matrix metallopeptidase 20
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A MMP20 gene provides instructions for making a protein called enamelysin, which is essential for normal tooth development. Enamelysin is involved in the formation of enamel, which is the hard, white material that forms the protective outer layer of each tooth. Enamel is composed mainly of mineral crystals. These microscopic crystals are arranged in organized bundles that give enamel its strength and durability.
Normal function
A MMP20 gene provides instructions for making a protein called enamelysin, which is essential for normal tooth development. Enamelysin is involved in the formation of enamel, which is the hard, white material that forms the protective outer layer of each tooth. Enamel is composed mainly of mineral crystals. These microscopic crystals are arranged in organized bundles that give enamel its strength and durability.
Certain proteins are needed to shape and organize the crystals as they form, but these proteins must be removed for enamel to harden normally. Enamelysin cuts (cleaves) other proteins involved in enamel formation, such as amelogenin and ameloblastin, into smaller pieces. Cleavage of these proteins makes them easier to remove when they are no longer needed.
Conditions referring to this gene or chromosome
Other names
enamel metalloproteinase
matrix metallopeptidase 20 (enamelysin)
matrix metalloproteinase 20
MMP-20
MMP20_HUMAN
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Leitura adicional e referências
- matrix metallopeptidase 20; MedlinePlus, National Library of Medicine.
- Gasse B, Karayigit E, Mathieu E, Jung S, Garret A, Huckert M, Morkmued S, Schneider C, Vidal L, Hemmerle J, Sire JY, Bloch-Zupan A. Homozygous and compound heterozygous MMP20 mutations in amelogenesis imperfecta. J Dent Res. 2013 Jul;92(7):598-603. doi: 10.1177/0022034513488393. Epub 2013 Apr 26.
- Iwata T, Yamakoshi Y, Hu JC, Ishikawa I, Bartlett JD, Krebsbach PH, Simmer JP. Processing of ameloblastin by MMP-20. J Dent Res. 2007 Feb;86(2):153-7. doi: 10.1177/154405910708600209.
- Khan F, Liu H, Reyes A, Witkowska HE, Martinez-Avila O, Zhu L, Li W, Habelitz S. The proteolytic processing of amelogenin by enamel matrix metalloproteinase (MMP-20) is controlled by mineral ions. Biochim Biophys Acta. 2013 Mar;1830(3):2600-7. doi: 10.1016/j.bbagen.2012.11.021.
- Kim JW, Simmer JP, Hart TC, Hart PS, Ramaswami MD, Bartlett JD, Hu JC. MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. J Med Genet. 2005 Mar;42(3):271-5. doi: 10.1136/jmg.2004.024505. No abstract available.
- Ozdemir D, Hart PS, Ryu OH, Choi SJ, Ozdemir-Karatas M, Firatli E, Piesco N, Hart TC. MMP20 active-site mutation in hypomaturation amelogenesis imperfecta. J Dent Res. 2005 Nov;84(11):1031-5. doi: 10.1177/154405910508401112.
- Simmer JP, Hu JC. Expression, structure, and function of enamel proteinases. Connect Tissue Res. 2002;43(2-3):441-9. doi: 10.1080/03008200290001159.
- Turk BE, Lee DH, Yamakoshi Y, Klingenhoff A, Reichenberger E, Wright JT, Simmer JP, Komisarof JA, Cantley LC, Bartlett JD. MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen. Biochemistry. 2006 Mar 28;45(12):3863-74. doi: 10.1021/bi052252o.
- Wang SK, Hu Y, Simmer JP, Seymen F, Estrella NM, Pal S, Reid BM, Yildirim M, Bayram M, Bartlett JD, Hu JC. Novel KLK4 and MMP20 mutations discovered by whole-exome sequencing. J Dent Res. 2013 Mar;92(3):266-71. doi: 10.1177/0022034513475626. Epub 2013 Jan 25.
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