Tags

Type your tag names separated by a space and hit enter

Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location.
J Bone Miner Res. 2011 Apr; 26(4):873-80.JB

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.

Authors+Show Affiliations

Institute of Dentistry, Biomedicum, University of Helsinki, Helsinki, Finland. pekka.nieminen@helsinki.fiNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20949630

Citation

Nieminen, Pekka, et al. "Frameshift Mutations in Dentin Phosphoprotein and Dependence of Dentin Disease Phenotype On Mutation Location." Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, vol. 26, no. 4, 2011, pp. 873-80.
Nieminen P, Papagiannoulis-Lascarides L, Waltimo-Siren J, et al. Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location. J Bone Miner Res. 2011;26(4):873-80.
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. (2011). Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location. Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, 26(4), 873-80. https://doi.org/10.1002/jbmr.276
Nieminen P, et al. Frameshift Mutations in Dentin Phosphoprotein and Dependence of Dentin Disease Phenotype On Mutation Location. J Bone Miner Res. 2011;26(4):873-80. PubMed PMID: 20949630.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location. AU - Nieminen,Pekka, AU - Papagiannoulis-Lascarides,Lisa, AU - Waltimo-Siren,Janna, AU - Ollila,Päivi, AU - Karjalainen,Sara, AU - Arte,Sirpa, AU - Veerkamp,Jaap, AU - Tallon Walton,Victoria, AU - Chimenos Küstner,Eduard, AU - Siltanen,Tarja, AU - Holappa,Heidi, AU - Lukinmaa,Pirjo-Liisa, AU - Alaluusua,Satu, PY - 2010/10/16/entrez PY - 2010/10/16/pubmed PY - 2011/9/3/medline SP - 873 EP - 80 JF - Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research JO - J Bone Miner Res VL - 26 IS - 4 N2 - 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. SN - 1523-4681 UR - https://www.unboundmedicine.com/medline/citation/20949630/Frameshift_mutations_in_dentin_phosphoprotein_and_dependence_of_dentin_disease_phenotype_on_mutation_location_ L2 - https://doi.org/10.1002/jbmr.276 DB - PRIME DP - Unbound Medicine ER -