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Novel FGF10 mutation in autosomal dominant aplasia of lacrimal and salivary glands
Seymen, F.,Koruyucu, M.,Toptanci, I. R.,Balsak, S.,Dedeoglu, S.,Celepkolu, T.,Shin, T. J.,Hyun, H. K.,Kim, Y. J.,Kim, J. W. Springer Science + Business Media 2017 Clinical oral investigations Vol.21 No.1
<P>Identification of the genetic etiology of the ALSG will help both the family members and dentist understand the nature of the disorder. Therefore, it will positively motivate oral health care to avoid further destruction of the tooth due to the lack of salivary production.</P>
Novel <i>ITGB6</i> mutation in autosomal recessive amelogenesis imperfecta
Seymen, F,Lee, K-E,Koruyucu, M,Gencay, K,Bayram, M,Tuna, EB,Lee, ZH,Kim, J-W Stockton Press 2015 Oral diseases Vol.21 No.4
<P><B>Objective</B></P><P>Hereditary defects in tooth enamel formation, amelogenesis imperfecta (AI), can be non-syndromic or syndromic phenotype. Integrins are signaling proteins that mediate cell–cell and cell–extracellular matrix communication, and their involvement in tooth development is well known. The purposes of this study were to identify genetic cause of an AI family and molecular pathogenesis underlying defective enamel formation.</P><P><B>Materials and Methods</B></P><P>We recruited a Turkish family with isolated AI and performed mutational analyses to clarify the underlying molecular genetic etiology.</P><P><B>Results</B></P><P>Autozygosity mapping and exome sequencing identified a novel homozygous <I>ITGB6</I> transversion mutation in exon 4 (c.517G>C, p.Gly173Arg). The glycine at this position in the middle of the <I>β</I>I-domain is conserved among a wide range of vertebrate orthologs and human paralogs. Clinically, the enamel was generally thin and pitted with pigmentation. Thicker enamel was noted at the cervical area of the molars.</P><P><B>Conclusions</B></P><P>In this study, we identified a novel homozygous <I>ITGB6</I> mutation causing isolated AI, and this advances the understanding of normal and pathologic enamel development.</P>
<i>ENAM</i> Mutations with Incomplete Penetrance
Seymen, F.,Lee, K.-E.,Koruyucu, M.,Gencay, K.,Bayram, M.,Tuna, E.B.,Lee, Z.H.,Kim, J.-W. Journal of Dental Research, Inc 2014 Journal of dental research Vol.93 No.10
<P>Amelogenesis imperfecta (AI) is a genetic disease affecting tooth enamel formation. AI can be an isolated entity or a phenotype of syndromes. To date, more than 10 genes have been associated with various forms of AI. We have identified 2 unrelated Turkish families with hypoplastic AI and performed mutational analysis. Whole-exome sequencing identified 2 novel heterozygous nonsense mutations in the <I>ENAM</I> gene (c.454G>T p.Glu152* in family 1, c.358C>T p.Gln120* in family 2) in the probands. Affected individuals were heterozygous for the mutation in each family. Segregation analysis within each family revealed individuals with incomplete penetrance or extremely mild enamel phenotype, in spite of having the same mutation with the other affected individuals. We believe that these findings will broaden our understanding of the clinical phenotype of AI caused by <I>ENAM</I> mutations.</P>
Novel <i>MMP20</i> and <i>KLK4</i> Mutations in Amelogenesis Imperfecta
Seymen, F.,Park, J.-C.,Lee, K.-E.,Lee, H.-K.,Lee, D.-S.,Koruyucu, M.,Gencay, K.,Bayram, M.,Tuna, E.B.,Lee, Z.H.,Kim, Y.-J.,Kim, J.-W. SAGE Publications 2015 Journal of dental research Vol.94 No.8
<P>In order to achieve highly mineralized tooth enamel, enamel proteinases serve the important function of removing the remaining organic matrix in the mineralization and maturation of the enamel matrix. Mutations in the kallikrein 4 (<I>KLK4</I>), enamelysin (<I>MMP20</I>), and <I>WDR72</I> genes have been identified as causing hypomaturation enamel defects in an autosomal-recessive hereditary pattern. In this report, 2 consanguineous families with a hypomaturation-type enamel defect were recruited, and mutational analysis was performed to determine the molecular genetic etiology of the disease. Whole exome sequencing and autozygosity mapping identified novel homozygous mutations in the <I>KLK4</I> (c.620_621delCT, p.Ser207Trpfs*38) and <I>MMP20</I> (c.1054G>A, p.Glu352Lys) genes. Further analysis on the effect of the mutations on the translation, secretion, and function of KLK4 and MMP20 revealed that mutant KLK4 was degraded intracellularly and became inactive while mutant MMP20 was expressed at a normal level but secreted only minimally with proteolytic function.</P>