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4 results on '"Siltanen T"'

1. Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location

Author

Nieminen, P. Papagiannoulis-Lascarides, L. Waltimo-Siren, J. Ollila, P. Karjalainen, S. Arte, S. Veerkamp, J. Tallon Walton, V. Chimenos Küstner, E. Siltanen, T. Holappa, H. Lukinmaa, P.-L. Alaluusua, S.

Subjects
stomatognathic diseases, stomatognathic system
Abstract

We describe results from a mutational analysis of the region of the dentin sialophosphoprotein (DSPP) gene encoding dentin phosphoprotein (DPP) in 12 families with dominantly inherited dentin diseases. In eight families (five mutations in the N-terminal third of DPP), the clinical and radiologic features were uniform and compatible with dentin dysplasia type II (DD-II) with major clinical signs in the deciduous dentition. In the other families (four mutations in the more C-terminal part), the permanent teeth also were affected, and the diseases could be classified as variants of dentinogenesis imperfecta. Attrition was not prominent, but periapical infections were common. Discoloring with varying intensity was evident, and pulps and root canals were obliterated in the permanent dentition. All mutations caused a frameshift that replaced the Ser-Ser-Asx repeat by a code for a hydrophobic downstream sequence of approximately original length. We conclude that frameshift mutations in DSPP explain a significant part of dentin diseases. Furthermore, we propose that the location of the mutation is reflected in the phenotypic features as a gradient from DD-II to more severe disease that does not conform to the classic definitions of DI-II. Copyright © 2011 American Society for Bone and Mineral Research.

Published
2011

4. Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location.

Author

Nieminen P, Papagiannoulis-Lascarides L, Waltimo-Siren J, Ollila P, Karjalainen S, Arte S, Veerkamp J, Tallon Walton V, Chimenos Küstner E, Siltanen T, Holappa H, Lukinmaa PL, and Alaluusua S

Subjects
Adolescent, Adult, Amelogenesis Imperfecta diagnosis, Amelogenesis Imperfecta diagnostic imaging, Amelogenesis Imperfecta genetics, Amelogenesis Imperfecta pathology, Amino Acid Sequence, Child, Child, Preschool, Dental Pulp Calcification, Dentin Dysplasia diagnosis, Dentin Dysplasia diagnostic imaging, Dentinogenesis Imperfecta diagnostic imaging, Exons genetics, Family, Heterozygote, Humans, Hydrophobic and Hydrophilic Interactions, Molecular Sequence Data, Pedigree, Phenotype, Radiography, Tooth diagnostic imaging, Tooth pathology, Tooth Abnormalities diagnostic imaging, Tooth Abnormalities pathology, Tooth, Deciduous abnormalities, Tooth, Deciduous diagnostic imaging, Tooth, Deciduous pathology, Young Adult, Dentin Dysplasia genetics, Dentin Dysplasia pathology, Dentinogenesis Imperfecta diagnosis, Dentinogenesis Imperfecta genetics, Dentinogenesis Imperfecta pathology, Extracellular Matrix Proteins genetics, Frameshift Mutation genetics, Phosphoproteins genetics, Sialoglycoproteins genetics
Abstract

We describe results from a mutational analysis of the region of the dentin sialophosphoprotein (DSPP) gene encoding dentin phosphoprotein (DPP) in 12 families with dominantly inherited dentin diseases. In eight families (five mutations in the N-terminal third of DPP), the clinical and radiologic features were uniform and compatible with dentin dysplasia type II (DD-II) with major clinical signs in the deciduous dentition. In the other families (four mutations in the more C-terminal part), the permanent teeth also were affected, and the diseases could be classified as variants of dentinogenesis imperfecta. Attrition was not prominent, but periapical infections were common. Discoloring with varying intensity was evident, and pulps and root canals were obliterated in the permanent dentition. All mutations caused a frameshift that replaced the Ser-Ser-Asx repeat by a code for a hydrophobic downstream sequence of approximately original length. We conclude that frameshift mutations in DSPP explain a significant part of dentin diseases. Furthermore, we propose that the location of the mutation is reflected in the phenotypic features as a gradient from DD-II to more severe disease that does not conform to the classic definitions of DI-II., (Copyright © 2011 American Society for Bone and Mineral Research.)

Published
2011
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