR. The genetics of amelogenesis imperfecta: a review of the literature. J Appl Oral Sci 2005; 13(3): 212-217.
Nagano T, Kakegawa A, Yamakoshi Y, Tsuchiya S, Hu JC, Gomi K et al. Mmp-20 and Klk4 cleavage site preferences for amelogenin sequences. J Dent Res 2009; 88(9): 823-828.
Chun YH, Yamakoshi Y, Yamakoshi F, Fukae M, Hu JC, Bartlett JD et al. Cleavage site specificity of MMP-20 for secretory-stage ameloblastin. J Dent Res 2010; 89(8): 785-790.
Sun Z, Carpiaux W, Fan D, Fan Y, Lakshminarayanan R, Moradian-Oldak J. Apatite reduces amelogenin proteolysis by MMP-20 and KLK4 in vitro. J Dent Res 2010; 89(4): 344-348.
Yamakoshi Y, Simmer JP, Bartlett JD, Karakida T, Oida S. MMP20 and KLK4 activation and inactivation interactions in vitro. Arch Oral Biol 2013; 58(11): 1569-1577.
Takahashi K, Shimonishi M, Wang R, Watanabe H, Kikuchi M. Epithelial-mesenchymal interactions induce enamel matrix proteins and proteases in the epithelial cells of the rests of Malassez in vitro. Eur J Oral Sci 2012; 120(6): 475-483.
Bromley KM, Lakshminarayanan R, Thompson M, Lokappa SB, Gallon VA, Cho KR et al. Amelogenin processing by MMP-20 prevents protein occlusion inside calcite crystals. Cryst Growth Des 2012; 12(10): 4897-4905.
Uskokovic V, Khan F, Liu H, Witkowska HE, Zhu L, Li W et al. Hydrolysis of amelogenin by matrix metalloprotease-20 accelerates mineralization in vitro. Arch Oral Biol. 2011; 56(12): 1548-1559.
Khan F, Liu H, Reyes A, Witkowska HE, Martinez-Avila O, Zhu L et al. The proteolytic processing of amelogenin by enamel matrix metalloproteinase (MMP-20) is controlled by mineral ions. Biochim Biophys Acta 2013; 1830(3): 2600-2607.
Lee HK, Lee DS, Ryoo HM, Park JT, Park SJ, Bae HS et al. The odontogenic ameloblast-associated protein (ODAM) cooperates with RUNX2 and modulates enamel mineralization via regulation of MMP-20. J Cell Biochem 2010; 111(3): 755-767.
Lee HK, Park SJ, Oh HJ, Kim JW, Bae HS, Park JC. Expression pattern, subcellular localization, and functional implications of ODAM in ameloblasts, odontoblasts, osteoblasts, and various cancer cells. Gene Expr Patterns 2012; 12(3-4): 102-108.
Gao Y, Zhang L, Xiang L, Li B, Liu X, Wang Y, et. al. Transforming growth factor-beta1 regulates expression of the matrix metalloproteinase 20 (Mmp20) gene through a mechanism involving the transcription factor, myocyte enhancer factor-2C, in ameloblast lineage cells. Eur J Oral Sci 2014; 122(2): 114-120.
Yamakoshi Y, Richardson AS, Nunez SM, Yamakoshi F, Milkovich RN, Hu JC et al. Enamel proteins and proteases in Mmp20 and Klk4 null and double-null mice. Eur J Oral Sci. 2011; 119 Suppl 1: 206-216.
Bartlett JD, Skobe Z, Nanci A, Smith CE. Matrix metalloproteinase 20 promotes a smooth enamel surface, a strong dentino-enamel junction, and a decussating enamel rod pattern. Eur J Oral Sci 2011; 119 Suppl 1: 199-205.
Shin M, Hu Y, Tye CE, Guan X, Deagle CC, Antone JV et al. Matrix metalloproteinase-20 over-expression is detrimental to enamel development: a Mus musculus model. PLoS One 2014; 9(1): e86774.
Shimada Y, Ichinose S, Sadr A, Burrow MF, Tagami J. Localization of matrix metalloproteinases (MMPs-2, 8, 9 and 20) in normal and carious dentine. Aust Dent J 2009; 54(4): 347-354.
Tannure PN, Kuchler EC, Lips A, Costa Mde C, Luiz RR, Granjeiro JM et al. Genetic variation in MMP20 contributes to higher caries experience. J Dent 2012; 40(5): 381-386.
McGuire JD, Mousa AA, Zhang BJ, Todoki LS, Huffman NT, Chandrababu KB et al. Extracts of irradiated mature human tooth crowns contain MMP-20 protein and activity. J Dent. 2014; 42(5): 626-635.
Horvath JE, Ramachandran GL, Fedrigo O, Nielsen WJ, Babbitt CC, St Clair EM et al. Genetic comparisons yield insight into the evolution of enamel thickness during human evolution. J Hum Evol 2014; 73: 75-87
Kuchler EC, Menezes R, Callahan N, Costa MC, Modesto A, Meira R et al. MMP1 and MMP20 contribute to tooth agenesis in humans. Arch Oral Biol 2011; 56(5): 506-511.
Antunes LS, Kuchler EC, Tannure PN, Dias JB, Ribeiro VN, Lips A et al. Genetic variations in MMP9 and MMP13 contribute to tooth agenesis in a Brazilian population. J Oral Sci 2013; 55(4): 281-286.
Downloads
Published
How to Cite
Issue
Section
Categories
License
Copyright (c) 2015 Revista Facultad de Odontología Universidad de Antioquia
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
Copyright Notice
Copyright comprises moral and patrimonial rights.
1. Moral rights: are born at the moment of the creation of the work, without the need to register it. They belong to the author in a personal and unrelinquishable manner; also, they are imprescriptible, unalienable and non negotiable. Moral rights are the right to paternity of the work, the right to integrity of the work, the right to maintain the work unedited or to publish it under a pseudonym or anonymously, the right to modify the work, the right to repent and, the right to be mentioned, in accordance with the definitions established in article 40 of Intellectual property bylaws of the Universidad (RECTORAL RESOLUTION 21231 of 2005).
2. Patrimonial rights: they consist of the capacity of financially dispose and benefit from the work trough any mean. Also, the patrimonial rights are relinquishable, attachable, prescriptive, temporary and transmissible, and they are caused with the publication or divulgation of the work. To the effect of publication of articles in the journal Revista de la Facultad de Odontología, it is understood that Universidad de Antioquia is the owner of the patrimonial rights of the contents of the publication.
The content of the publications is the exclusive responsibility of the authors. Neither the printing press, nor the editors, nor the Editorial Board will be responsible for the use of the information contained in the articles.
I, we, the author(s), and through me (us), the Entity for which I, am (are) working, hereby transfer in a total and definitive manner and without any limitation, to the Revista Facultad de Odontología Universidad de Antioquia, the patrimonial rights corresponding to the article presented for physical and digital publication. I also declare that neither this article, nor part of it has been published in another journal.
Open Access Policy
The articles published in our Journal are fully open access, as we consider that providing the public with free access to research contributes to a greater global exchange of knowledge.
Creative Commons License
The Journal offers its content to third parties without any kind of economic compensation or embargo on the articles. Articles are published under the terms of a Creative Commons license, known as Attribution – NonCommercial – Share Alike (BY-NC-SA), which permits use, distribution and reproduction in any medium, provided that the original work is properly cited and that the new productions are licensed under the same conditions.
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.