Dentin phosphoprotein compound mutation in dentin sialophosphoprotein causes dentinogenesis imperfecta type III

2004 ◽  
Vol 132A (3) ◽  
pp. 305-309 ◽  
Author(s):  
Juan Dong ◽  
TingTing Gu ◽  
Leticia Jeffords ◽  
Mary MacDougall
Keyword(s):  
Dentinogenesis Imperfecta ◽  
Dentin Sialophosphoprotein ◽  
Type Iii ◽  
Dentin Phosphoprotein ◽  
Compound Mutation

scholarly journals Dentin Sialophosphoprotein Knockout Mouse Teeth Display Widened Predentin Zone and Develop Defective Dentin Mineralization Similar to Human Dentinogenesis Imperfecta Type III

2003 ◽  
Vol 278 (27) ◽  
pp. 24874-24880 ◽  
Author(s):  
Taduru Sreenath ◽  
Tamizchelvi Thyagarajan ◽  
Bradford Hall ◽  
Glenn Longenecker ◽  
Rena D'Souza ◽  
...  
Keyword(s):  
Knockout Mouse ◽  
Dentinogenesis Imperfecta ◽  
Dentin Sialophosphoprotein ◽  
Type Iii ◽  
Dentin Mineralization

scholarly journals Effects of DSPP Gene Mutations on Periodontal Tissues

2021 ◽  
Author(s):  
Zhaojun Jing ◽  
Zhibin Chen ◽  
Yong Jiang
Keyword(s):  
Alveolar Bone ◽  
Gene Mutations ◽  
Specific Protein ◽  
Dentinogenesis Imperfecta ◽  
Dentin Sialophosphoprotein ◽  
Periodontal Tissues ◽  
Furcation Involvement ◽  
Almost All ◽  
Alveolar Bone Defect ◽  
Deficient Mice

AbstractDentin sialophosphoprotein (DSPP) gene mutations cause autosomal dominantly inherited diseases. DSPP gene mutations lead to abnormal expression of DSPP, resulting in a series of histological, morphological, and clinical abnormalities. A large number of previous studies demonstrated that DSPP is a dentinal-specific protein, and DSPP gene mutations lead to dentin dysplasia and dentinogenesis imperfecta. Recent studies have found that DSPP is also expressed in bone, periodontal tissues, and salivary glands. DSPP is involved in the formation of the periodontium as well as tooth structures. DSPP deficient mice present furcation involvement, cementum, and alveolar bone defect. We speculate that similar periodontal damage may occur in patients with DSPP mutations. This article reviews the effects of DSPP gene mutations on periodontal status. However, almost all of the research is about animal study, there is no evidence that DSPP mutations cause periodontium defects in patients yet. We need to conduct systematic clinical studies on DSPP mutation families in the future to elucidate the effect of DSPP gene on human periodontium.

The Expression of Dentin Sialophosphoprotein Gene in Bone

2002 ◽  
Vol 81 (6) ◽  
pp. 392-394 ◽  
Author(s):  
C. Qin ◽  
J.C. Brunn ◽  
E. Cadena ◽  
A. Ridall ◽  
H. Tsujigiwa ◽  
...  
Keyword(s):  
Specific Protein ◽  
Regulatory Mechanisms ◽  
Long Bone ◽  
Mrna Transcript ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Dentin Sialophosphoprotein ◽  
Dentin Phosphoprotein ◽  
Polymerase Chain ◽  
Dentin Sialoprotein

Dentin sialoprotein (DSP) and dentin phosphoprotein (DPP) are expressed as a single mRNA transcript coding for a large precursor protein termed dentin sialophosphoprotein (DSPP). DSP, DPP, and DSPP have been considered to be tooth-specific. To test for the expression of the dspp gene in bone, we performed Western immunoblots and reverse-transcription polymerase chain-reaction (RT-PCR). With Western immunoblots, we detected DSP in the Gdm/EDTA extracts of rat long bone, at a level of about 1/400 of that in dentin. Using RT-PCR, we detected DSPP mRNA in mouse calvaria. Similar to Western immunoblots, the results of RT-PCR indicated that the dspp gene is expressed at a lower level in bone than in dentin and odontoblasts. Analysis of the data shows that DSPP is not a tooth-specific protein, and that dramatically different regulatory mechanisms governing DSPP expression are involved in the bone and dentin.

Dentinogenesis imperfecta type III with enamel and cementum defects

1985 ◽  
Vol 59 (5) ◽  
pp. 505-510 ◽  
Author(s):  
Suzanne Clergeau-Guerithault ◽  
Jean R. Jasmin
Keyword(s):  
Dentinogenesis Imperfecta ◽  
Type Iii

scholarly journals Mutant Dentin Sialophosphoprotein Causes Dentinogenesis Imperfecta

2019 ◽  
Vol 98 (8) ◽  
pp. 912-919 ◽  
Author(s):  
T. Liang ◽  
H. Zhang ◽  
Q. Xu ◽  
S. Wang ◽  
C. Qin ◽  
...  
Keyword(s):  
Dental Pulp ◽  
Matrix Protein ◽  
Mutant Mice ◽  
Extracellular Matrix Protein ◽  
Dentinogenesis Imperfecta ◽  
Wild Type ◽  
Pulp Chamber ◽  
Dentin Sialophosphoprotein ◽  
In The Wild

Dentin sialophosphoprotein (DSPP) is an extracellular matrix protein highly expressed by odontoblasts in teeth. DSPP mutations in humans may cause dentinogenesis imperfecta (DGI), an autosomal dominant dentin disorder. We recently generated a mouse model (named “ DsppP19L/+ mice”) that expressed a mutant DSPP in which the proline residue at position 19 was replaced by a leucine residue. We found that the DsppP19L/+ and DsppP19L/P19L mice at a younger age displayed a tooth phenotype resembling human DGI type III characterized by enlarged dental pulp chambers, while the teeth of older DsppP19L/+ and DsppP19L/P19L mice had smaller dental pulp chambers mimicking DGI type II. The teeth of DsppP19L/+ and DsppP19L/P19L mice had a narrower pulp chamber roof predentin layer, thinner pulp chamber roof dentin, and thicker pulp chamber floor dentin. In addition, these mice also had increased enamel attrition, accompanied by excessive deposition of peritubular dentin. Immunohistochemistry, in situ hybridization, and real-time polymerase chain reaction analyses showed that the odontoblasts in both DsppP19L/+ and DsppP19L/P19L mice had reduced DSPP expression, compared to the wild-type mice. We also observed that the levels of DSPP expression were much higher in the roof-forming odontoblasts than in the floor-forming odontoblasts in the wild-type mice and mutant mice. Moreover, immunohistochemistry showed that while the immunostaining signals of dentin sialoprotein (N-terminal fragment of DSPP) were decreased in the dentin matrix, they were remarkably increased in the odontoblasts of the DsppP19L/+ and DsppP19L/P19L mice. Consistently, our in vitro studies showed that the secretion of the mutant DSPP was impaired and accumulated within endoplasmic reticulum. These findings suggest that the dental phenotypes of the mutant mice were associated with the intracellular retention of the mutant DSPP in the odontoblasts of the DSPP-mutant mice.

scholarly journals Expression of Dentin Sialophosphoprotein in Non-mineralized Tissues

2011 ◽  
Vol 59 (11) ◽  
pp. 1009-1021 ◽  
Author(s):  
Monica Prasad ◽  
Qinglin Zhu ◽  
Yao Sun ◽  
Xiaofang Wang ◽  
Ashok Kulkarni ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Real Time ◽  
Real Time Pcr ◽  
Soft Tissues ◽  
Dentin Sialophosphoprotein ◽  
Mineralized Tissues ◽  
Dentin Phosphoprotein ◽  
Liver And Kidney ◽  
Polymerase Chain ◽  
Dentin Sialoprotein

Dentin sialophosphoprotein (DSPP) and its cleaved products, dentin phosphoprotein (DPP) and dentin sialoprotein (DSP), play important roles in biomineralization. Believed to be tooth specific, the authors’ group revealed its expression in bone, and more recently, they and other groups also showed its expression in a few types of soft tissues. In this study, the authors systematically examined the expression of DSPP in a variety of non-mineralized tissues using reverse-transcription polymerase chain reaction (RT-PCR), real-time PCR, Western immunoblotting, and immunohistochemistry analyses in wild-type mice as well as β-galactosidase assays in the Dspp lacZ knock-in mice. These approaches showed the presence of DSPP in the salivary glands, cartilage, liver, kidney, and brain and its absence in the heart and spleen. Real-time PCR showed that the expression levels of DSPP mRNA in salivary glands, cartilage, liver, and kidney were higher than in the bone. Interestingly, DSPP was observed in the pericytes of blood vessels in the dental pulp, which are believed to be able to differentiate into odontoblasts. On the basis of these observations, the authors conclude that DSPP and/or its cleaved products may fulfill important functions in certain non-mineralized tissues in addition to its role in biomineralization.

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