Comparative analysis of mouse DSP and DPP expression in odontoblasts, preameloblasts, and experimentally induced odontoblast‐like cells

Bègue-Kirn, Catherine; Ruch, J V; Ridall, Amy L.; Butler, William T.

doi:10.1111/j.1600-0722.1998.tb02184.x

Cited by 75 publications

(48 citation statements)

References 5 publications

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“…Some of the macromolecules secreted by the odontoblasts are proteoglycans such as decorin, biglycan, and fibromodulin; Gla proteins such as osteocalcin; members of the SIBLING family such as DMP1, DSPP, OPN, MEPE, and BSP; and other non-collagenous proteins such as amelogenin and other serum-derived proteins (Begue-Kirn et al 1998b;Ruch 1998). Among these dentin constituents, we focused on the temporal and spatial localization of three major secretory products of the odontoblasts, DMP1, DSP, and DPP, during dentinogenesis.…”

Section: Discussionmentioning

confidence: 99%

Temporal and Spatial Localization of the Dentin Matrix Proteins During Dentin Biomineralization

Hao

Ramachandran

George

2008

J Histochem Cytochem.

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S U M M A R Y Formation of bone and dentin are classical examples of matrix-mediated mineralization. The mineral phase is essentially the same in these two tissues and primarily consists of a carbonated hydroxyapatite, but the difference lies in the crystal size and shape. There are three components that are necessary for proper mineralization, namely the proper synthesis and secretion of the non-collagenous proteins (NCPs), self-assembly of the collagenous matrix, and delivery of calcium and phosphate ions to the extracellular matrix. Three major NCPs present in the dentin matrix are dentin matrix protein 1 (DMP1), dentin phosphophorin (DPP), and dentin sialoprotein (DSP). In this study, we show the temporal and spatial localization of these NCPs and correlate their expression with the presence of collagenous matrix and calcified deposits in developing mouse incisors and molars. DMP1, an acidic protein, is present predominantly at the mineralization front and in the nucleus of undifferentiated preodontoblast cells. DPP, the major NCP, is present in large amounts at the mineralization front and might function to regulate the size of the growing hydroxyapatite crystals. For the first time, we report the localization of DPP in the nucleus of preodontoblast cells, suggesting a signaling function during the odontoblast differentiation process. DSP is localized predominantly in the dentinal tubules at the site of peritubular dentin, which is highly mineralized in nature. Thus, the precise localization of DMP1, DPP, and DSP in the dentin tissue suggests that a concerted effort between several NCPs is necessary for dentin formation.

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Section: Discussionmentioning

confidence: 99%

Temporal and Spatial Localization of the Dentin Matrix Proteins During Dentin Biomineralization

Hao

Ramachandran

George

2008

J Histochem Cytochem.

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“…2b). (b) PHEX is expressed in osteoblasts, osteocytes, and odontoblasts (Du et al, 1996;Guo and Quarles, 1997;Lipman et al, 1998;Ruchon et al, 1998Ruchon et al, , 2000Thompson et al, 2002), as are DMP1 Feng et al, 2002b) and DSPP D'Souza et al, 1992;Bègue-Kirn et al, 1998;Qin et al, 2002Qin et al, , 2003c. (c) The bony and dental defects of DMP1 knock-out mice at post-natal stage (after the age of 3 wks; Feng et al, 2002a) are similar to those of XLH and Hyp, while the dental defects in the DSPP null mice (Sreenath et al, 2003) show similarities to those of XLH and Hyp.…”

Section: (5) Phex Protein a Possible Proteinase That Cleaves Dmp1 Anmentioning

confidence: 99%

Post-translational Modifications of SIBLING Proteins and Their Roles in Osteogenesis and Dentinogenesis

Qin

Baba

Butler

2004

Critical Reviews in Oral Biology & Medicine

392

360

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ABSTRACT:The extracellular matrix (ECM) of bone and dentin contains several non-collagenous proteins. One category of non-collagenous protein is termed the SIBLING (Small Integrin-Binding LIgand, N-linked Glycoprotein) family, that includes osteopontin (OPN), bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), and matrix extracellular phosphoglycoprotein (MEPE). These polyanionic SIBLING proteins are believed to play key biological roles in the mineralization of bone and dentin. Although the specific mechanisms involved in controlling bone and dentin formation are still unknown, it is clear that some functions of the SIBLING family members are dependent on the nature and extent of posttranslational modifications (PTMs), such as phosphorylation, glycosylation, and proteolytic processing, since these PTMs would have significant effects on their structure. OPN and BSP are present in the ECM of bone and dentin as full-length forms, whereas amino acid sequencing indicates that DMP1 and DSPP exist as proteolytically processed fragments that result from scission of X-Asp bonds. We hypothesized that the processing of DMP1 and DSPP is catalyzed by the PHEX enzyme, since this protein, an endopeptidase that is predominantly expressed in bone and tooth, has a strong preference for cleavage at the NH 2 -terminus of aspartyl residue. We envision that the proteolytic processing of DMP1 and DSPP may be an activation process that plays a significant, crucial role in osteogenesis and dentinogenesis, and that a failure in this processing would cause defective mineralization in bone and dentin, as observed in X-linked hypophosphatemic rickets.

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“…DSPP expression is restricted to differentiated odontoblasts (with transient expression in presecretory ameloblast). 14,27 So, DSPP-related peptides were initially qualified as dentinal-specific proteins. However, later, low levels of DSPP transcripts have been detected in mouse inner ear, 28 periodontal ligament, 29 and bone ( Â 400 less).…”

Section: Dentinogenesis and Dental Biomineralizationmentioning

confidence: 99%

Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification

Molla¹,

Fournier²,

Berdal³

2014

Eur J Hum Genet

103

134

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Dentinogenesis imperfecta is an autosomal dominant disease characterized by severe hypomineralization of dentin and altered dentin structure. Dentin extra cellular matrix is composed of 90% of collagen type I and 10% of non-collagenous proteins among which dentin sialoprotein (DSP), dentin glycoprotein (DGP) and dentin phosphoprotein (DPP) are crucial in dentinogenesis. These proteins are encoded by a single gene: dentin sialophosphoprotein (DSPP) and undergo several posttranslational modifications such as glycosylation and phosphorylation to contribute and to control mineralization. Human mutations of this DSPP gene are responsible for three isolated dentinal diseases classified by Shield in 1973: type II and III dentinogenesis imperfecta and type II dentin dysplasia. Shield classification was based on clinical phenotypes observed in patient. Genetics results show now that these three diseases are a severity variation of the same pathology. So this review aims to revise and to propose a new classification of the isolated forms of DI to simplify diagnosis for practitioners.

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Comparative analysis of mouse DSP and DPP expression in odontoblasts, preameloblasts, and experimentally induced odontoblast‐like cells

Cited by 75 publications

References 5 publications

Temporal and Spatial Localization of the Dentin Matrix Proteins During Dentin Biomineralization

Temporal and Spatial Localization of the Dentin Matrix Proteins During Dentin Biomineralization

Post-translational Modifications of SIBLING Proteins and Their Roles in Osteogenesis and Dentinogenesis

Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification

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