Tags

Type your tag names separated by a space and hit enter

Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification.
Eur J Hum Genet. 2015 Apr; 23(4):445-51.EJ

Abstract

Dentinogenesis imperfecta is an autosomal dominant disease characterized by severe hypomineralization of dentin and altered dentin structure. Dentin extra cellular matrix is composed of 90% of collagen type I and 10% of non-collagenous proteins among which dentin sialoprotein (DSP), dentin glycoprotein (DGP) and dentin phosphoprotein (DPP) are crucial in dentinogenesis. These proteins are encoded by a single gene: dentin sialophosphoprotein (DSPP) and undergo several post-translational modifications such as glycosylation and phosphorylation to contribute and to control mineralization. Human mutations of this DSPP gene are responsible for three isolated dentinal diseases classified by Shield in 1973: type II and III dentinogenesis imperfecta and type II dentin dysplasia. Shield classification was based on clinical phenotypes observed in patient. Genetics results show now that these three diseases are a severity variation of the same pathology. So this review aims to revise and to propose a new classification of the isolated forms of DI to simplify diagnosis for practitioners.

Authors+Show Affiliations

1] Centre de Recherche des Cordeliers, INSERM UMRS 872, Laboratory of Molecular Oral Pathophysiology, Paris, France [2] Paris-Descartes University, Paris, France [3] The Pierre-and-Marie-Curie University, Paris, France [4] Paris-Diderot, School of Dentistry, Paris, France [5] Reference Center for Dental Rare Disease, MAFACE Rothschild Hospital, AP-HP, Paris, France.1] Centre de Recherche des Cordeliers, INSERM UMRS 872, Laboratory of Molecular Oral Pathophysiology, Paris, France [2] Paris-Descartes University, Paris, France [3] The Pierre-and-Marie-Curie University, Paris, France [4] Paris-Diderot, School of Dentistry, Paris, France [5] Reference Center for Dental Rare Disease, MAFACE Rothschild Hospital, AP-HP, Paris, France.1] Centre de Recherche des Cordeliers, INSERM UMRS 872, Laboratory of Molecular Oral Pathophysiology, Paris, France [2] Paris-Descartes University, Paris, France [3] The Pierre-and-Marie-Curie University, Paris, France [4] Paris-Diderot, School of Dentistry, Paris, France [5] Reference Center for Dental Rare Disease, MAFACE Rothschild Hospital, AP-HP, Paris, France.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

25118030

Citation

de La Dure-Molla, Muriel, et al. "Isolated Dentinogenesis Imperfecta and Dentin Dysplasia: Revision of the Classification." European Journal of Human Genetics : EJHG, vol. 23, no. 4, 2015, pp. 445-51.
de La Dure-Molla M, Philippe Fournier B, Berdal A. Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification. Eur J Hum Genet. 2015;23(4):445-51.
de La Dure-Molla, M., Philippe Fournier, B., & Berdal, A. (2015). Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification. European Journal of Human Genetics : EJHG, 23(4), 445-51. https://doi.org/10.1038/ejhg.2014.159
de La Dure-Molla M, Philippe Fournier B, Berdal A. Isolated Dentinogenesis Imperfecta and Dentin Dysplasia: Revision of the Classification. Eur J Hum Genet. 2015;23(4):445-51. PubMed PMID: 25118030.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification. AU - de La Dure-Molla,Muriel, AU - Philippe Fournier,Benjamin, AU - Berdal,Ariane, Y1 - 2014/08/13/ PY - 2014/02/07/received PY - 2014/07/08/revised PY - 2014/07/10/accepted PY - 2014/8/14/entrez PY - 2014/8/15/pubmed PY - 2015/12/17/medline SP - 445 EP - 51 JF - European journal of human genetics : EJHG JO - Eur J Hum Genet VL - 23 IS - 4 N2 - Dentinogenesis imperfecta is an autosomal dominant disease characterized by severe hypomineralization of dentin and altered dentin structure. Dentin extra cellular matrix is composed of 90% of collagen type I and 10% of non-collagenous proteins among which dentin sialoprotein (DSP), dentin glycoprotein (DGP) and dentin phosphoprotein (DPP) are crucial in dentinogenesis. These proteins are encoded by a single gene: dentin sialophosphoprotein (DSPP) and undergo several post-translational modifications such as glycosylation and phosphorylation to contribute and to control mineralization. Human mutations of this DSPP gene are responsible for three isolated dentinal diseases classified by Shield in 1973: type II and III dentinogenesis imperfecta and type II dentin dysplasia. Shield classification was based on clinical phenotypes observed in patient. Genetics results show now that these three diseases are a severity variation of the same pathology. So this review aims to revise and to propose a new classification of the isolated forms of DI to simplify diagnosis for practitioners. SN - 1476-5438 UR - https://www.unboundmedicine.com/medline/citation/25118030/Isolated_dentinogenesis_imperfecta_and_dentin_dysplasia:_revision_of_the_classification_ L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25118030/ DB - PRIME DP - Unbound Medicine ER -