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Abnormal dentin structure in two novel gene mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] causing rare type I collagen disorders.
Arch Oral Biol. 2007 Feb; 52(2):101-9.AO

Abstract

Histological and ultrastructural observations of dentin of two patients affected with rare types of type I collagen disorders are presented. In the first case, a homozygous nonsense mutation in ADAMTS2 (substitution of a codon for tryptophan by a stopcodon) causes type VIIC Ehlers-Danlos syndrome (EDS) with multiple tooth agenesis and focal dysplastic dentin defects. In the second case, a missense mutation in COL1A1 (substitution of arginine by cysteine) results in a type I EDS phenotype with clinically normal-appearing dentition. Tooth samples are investigated by using light microscopy (LM), transmission electron microscopy (TEM) and immunostaining for types I and III collagen, and tenascin. These are compared with samples from patients with types III and IV osteogenesis imperfecta (OI) in association with dentinogenesis imperfecta (DI), showing a consistently abnormal appearance of the dentin in all specimens, with variations being primarily those of degree of change. Similarities in histological changes include the alternating presence of normal and severe pathological areas in primary and secondary dentin, the latter being characterized by large canal-like structures in atubular areas. Ultrastructural evidence of pathological dentinogenesis include abnormal distribution, size and organization of collagen fibers, which may also be found in clinically unaffected teeth. The histological and ultrastructural changes seen can be explained on the basis of odontoblast dysfunction which may be secondary to the collagen defect, interfering with different levels of odontoblast cell function and intercellular communication. These observations on (ultra)structural dentin defects associated with the two novel gene mutations are the first ever reported.

Authors+Show Affiliations

Department of Paediatric Dentistry and Special Care, Paecamed Research, Ghent University, Ghent, Belgium. peter.decoster@ugent.beNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

17118335

Citation

De Coster, P J., et al. "Abnormal Dentin Structure in Two Novel Gene Mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] Causing Rare Type I Collagen Disorders." Archives of Oral Biology, vol. 52, no. 2, 2007, pp. 101-9.
De Coster PJ, Cornelissen M, De Paepe A, et al. Abnormal dentin structure in two novel gene mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] causing rare type I collagen disorders. Arch Oral Biol. 2007;52(2):101-9.
De Coster, P. J., Cornelissen, M., De Paepe, A., Martens, L. C., & Vral, A. (2007). Abnormal dentin structure in two novel gene mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] causing rare type I collagen disorders. Archives of Oral Biology, 52(2), 101-9.
De Coster PJ, et al. Abnormal Dentin Structure in Two Novel Gene Mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] Causing Rare Type I Collagen Disorders. Arch Oral Biol. 2007;52(2):101-9. PubMed PMID: 17118335.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Abnormal dentin structure in two novel gene mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] causing rare type I collagen disorders. AU - De Coster,P J, AU - Cornelissen,M, AU - De Paepe,A, AU - Martens,L C, AU - Vral,A, Y1 - 2006/11/21/ PY - 2006/03/30/received PY - 2006/08/01/accepted PY - 2006/11/23/pubmed PY - 2007/11/10/medline PY - 2006/11/23/entrez SP - 101 EP - 9 JF - Archives of oral biology JO - Arch Oral Biol VL - 52 IS - 2 N2 - Histological and ultrastructural observations of dentin of two patients affected with rare types of type I collagen disorders are presented. In the first case, a homozygous nonsense mutation in ADAMTS2 (substitution of a codon for tryptophan by a stopcodon) causes type VIIC Ehlers-Danlos syndrome (EDS) with multiple tooth agenesis and focal dysplastic dentin defects. In the second case, a missense mutation in COL1A1 (substitution of arginine by cysteine) results in a type I EDS phenotype with clinically normal-appearing dentition. Tooth samples are investigated by using light microscopy (LM), transmission electron microscopy (TEM) and immunostaining for types I and III collagen, and tenascin. These are compared with samples from patients with types III and IV osteogenesis imperfecta (OI) in association with dentinogenesis imperfecta (DI), showing a consistently abnormal appearance of the dentin in all specimens, with variations being primarily those of degree of change. Similarities in histological changes include the alternating presence of normal and severe pathological areas in primary and secondary dentin, the latter being characterized by large canal-like structures in atubular areas. Ultrastructural evidence of pathological dentinogenesis include abnormal distribution, size and organization of collagen fibers, which may also be found in clinically unaffected teeth. The histological and ultrastructural changes seen can be explained on the basis of odontoblast dysfunction which may be secondary to the collagen defect, interfering with different levels of odontoblast cell function and intercellular communication. These observations on (ultra)structural dentin defects associated with the two novel gene mutations are the first ever reported. SN - 0003-9969 UR - https://www.unboundmedicine.com/medline/citation/17118335/Abnormal_dentin_structure_in_two_novel_gene_mutations_[COL1A1_Arg134Cys]_and_[ADAMTS2_Trp795_to_ter]_causing_rare_type_I_collagen_disorders_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9969(06)00231-7 DB - PRIME DP - Unbound Medicine ER -