Histological distribution of phosphophoryn in normal and pathological human dentins

Takagi, Yasuaki; Sasaki, Satoshi

doi:10.1111/j.1600-0714.1986.tb00659.x

Cited by 52 publications

(32 citation statements)

References 25 publications

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“…DSP is a glycoprotein also present in dentin in low but measurable quantities (5-7). As early as 1988 it was suggested that mutations to the "dentin" phosphophoryn (sic) gene locus were a causative factor in DI-II (8,9). DI-II has been mapped to 4q21-q23 by linkage studies (10), which are consistent with the mapping of the human DSPP gene locus to chromosome 4q21.3 (4).…”

mentioning

confidence: 77%

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Paine

Luo

Wang

et al. 2005

Journal of Biological Chemistry

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The gene for dentin sialophosphoprotein produces a single protein that is post-translationally modified to generate two distinct extracellular proteins: dentin sialoprotein and dentin phosphoprotein. In teeth, dentin sialophosphoprotein is expressed primarily by odontoblast cells, but is also transiently expressed by presecretory ameloblasts. Because of this expression profile it appears that dentin sialophosphoprotein contributes to the early events of amelogenesis, and in particular to those events that result in the formation of the dentinoenamel junction and the adjacent "aprismatic" enamel. Using a transgenic animal approach we have extended dentin sialoprotein or dentin phosphoprotein expression throughout the developmental stages of amelogenesis. Overexpression of dentin sialoprotein results in an increased rate of enamel mineralization, however, the enamel morphology is not significantly altered. In wildtype animals, the inclusion of dentin sialoprotein in the forming aprismatic enamel may account for its increased hardness properties, when compared with bulk enamel. In contrast, the overexpression of dentin phosphoprotein creates "pitted" and "chalky" enamel of nonuniform thickness that is more prone to wear. Disruptions to the prismatic enamel structure are also a characteristic of the dentin phosphoprotein overexpressing animals. These data support the previous suggestion that dentin sialoprotein and dentin phosphoprotein have distinct functions related to tooth formation, and that the dentino-enamel junction should be viewed as a unique transition zone between enamel and the underlying dentin. These results support the notion that the dentin proteins expressed by presecretory ameloblasts contribute to the unique properties of the dentino-enamel junction.Dentin is an ectomesenchymal derived, collagen containing, calcified tissue that forms the major part of the tooth. Genetic diseases that result in abnormal dentin are classified in a subgrouping of dentinogenesis imperfecta. Dentinogenesis imperfecta type I (DI-I) 1 is always associated with one of the osteogenesis imperfectas, where mutations have been characterized in the following collagens: COL1A1, COL1A2, COL5A1, and COL2A1 (1), whereas dentinogenesis imperfecta type II (DI-II) is a disorder in dentin mineralization. Dentinogenesis imperfecta type III (DI-III) has a more extreme abnormal dental phenotype that impacts beyond dentin to the enamel and the pulps of affected teeth (2, 3).In dentin, two of the noncollagenous dentin matrix proteins are dentin siaolprotein (DSP) and dentin phosphoprotein (DPP). Both DSP and DPP are products of a single gene called dentin sialophosphoprotein (DSPP). Following transcription and translation of DSPP, the resulting product is post-translational cleaved to produce DSP and DPP that are primarily expressed in the dentin matrix (4). DPP (also known as phosphophoryn) is a highly acidic protein and is the major noncollagenous matrix component of dentin (ϳ90% of the dentin matrix is collagen) (5, 6). DSP is a glyco...

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mentioning

confidence: 77%

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Paine

Luo

Wang

et al. 2005

Journal of Biological Chemistry

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“…In rat teeth, Gla proteins of the osteocalcin type can be demonstrated by immunostaining in newly differentiated odontoblasts as well as in predentin before initiation of mineralization (Bronckers etal., 1987;Gorter de Vries etal., 1987); the staining in mantle dentin is reportedly restricted to mineralized globular patches (Camarda et al, 1987). Also dentin phosphoprotein seems to be absent from mantle dentin (Nakamura et al, 1985;Takagi and Sasaki, 1986;Rahima et al, 1988).…”

Section: Cellsmentioning

confidence: 98%

Dentinogenesis

Linde

Goldberg

1993

Critical Reviews in Oral Biology & Medicine

428

333

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The formation of dentin, dentinogenesis, comprises a sophisticated interplay between several factors in the tissue, cellular as well as extracellular. Dentin may be regarded as a calcified connective tissue. In this respect, as well as in its mode of formation, it is closely related to bone. Using dentinogenesis as an experimental model to study biomineralization provides several practical advantages, and the results may be extrapolated to understand similar processes in other tissues, primarily bone. After describing dentin structure and composition, this review discusses items such as the morphology of dentinogenesis; the dentinogenically active odontoblast, transport, and concentrations of mineral ions; the constituents of the dentin organic matrix; and the presumed mechanisms involved in mineral formation.

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“…8B shows the ion distributions in coronal molar dentin after demineralization with 0.5 M acetic acid for 1 h in the presence of cross-linking fixative. This acetic acid etching treatment was used for demineralization preparatory to immunohistochemical localization of the dentin noncollagenous protein-phosphophoryn (Rahima et al, 1988) and relied on the fact that phosphophoryn is not readily soluble in acetic acid (Butler et al, 1972;Takagi and Sasaki, 1986) as well as the cross-linking insolubilization of the proteins by the glutaraldehyde and formaldehyde. The total positive ion image presented in Fig.…”

Section: Demineralizationmentioning

confidence: 99%

The composition and structure of bovine peritubular dentin: Mapping by time of flight secondary ion mass spectroscopy

Gotliv

Robach

Veis

2006

Journal of Structural Biology

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Histological distribution of phosphophoryn in normal and pathological human dentins

Cited by 52 publications

References 25 publications

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Dentinogenesis

The composition and structure of bovine peritubular dentin: Mapping by time of flight secondary ion mass spectroscopy

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