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At least 19 recordsLinked to original sources
PubMed1992

Dentinogenesis imperfecta: a case report.

Dentinogenesis imperfecta is a localized form of mesodermal dysplasia of the dentin affecting both the primary and permanent dentitions. Most previous reports on dentinogenesis imperfecta describe treatment with overdentures, which have several disadvantages. The present report describes a case of dentinogenesis imperfecta in an 11-year-old girl. A combination of restorative, prosthetic, and surgical treatment was used to resolve the condition.

Cephalometry↗
PubMed1975

Uninherited dentinogenesis imperfecta.

The rare hereditary disease, dentinogenesis imperfecta, is a disturbance of dentin formation in both the deciduous and permanent dentitions. It may be associated with osteogenesis imperfecta, though it is probably that the two diseases are carried by different genes. This association was recognized in a 19-year-old man. Dentinogenesis imperfecta had been diagnosed at the age of 6 and had been regarded as a mutation; 11 years later, an atypical form of osteogenesis imperfecta developed. The case is atypical because of the apparent absence of dentinogenesis imperfecta in the patient's family. The dental manifestations may have heralded the bone disease.

Adult↗
PubMedDate not supplied

[Oral rehabilitation in dentinogenesis imperfecta. Report of a case].

We present a case of Amelogenesis imperfecta associated with Dentinogenesis imperfecta, affecting the primary dentition which is rehabilitated under general anesthesia. Dentinogenesis imperfecta is a tooth abnormality which presents clinical, radiological and histological characteristics, they should be recognized by the dentist who will determine the treatment depending on age and grade of affection. In the primary dentition we recommend the use of stainless steel crowns do to it's resistance and easy adaptation which will remain in the mouth until it's normal exfoliation.

Child, Preschool↗
PubMed1992

Dentin phosphoprotein gene locus is not associated with dentinogenesis imperfecta types II and III.

Dentinogenesis imperfecta (DGI) is an autosomal dominant inherited dental disease which affects dentin production and mineralization. Genetic linkage studies have been performed on several multigeneration informative kindreds. These studies determined linkage between DGI type II and III and group-specific component (vitamin D-binding protein). This gene locus has been localized to the long arm of human chromosome 4 in the region 4q11-q21. Although this disease has been mapped to chromosome 4, the defective gene product is yet to be determined. Biochemical studies have suggested abnormal levels of dentin phosphoprotein (DPP) associated with DGI type II. This highly acidic protein is the major noncollagenous component of dentin, being solely expressed by the ectomesenchymal derived odontoblast cells of the tooth. The purpose of the present study was to establish whether DPP is associated with DGI types II and III, by using molecular biology techniques. The strategy was to use a synthetic degenerative DPP oligonucleotide probe to map this sequence to the long arm of human chromosome 4, 4q13-q21, by using somatic cell hybrids. Our results indicated that DPP is not localized to any region of human chromosome 4, thus suggesting that the DPP gene is not directly associated with DGI type II or DGI type III. Our data do not exclude the possibility that other proteins associated with DPP posttranslational modifications might be responsible for this genetic disease.

Adult↗
PubMed1975

[Dentinogenesis imperfecta: a structural and ultrastructural study].

Histopathology of dentinogenesis imperfecta shows a haphazard distribution of dentinal tubules as well as changes in their diameters, sometimes narrowed, sometimes widened. These tubules appear as bundles or sheaves. This kind of dentine is often similar to secondary (also called tertiary) dentine, only mantle dentine preserving a normal structure. There is a complete obliteration of the pulp chamber and an almost complete obliteration of the root canal. Through SEM, the tubules appear to be few in number, their diameters are small and their fine ramifications are intricate through all planes. An heterogenous intertubular substance can be seen. Through TEM, collagenous fibers appear to be uncalcified or incompletely calcified, with a haphazard distribution. There are wide differences in the sizes of crystals and numerous spaces appear between crystals and collagen. Differences between the ultrastructure of human dentinogenesis imperfecta and the dentine of some lower vertebrates are clearly pointed out.

Dental Cementum↗
PubMed1992

Unusual dentinal changes in dentinogenesis imperfecta associated with osteogenesis imperfecta. A case report.

A case is described of a boy with dentinogenesis imperfecta associated with osteogenesis imperfecta. The dentin of extracted deciduous teeth was found to show an abrupt transition to a normal tubular structure before a reversion to the more typical structure seen in dentinogenesis imperfecta. This change in the dentin appeared to have occurred in a chronologic manner. The possibilities that either a metabolic disturbance or a temporary reduced expression of the mutant gene had caused the abnormality and could account for the unusual histologic findings are discussed.

Child↗
PubMed1991

[The pedodontist and dentinogenesis imperfecta].

The purpose of this article is to present a treatment of dentinogenesis imperfecta in a 3 years old child. We reviewed some of the aspects to consider in the treatments of this alteration in primary dentition.

Child, Preschool↗
PubMed1988

A probable common disturbance in the early stage of odontoblast differentiation in Dentinogenesis imperfecta type I and type II.

Deciduous teeth from 7 patients with dentinogenesis imperfecta (DI) Type I and Type II were examined by conventional microscopy. A defective layer was found which runs parallel with the dentinal surface in the outer portion of dentin in teeth of both types. Dentinal tubules were interrupted in the vicinity of this layer. When the ground sections were examined after being stained by the phosphophoryn staining method, the DI Type I dentin was found to contain phosphophoryn at the same low level as the DI Type II dentin, suggesting similar deficiency in phosphophoryn concentration. These results suggest that both types of DI have a common primary disturbance in the early stage of odontoblast differentiation.

Cell Differentiation↗
PubMed1990

[Study of the fine structure of human deciduous dentin with dentinogenesis imperfecta, with special reference to the mantle dentin].

A lower deciduous incioer exhibiting dentinogenesis imperfecta (D.I) obtained from a 6-year-old boy with osteogenesis imperfecta (Shields' Type I) was examined by means of light microscopy (LM), scanning electron microscopy (SEM), and X-ray microanalysis (XMA). With LM, the dentin displayed a sparse and irregular tubular pattern near the dentino-enamel junction (DEJ) and only few or no tubular structures in the area corresponding to the circumpulpal dentin. Between these two areas, cleft-like structures were characteristically noted. Structural irregularities in the dentinal tubules were also shown with SEM observation. XMA demonstrated that the distribution of both Ca and P in the dentin of DI teeth was apparently lower than that in the normal deciduous incisor used as a control. Specifically, an area along EDJ at a distance of 25-35 microns, corresponding to the mantle dentin, revealed extremely low or no distribution of the both elements. From the present observation, it is suggested that the generic disorder mainly involved in the primary odontoblasts and consequently results in the disturbance of calcification, especially that mediated by the matrix vesicles, and shortening of the cell life. After the death of these cells, the cells originate in, from the undifferentiated pulp cells may participate in the deposition of another irregular dentin.

Calcium↗
PubMedDate not supplied

Hereditary dentinogenesis imperfecta: a treatment program using an overdenture.

The aim of treatment in cases of dentinogenesis imperfecta is to improve the esthetic appearance and maintain the oral masticatory apparatus in a healthy and functional state. In the growing child, it was decided to maintain the teeth for as long as possible under an overdenture, until such time when a permanent prosthetic solution can be decided upon.

Child↗
PubMed1992

Type II collagen defect in two sibs with the Goldblatt syndrome, a chondrodysplasia with dentinogenesis imperfecta, and joint laxity.

We report on a syndrome of spondylo-epimetaphyseal dysplasia, dentinogenesis imperfecta, and ligamentous hyperextensibility in two sibs born to nonconsanguineous parents. This chondrodysplasia was characterized by severe shortness of stature and an osteoporosis without fractures. Electron microscopic examination of the cartilage documented large vacuoles of dilated rough endoplasmic reticulum within the cytoplasm of chondrocytes. Gel electrophoresis of pepsin-soluble collagen extracted from cartilage demonstrated the presence of type II collagen chains with an abnormal mobility. Prolyl and lysyl hydroxylations were slightly increased. The abnormal molecules melted at a higher temperature than the normal ones. CNBr peptide mapping of type II collagen showed an altered electrophoretic migration of peptides CB 11, CB 8, and CB 10,5 whereas CB 9,7 looked normal. In addition, two small non-collagenous proteins isolated from cartilage were not found in an age-matched control individual but were detected in a normal newborn infant. The quantitation of proline-labelled collagen synthesized by dermal fibroblasts demonstrated a 50% reduction of total collagen. This decrease essentially affected the amount of extracellular type I collagen, which was secreted less efficiently than in control cells. Nevertheless, type I collagen chains behaved normally on 5% polyacrylamide gels. The reduced mRNA levels of alpha 1I and alpha 2I chains might reflect either a transcriptional defect or a decreased stability of mRNA transcripts. We suggest that the association of both pathological chondrocytes producing altered collagen type II and decreased synthesis of type I could be responsible for this peculiar phenotype. The overmodification of alpha 1II CNBr peptides is consistent with the presence of a single-base substitution in the COL2A1 gene. Whether there is a direct causal relationship between the type II collagen defect and the underexpression of type I collagen will require clarification.

Abnormalities, Multiple↗
PubMedDate not supplied

[Multidisciplinary focus on dentinogenesis imperfecta type II. Clinical analysis. Ultrastructural and genetic pathology].

A review of the more relevant clinical, radiological, histopathological and genetics aspects of Dentinogenesis imperfecta (DI) is presented, together with the description of a family with DI. The complete analysis of the affected and non-affected members showed that the defect can be classified as a DI type II with an autosomal dominant mode of inheritance with complete penetrance and variable expressivity. Also it is necessary to emphasize the importance of a multidisciplinary approach (Pedodontists, Oral Pathologists and geneticists) in the description, diagnosis and treatment of the individuals affected with DI.

Adult↗
PubMed1992

Dentin phosphoprotein in dentin development: implications in dentinogenesis imperfecta.

Dentin phosphoprotein (DPP, phosphophoryn) is the major non-collagenous protein component of the dentin extracellular matrix. This highly acidic phosphorylated protein is solely expressed by ectomesenchymal-derived odontoblast cells of the tooth organ. Previous biochemical studies have suggested the absence of this protein associated with the human genetic disease dentinogenesis imperfecta (DGI) Types I and II. However, due to the normal degradation of human DPP during dentin maturation, it has not been possible to establish if these reported differences were due to changes in DPP expression or secondary degradation rates in DGI affected versus normal teeth. Recently, we have taken both a molecular and biochemical approach to address this problem. Molecular studies have utilized genetic linkage studies performed on several multi-generation informative DGI kindreds. These studies have determined linkage between DGI Types II and III and two markers localized to the long arm of human chromosome 4 in the region 4q11-4q21. The strategy used in our study was to map the DPP gene locus to the long arm of human chromosome 4, in the same region as DGI, using a DPP oligonucleotide probe and somatic hybrid cell lines. The results indicate DPP is not localized to any region of human chromosome 4. Our data indicates that a mutation within the DPP gene locus is not associated with DGI Types II or III. This data is supported by the identification of human DPP (95 kDa) within the dentin extracellular matrix of molars isolated from an affected DGI type II patient using a mouse anti-DPP antibody. However, this does not exclude the possibility that enzymes associated with DPP post-translational modifications (ie. phosphorylation or degradation) might be responsible for this genetic disease.

Animals↗