The Non-collagenous Dentin Matrix Proteins are Involved in Dentinogenesis Imperfecta Type II (DGI-II)

@article{Thotakura2000TheND,
  title={The Non-collagenous Dentin Matrix Proteins are Involved in Dentinogenesis Imperfecta Type II (DGI-II)},
  author={Sushma Thotakura and T. Mah and Rajini Srinivasan and Yuzo Takagi and Arthur Veis and A George},
  journal={Journal of Dental Research},
  year={2000},
  volume={79},
  pages={835 - 839},
  url={https://api.semanticscholar.org/CorpusID:38418321}
}
This study suggests that the different restriction enzyme digestion profiles of the DNA from the D GI-II patient, as probed by DMP2, might be related to the defective mineralization of dentin in DGI-II.
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These findings offer an explanation of how structural changes in the dentin could be responsible for the failure of some adhesive restorative materials as observed in patients affected by OIDI.

Differential expression patterns of the dentin matrix proteins during mineralized tissue formation.

A Novel DSPP Mutation in Dentinogenesis Imperfecta Shields Type II: Clinical, Genetic and Stem Cell Perspectives

Intrafibrillar Mineral May be Absent in Dentinogenesis Imperfecta Type II (DI-II)

High-resolution synchrotron radiation computed tomography and small-angle x-ray scattering data are consistent with an absence of intrafibrillar mineral in DI-II dentin.

Physiology of dentinogenesis and pathophysiology of dentinogenesis imperfecta: how does it affect dentin structure and biomechanics?

To the Editor

    Medicine
  • 2000
It is concluded that the DMP2 probe produced the most "dramatic shift in the restriction pattern", this gene "might be related to the defective mineralization of dentin in DGI-II", and that the polymorphism in the D MP2 gene was the most distinctive.

The authors reply

It is concluded that the DMP2 probe produced the most "dramatic shift in the restriction pattern", this gene "might be related to the defective mineralization of dentin in DGI-II", and that the polymorphism in the D MP2 gene was the most distinctive.

Study of the Maturation of the Organic (Type I Collagen) and Mineral (Nonstoichiometric Apatite) Constituents of a Calcified Tissue (Dentin) as a Function of Location: A Fourier Transform Infrared Microspectroscopic Investigation

Results showed that dentin apatite became increasingly mature (stoichiometric) from the mineralization front toward the enamel, especially through loss of HPO42− groups and vacancies, suggesting that intrafibrillar mineralization partially dehydrated the collagen.

Dentin Matrix Protein 1 Regulates Dentin Sialophosphoprotein Gene Transcription during Early Odontoblast Differentiation*

It is demonstrated that dentin matrix protein 1 (DMP1), which is localized in the nucleus during early differentiation of odontoblasts, is able to bind specifically with the DSPP promoter and activate its transcription.

Multiple teeth fractures in dentinogenesis imperfecta: a case report.

The multiple fractures of DGI-affected teeth are presented and the reason of low fracture resistance is suggested to be attributed to the poorly woven microstructure of their dentin, which leads to a reduction in hardness.

27 References

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

The 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 D GI type II or DGI type III, and the data do not exclude the possibility that other proteinsassociated with DPP posttranslational modifications might be responsible for this genetic disease.

Relation of mineralization defects in collagen matrices to noncollagenous protein components. Identification of a molecular defect in dentinogenesis imperfecta.

Comparisons of the NCP in normal human dentin and dentinogenesis imperfecta Type II (hereditary opalescent dentin) dentin imply that dentin phosphophoryn may be related in function to the mineralization process.

Genetic mapping of the dentinogenesis imperfecta type II locus.

The presence of a marker that shows no recombination with the DGI-II phenotype between the flanking markers provides an important anchor point for the creation of physical continuity across the D GI-II candidate region.

Gene Expression Patterns of Murine Dentin Matrix Protein 1 (Dmp1) and Dentin Sialophosphoprotein (DSPP) Suggest Distinct Developmental Functions In Vivo

The in vivo temporospatial expression patterns of two dentin NCP genes, dentin matrix protein 1 (Dmp1), and dentin sialophosphoprotein (DSPP) in developing molars are compared, implying that these molecules serve different biological functions in vivo.

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

Both types of DI have a common primary disturbance in the early stage of odontoblast differentiation, suggesting similar deficiency in phosphophoryn concentration.

The ultrastructure of the dental tissues in dentinogenesis imperfecta in man.

Histological distribution of phosphophoryn in normal and pathological human dentins.

It is suggested that phosphophoryn is synthesized and secreted only by physiologically-differentiated odontoblasts and that the mineralization processes of mantle, secondary, reparative and DI dentins may be different from that of circumpulpal orthodentin.

Elucidation of the sequence and the genomic organization of the human dentin matrix acidic phosphoprotein 1 (DMP1) gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II.

Sequencing of each of the coding exons in individuals affected by dentinogenesis imperfecta type II failed to reveal any disease-specific mutations, suggesting that mutations in DMP1 are not causative of this condition at least in the two families examined in this study.

Rat dentin matrix protein 3 is a compound protein of rat dentin sialoprotein and phosphophoryn.

Another clone of the rat incisor phosphophoryn gene is sequenced, which appears to be bifunctional, or at minimum, has two distinct domains and is named Dmp3, in keeping with the current nomenclature adopted in the laboratory.

Genomic organization of the human osteopontin gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II.

A highly informative short tandem repeat polymorphism isolated at the SPP1 locus showed no recombination with the autosomal dominant disorder dentinogenesis imperfecta type II, and sequencing of each exon in individuals affected by this disorder failed to reveal any disease-specific mutations.