The Expression of Dentin Sialophosphoprotein Gene in Bone

Qin, Chunlin; Brunn, Jan C.; Cadena, Elizabeth; Ridall, Amy L.; Tsujigiwa, Hidetsugu; Nagatsuka, H.; Nagai, Noriyuki; Butler, William T.

doi:10.1177/154405910208100607

Cited by 243 publications

(195 citation statements)

References 16 publications

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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.

112

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.

112

103

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“…TNF receptor fusion protein (ENBREL) was from Amgen (Thousand Oaks, CA). DSP and dentin phosphoprotein (DPP) were extracted from rat dentin, and OPN was extracted from rat long bone cortex as we reported previously (38). Wild-type (WT) mice (C57Bl/6), NF-B p50/p52 double knock-out (dKO) mice (C57Bl/6ϫ129), and human TNF transgenic (TNF-Tg) mice (line 3647, CBAϫC57Bl/6) were used as we described previously (7,39).…”

Section: Methodsmentioning

confidence: 99%

Osteoclast Precursor Interaction with Bone Matrix Induces Osteoclast Formation Directly by an Interleukin-1-mediated Autocrine Mechanism

Yao

Xing

Qin

et al. 2008

Journal of Biological Chemistry

100

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Interleukin-1 (IL-1) and tumor necrosis factor (TNF) mediate bone resorption in a variety of diseases affecting bone. Like TNF, IL-1 is secreted by osteoclast precursors (OCPs), but unlike TNF, it does not induce osteoclast formation directly from OCPs in vitro. TNF induces IL-1 expression and activates c-Fos, a transcription factor required in OCPs for osteoclast formation. Here, we examined whether IL-1 can induce osteoclast formation directly from OCPs overexpressing c-Fos and whether interaction with bone matrix affects OCP cytokine expression. We infected OCPs with c-Fos or green fluorescent protein retrovirus, cultured them with macrophage colony-stimulating factor and IL-1 on bone slices or plastic dishes, and assessed osteoclast and resorption pit formation and expression of IL-1 by OCPs. We used a Transwell assay to determine whether OCPs secrete IL-1 when they interact with bone matrix. IL-1 induced osteoclast formation directly from c-Fos-expressing OCPs on plastic. c-Fos-expressing OCPs formed osteoclasts spontaneously on bone slices without addition of cytokines. OCPs on bone secreted IL-1, which induced osteoclast formation from c-Fos-expressing OCPs in the lower Transwell dishes. The bone matrix proteins dentin sialoprotein and osteopontin, but not transforming growth factor-␤, stimulated OCP expression of IL-1 and induced c-Fos-expressing OCP differentiation into osteoclasts. Osteoclasts eroding inflamed joints have higher c-Fos expression compared with osteoclasts inside bone. We conclude that OCPs expressing c-Fos may induce their differentiation directly into osteoclasts by an autocrine mechanism in which they produce IL-1 through interaction with bone matrix. TNF could induce c-Fos expression in OCPs at sites of inflammation in bone to promote this autocrine mechanism and thus amplify bone loss.

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“…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.…”

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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The Expression of Dentin Sialophosphoprotein Gene in Bone

Cited by 243 publications

References 16 publications

Development of teeth in chick embryos after mouse neural crest transplantations

Development of teeth in chick embryos after mouse neural crest transplantations

Osteoclast Precursor Interaction with Bone Matrix Induces Osteoclast Formation Directly by an Interleukin-1-mediated Autocrine Mechanism

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

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