Isolation, Characterization and Immunolocalization of a 53-kDal Dentin Sialoprotein (DSP)

Butler, William T.; Bhown, Meera; Brunn, Jan C.; D’Souza, Rena N.; Farach-Carson, Mary C.; Happonen, Risto Pekka; Schrohenloher, Ralph E.; Seyer, Jerome M.; Somerman, Martha J.; Foster, Ruth A.; Tomana, Milan; Dijk, Simon van

doi:10.1016/s0934-8832(11)80030-2

Cited by 137 publications

(136 citation statements)

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“…6G) were expressed, respectively, in dental mesenchyme and epithelium of the chimera teeth. Dentin sialoprotein, a noncollagenous extracellular matrix protein produced by odontoblasts (28) and osteoblasts (29), was detected in ectomesenchymal cells and the mineralized matrix (Fig. 6H).…”

Section: Resultsmentioning

confidence: 99%

Development of teeth in chick embryos after mouse neural crest transplantations

Mitsiadis

Chéraud

Sharpe

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

110

103

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Teeth were lost in birds 70 -80 million years ago. Current thinking holds that it is the avian cranial neural crest-derived mesenchyme that has lost odontogenic capacity, whereas the oral epithelium retains the signaling properties required to induce odontogenesis. To investigate the odontogenic capacity of ectomesenchyme, we have used neural tube transplantations from mice to chick embryos to replace the chick neural crest cell populations with mouse neural crest cells. The mouse͞chick chimeras obtained show evidence of tooth formation showing that avian oral epithelium is able to induce a nonavian developmental program in mouse neural crestderived mesenchymal cells.

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Section: Resultsmentioning

confidence: 99%

Development of teeth in chick embryos after mouse neural crest transplantations

Mitsiadis

Chéraud

Sharpe

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

110

103

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“…The two acidic proteins, DSP and DPP, are individual, distinctive proteins that are found in abundance in the ECM of dentin (Dickson et al, 1975;DiMuzio and Veis, 1978;Butler, 1987;Butler et al, 1992). It appeared that they had no relationship to each other, an idea that changed when results from cDNA cloning and sequencing of a mouse mRNA library showed that DSP and DPP are derived from the same precursor, DSPP (MacDougall et al, 1997).…”

Section: (4) Dsppmentioning

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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“…Cloning and characterization of the first DPP cDNA transcript revealed the extreme redundancy of its DNA and deduced amino acid sequences (17). Surprisingly, the cloned DPP transcript also encoded DSP, another major noncollagenous protein in dentin (18,19). DSP is a highly glycosylated proteoglycan (19 -21).…”

Section: Dentin Sialophosphoprotein (Dspp)mentioning

confidence: 99%

Dentin Sialophosphoprotein Is Processed by MMP-2 and MMP-20 in Vitro and in Vivo

Yamakoshi

Iwata

et al. 2006

Journal of Biological Chemistry

116

135

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Dentin sialophosphoprotein (DSPP) is a major secretory product of odontoblasts and is critical for proper tooth dentin formation. During dentinogenesis, DSPP is proteolytically cleaved into smaller subunits. These cleavages are proposed activation steps, and failure to make these cleavages is a potential cause of developmental tooth defects. We tested the hypothesis that dentin-resident matrix metalloproteinases catalyze the cleavages that process DSPP. We defined the exact DSPP cleavages that are catalyzed by proteases during crown formation by isolating DSPP-derived proteins from developing porcine molars and characterizing their N-terminal sequences and apparent size on SDS-PAGE and Western blots. The in vivo DSPP cleavage sites were on the N-terminal sides of Thr Dentin sialophosphoprotein (DSPP)2 is a multidomain extracellular matrix protein that is critical for proper dentin formation. The major DSPP domains are dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP) (1-3). In humans, nine disease-causing mutations in the DSPP gene on chromosome 4q21.3 have been reported in kindreds with isolated inherited dentin defects (4 -10). No other genes have been implicated in their etiology by mutation analyses. DSPP mutations result in a variety of dental phenotypes, including dentin dysplasia type II and dentinogenesis imperfecta types II and III. In mice, targeted knock-out of the Dspp gene (Dspp Ϫ/Ϫ ) resulted in tooth defects resembling dentinogenesis imperfecta type III (11). DSPP is expressed in other tissues besides dentin, such as in bone (12), but the protein levels in the secondary locations are hundreds of times lower than in dentin. Outside of a poorly understood association with progressive high frequency sensorineural hearing loss, DSPP mutations result in defects limited to the teeth. Perhaps because DSPP functions are so specialized, relatively little research has been focused on it, and many of its basic structural features are still unknown. DSPP itself has never been isolated or detected in dentin extracts. DSPP was discovered through its proteolytic cleavage products, starting with DPP (13). DPP is a highly acidic phosphoprotein with an isoelectric pH of 1.1 (14). Besides its distinctive amino acid composition, dominated by serine and aspartic acid (15), DPP has a conserved N-terminal sequence of AspAsp-Pro-Asn (1). DPP is difficult to study at the protein level, because it is resistant to digestion by proteases, such as trypsin (16). Cloning and characterization of the first DPP cDNA transcript revealed the extreme redundancy of its DNA and deduced amino acid sequences (17). Surprisingly, the cloned DPP transcript also encoded DSP, another major noncollagenous protein in dentin (18,19). DSP is a highly glycosylated proteoglycan (19 -21). Demonstration of a continuous open reading frame between the DSP and DPP coding regions disclosed that DSP and DPP are cleavage products of a larger protein, called DSPP (22). DGP is the most recent and smallest DSPP-derived pro...

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Isolation, Characterization and Immunolocalization of a 53-kDal Dentin Sialoprotein (DSP)

Cited by 137 publications

References 1 publication

Development of teeth in chick embryos after mouse neural crest transplantations

Development of teeth in chick embryos after mouse neural crest transplantations

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

Dentin Sialophosphoprotein Is Processed by MMP-2 and MMP-20 in Vitro and in Vivo

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