TY - JOUR
TI - Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location
AU - Nieminen, P.
AU - Papagiannoulis-Lascarides, L.
AU - Waltimo-Siren, J.
AU - Ollila, P.
AU - Karjalainen, S.
AU - Arte, S.
AU - Veerkamp, J.
AU - Tallon Walton, V.
AU - Chimenos Küstner, E.
AU - Siltanen, T.
AU - Holappa, H.
AU - Lukinmaa, P.-L.
AU - Alaluusua, S.
JO - JOURNAL OF BONE AND MINERAL RESEARCH
PY - 2011
VL - 26
TODO - 4
SP - 873-880
PB - 
SN - 0884-0431
TODO - 10.1002/jbmr.276
TODO - phosphoprotein, adolescent;  adult;  article;  carboxy terminal sequence;  child;  clinical article;  controlled study;  dentin;  female;  frameshift mutation;  gene mutation;  genetic code;  human;  hydrophobicity;  male;  phenotype;  preschool child;  school child;  sequence analysis;  tooth malformation, Adolescent;  Adult;  Amelogenesis Imperfecta;  Amino Acid Sequence;  Child;  Child, Preschool;  Dentin Dysplasia;  Dentinogenesis Imperfecta;  Exons;  Extracellular Matrix Proteins;  Family;  Frameshift Mutation;  Heterozygote;  Humans;  Hydrophobic and Hydrophilic Interactions;  Molecular Sequence Data;  Pedigree;  Phenotype;  Phosphoproteins;  Sialoglycoproteins;  Tooth;  Tooth Abnormalities;  Tooth, Deciduous;  Young Adult
TODO - 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.
ER -