This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Ozdemir, D. Articles by Hart, T.C. Search for Related Content PubMed PubMed Citation Articles by Ozdemir, D. Articles by Hart, T.C. Pubmed/NCBI databases Compound via MeSH Substance via MeSH Hazardous Substances DB (L)-HISTIDINE 6-METHYLURACIL Genetics Home Reference Social Bookmarking                         What's this?

MMP20 Active-site Mutation in Hypomaturation Amelogenesis Imperfecta

¹ NIDCR, NIH, 10 Center Drive, Building 10, Room 5-2531, Bethesda, MD 20892-1432, USA;
² Istanbul University, School of Dentistry, Istanbul, Turkey;
³ NHGRI, NIH, Bethesda, MD 20892, USA;
⁴ University of Pittsburgh, School of Dental Medicine, Pittsburgh, PA 15261, USA; and
⁵ current address, Department of Pedodontics, Faculty of Dentistry, Yeditepe University, Istanbul, Turkey;

Correspondence: ^* corresponding author, thart{at}mail.nih.gov

The Amelogenesis Imperfecta (AI) are a group of clinically and genetically heterogeneous disorders that affect enamel formation. To date, mutations in 4 genes have been reported in various types of AI. Mutations in the genes encoding the 2 enamel proteases, matrix metalloproteinase 20 (MMP20) and kallikrein 4 (KLK4), have each been reported in a single family segregating autosomal-recessive hypomaturation AI. To determine the frequency of mutations in these genes, we analyzed 15 Turkish probands with autosomal-recessive hypomaturation AI for MMP20 and KLK4 gene mutations. No KLK4 mutations were found. A novel MMP20 mutation (g.16250T>A) was found in one family. This missense mutation changed the conserved active-site His226 residue of the zinc catalytic domain to Gln (p.H226Q). Zymogram analysis demonstrated that this missense mutation abolished MMP20 proteolytic activity. No MMP20 mutations were found in the remaining 14 probands, underscoring the genetic heterogeneity of hypomaturation AI.

Key Words: amelogenesis imperfecta • MMP20 • proteolytic activity • hypomaturation • enamelysin.

Journal of Dental Research, Vol. 84, No. 11, 1031-1035 (2005)
DOI: 10.1177/154405910508401112


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				J. P. Simmer, Y. Hu, R. Lertlam, Y. Yamakoshi, and J. C.-C. Hu Hypomaturation Enamel Defects in Klk4 Knockout/LacZ Knockin Mice J. Biol. Chem., July 10, 2009; 284(28): 19110 - 19121. [Abstract] [Full Text] [PDF]

				H.-Y. Kang, F. Seymen, S.-K. Lee, M. Yildirim, E. B. Tuna, A. Patir, K.-E. Lee, and J.-W. Kim Candidate Gene Strategy Reveals ENAM Mutations Journal of Dental Research, March 1, 2009; 88(3): 266 - 269. [Abstract] [Full Text] [PDF]

				Y. Li, C. Suggs, J. T. Wright, Z.-a. Yuan, M. Aragon, H. Fong, D. Simmons, B. Daly, E. E. Golub, G. Harrison, et al. Partial Rescue of the Amelogenin Null Dental Enamel Phenotype J. Biol. Chem., May 30, 2008; 283(22): 15056 - 15062. [Abstract] [Full Text] [PDF]

				J. C.-C. Hu, Y. Hu, C. E. Smith, M. D. McKee, J. T. Wright, Y. Yamakoshi, P. Papagerakis, G. K. Hunter, J. Q. Feng, F. Yamakoshi, et al. Enamel Defects and Ameloblast-specific Expression in Enam Knock-out/lacZ Knock-in Mice J. Biol. Chem., April 18, 2008; 283(16): 10858 - 10871. [Abstract] [Full Text] [PDF]

				K. Takamori, R. Hosokawa, X. Xu, X. Deng, P. Bringas Jr., and Y. Chai Epithelial Fibroblast Growth Factor Receptor 1 Regulates Enamel Formation Journal of Dental Research, March 1, 2008; 87(3): 238 - 243. [Abstract] [Full Text] [PDF]

				K. J. Greenlee, Z. Werb, and F. Kheradmand Matrix Metalloproteinases in Lung: Multiple, Multifarious, and Multifaceted Physiol Rev, January 1, 2007; 87(1): 69 - 98. [Abstract] [Full Text] [PDF]

				Y. Yamakoshi, J. C-C. Hu, T. Iwata, K. Kobayashi, M. Fukae, and J. P. Simmer Dentin Sialophosphoprotein Is Processed by MMP-2 and MMP-20 in Vitro and in Vivo J. Biol. Chem., December 15, 2006; 281(50): 38235 - 38243. [Abstract] [Full Text] [PDF]