Dentin Sialoprotein (DSP) Has Limited Effects on In Vitro Apatite Formation and Growth

Boskey, Adele L.; Spevak, Lyudmila; Tan, M.; Doty, Stephen B.; Butler, William T.

doi:10.1007/s002230001169

Cited by 85 publications

(82 citation statements)

References 38 publications

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“…Interestingly, a maximum in calcium phosphate amounts nucleated occurred at 6.5 μg/mL amelogenin and then the amounts precipitated decreased as the amelogenin concentration increased up to 130 μg/mL. This has been observed for other proteins and molecules, where a maximum in amounts of calcium phosphate precipitated in the presence of polyglutamic acid was ~15 μg/mL protein [27], in the presence of dentin sialoprotein at 5 μg/mL [28] and in the presence of citric acid at ratios of 2-12 calcium ions per citric acid molecule [25]. Other studies have shown that high concentrations of amelogenin (15 mg/mL) in a gel matrix [20] and high concentrations of phosphophoryn (100 μg/mL) [29] inhibited calcium phosphate nucleation.…”

Section: Nucleation Behaviormentioning

confidence: 58%

The nucleation and growth of calcium phosphate by amelogenin

Tarasevich

Howard

Larson

et al. 2007

Journal of Crystal Growth

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The nucleation processes involved in calcium phosphate formation in tooth enamel are not well understood but are believed to involve proteins in the extracellular matrix. The ability of one enamel protein, amelogenin, to promote the nucleation and growth of calcium phosphate was studied in an in vitro system involving metastable supersaturated solutions. It was found that recombinant amelogenin (rM179 and rp(H)M180) promoted the nucleation of calcium phosphate compared to solutions without protein. The amount of calcium phosphate increased with increasing supersaturation of the solutions and increasing protein concentrations up to 6.5 μg/mL. At higher protein concentrations, the amount of calcium phosphate decreased. The kinetics of nucleation was studied in situ and in real time using a quartz crystal microbalance (QCM) and showed that the protein reduced the induction time for nucleation compared to solutions without protein. This work shows a nucleation role for amelogenin in vitro which may be promoted by the association of amelogenin into nanosphere templates, exposing charged functionality at the surface.

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Section: Nucleation Behaviormentioning

confidence: 58%

The nucleation and growth of calcium phosphate by amelogenin

Tarasevich

Howard

Larson

et al. 2007

Journal of Crystal Growth

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“…Two X-Asp bonds are also cleaved in the posttranslational processing of dentin sialophosphoprotein (34). Dentin sialoprotein is a relatively weak HA nucleator (35), whereas dentin phosphoprotein is an extremely effective nucleator (24). Dentin sialoprotein and dentin phosphoprotein exist as individual proteins and are not co-localized in mineralizing tissues (36).…”

Section: Resultsmentioning

confidence: 99%

In Vitro Effects of Dentin Matrix Protein-1 on Hydroxyapatite Formation Provide Insights into in Vivo Functions

Tartaix

Doulaverakis

George

et al. 2004

Journal of Biological Chemistry

174

146

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Dentin matrix protein-1 (DMP1) is a mineralized tissue matrix protein synthesized by osteoblasts, hypertrophic chondrocytes, and ameloblasts as well as odontoblasts. DMP1 is believed to have multiple in vivo functions, acting both as a signaling molecule and a regulator of biomineralization. Using a cell-free system in vitro, we evaluated the action of DMP1 in the regulation of hydroxylapatite (HA) formation and crystal growth. The non-phosphorylated recombinant protein acted as an HA nucleator, increasing the amount of mineral formed in a gelatin gel HA growth system relative to protein-free controls. The recombinant protein phosphorylated in vitro had no detectable effect on HA formation and growth. In contrast, phosphorylated bovine DMP1 expressed in marrow stromal cells with an adenovirus vector containing 29.7 phosphates/mol was an effective inhibitor of HA formation and growth. The native full-length protein appeared to be absent or present in only small amounts in the extracellular matrix of bones and teeth. However, two highly phosphorylated fragments representing the N-and C-terminal portions of DMP1 have been identified, apparently arising from proteolytic cleavage of four X-Asp bonds. The highly phosphorylated C-terminal 57-kDa fragment (containing 42 phosphates/mol), like the non-phosphorylated DMP1, was an HA nucleator. These data suggest that, in its native form, DMP1 inhibits mineralization, but when cleaved or dephosphorylated, it initiates mineralization. These in vitro data are consistent with the findings in the DMP1 knockout mouse.Dentin matrix protein-1 (DMP1) 1 is an acidic, phosphorylated, integrin-binding extracellular matrix protein first identified by screening a rat cDNA library (1). Northern blot analysis in the rat originally suggested that the DMP1 message was odontoblast-specific, with in situ hybridization showing DMP1 mRNA expression to be restricted to those fully differentiated odontoblasts engaged in active dentin matrix formation, with transient expression by ameloblasts (1, 2). More recent in situ hybridization studies show a much broader pattern of expression of DMP1, with expression associated with a number of mineralizing tissues, including bone and cementum (3). In rat and chicken bone, immunohistochemical detection showed an association of DMP1 with osteocytes, but not with osteoblasts (4). In the mouse, hypertrophic chondrocytes express more DMP1 than other cell types (5). DMP1 was detected at high levels by Northern analysis in fetal bovine brain and cultured long bone as well as in odontoblasts (6). Most recently, DMP1 was localized by immunohistochemistry in human lung cancer tissue (7).DMP1 is a small protein that has been postulated to have a high affinity for hydroxylapatite (HA) (8,9). This coupled with its localization in mineralized tissues suggested that DMP1 could have an important role in mineralization. DMP1 is a member of the SIBLING (small integrin-binding ligand, Nlinked glycoprotein) family of proteins (10, 11). Like other members of the SIBLING family...

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“…23 On the other hand, DSP has still unclear functions but is involved in mineral nucleation. 17,[24][25][26] The DSPPs are encoded by a 5-exon gene. Exons 2, 3, 4 and the beginning of exon 5 encode for DSP.…”

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

101

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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Dentin Sialoprotein (DSP) Has Limited Effects on In Vitro Apatite Formation and Growth

Cited by 85 publications

References 38 publications

The nucleation and growth of calcium phosphate by amelogenin

The nucleation and growth of calcium phosphate by amelogenin

In Vitro Effects of Dentin Matrix Protein-1 on Hydroxyapatite Formation Provide Insights into in Vivo Functions

Isolated dentinogenesis imperfecta and dentin dysplasia: revision of the classification

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