A novel rat dentin mRNA coding only for dentin sialoprotein

Ritchie, Helena H.; Li, Xiurong

doi:10.1034/j.1600-0722.2001.00093.x

Cited by 14 publications

(14 citation statements)

References 23 publications

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“…DSP-only transcripts have been reported for rat (32) and pig (24), but no full-length mRNA transcripts encoding only the DPP portion of the protein have ever been identified. In the absence of selective proteolytic degradation of DSP, one might expect that DSP should be the most abundant noncollagenous protein and DPP should be expressed in almost equal amounts.…”

Section: Discussionmentioning

confidence: 99%

Porcine Dentin Sialoprotein Is a Proteoglycan with Glycosaminoglycan Chains Containing Chondroitin 6-Sulfate

Yamakoshi

Fukae

et al. 2005

Journal of Biological Chemistry

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Dentin sialoprotein (DSP) is a glycoprotein that is critical for proper tooth dentin formation, but little is known about the nature of its carbohydrate attachments and other post-translational modifications. We have isolated DSP from pig dentin and demonstrate that it is a proteoglycan. Polyclonal antibodies were raised in chicken against recombinant pig DSP, and used to identify native DSP in fractions of tooth dentin proteins extracted from developing pig molars. Amino acid analyses and characterization of lysylendopeptidase cleavage products confirmed that the purified protein was DSP, and that Arg 391 is at the DSP C terminus. On SDS-PAGE and on urea gels, DSP appeared as a smear extending from 280 to 100 kDa, but in the presence of ␤-mercaptoethanol the top of the DSP smear disappeared. The high molecular weight material was likely comprised of covalent DSP dimers connected by a disulfide bridge at Cys 205 . Oligosaccharides were released from DSP following N-and O-linked glycosidase digestions, but these digestions had little effect on the apparent molecular weight of DSP on SDS-PAGE, when compared with the significant reduction following chondroitinase ABC digestion. Glycosaminoglycanases with assorted glycosaminoglycan (GAG) cleavage specificities coupled with Western analyses of the cleaved GAG "stubs" demonstrated that the DSP GAG attachments contain chondroitin 6-sulfate, but not keratan sulfate, heparan sulfate, chondroitin, or chondroitin 4-sulfate. DSP binds biotin-labeled hyaluronic acid, and such binding is inhibited by the addition of unlabeled hyaluronic acid. We conclude that DSP is a proteoglycan and that GAG attachments are the predominant structural feature of porcine DSP.The dentin sialophosphoprotein gene (DSPP) 1 on human chromosome 4q21.3 encodes the two major noncollagenous proteins in tooth dentin: dentin sialoprotein (DSP) and dentin phosphoprotein (DPP) (1, 2), and these proteins are critical for proper dentin formation. As of this writing, eight mutations have been identified in the human DSPP gene that cause hereditary dentin defects (3-7). In each case, the phenotype is inherited in an autosomal dominant pattern and is usually limited to the teeth. Occasionally the condition is associated with progressive neurosensory high frequency hearing loss (DFNA39/DGI1, MIM 605594). In addition, DSPP-null mice developed dentin defects in the absence of other symptoms (8).Whereas it is known that DSPP gene products are essential for normal dentin biomineralization, DSP structural features are only partially characterized, and its functions are unknown.Much of our current understanding of the structure and function of dentin sialoprotein comes from studies of the rat protein (9 -11). Rat DSP is the N-terminal portion of DSPP and is generated by proteolytic cleavages, primarily after Tyr 421 but also following His 406 (12). The molecular mass of the major rat DSP component, which contains 29.6% carbohydrate, was determined by sedimentation equilibrium analysis to be 52.57 kDa (13), although t...

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Section: Discussionmentioning

confidence: 99%

Porcine Dentin Sialoprotein Is a Proteoglycan with Glycosaminoglycan Chains Containing Chondroitin 6-Sulfate

Yamakoshi

Fukae

et al. 2005

Journal of Biological Chemistry

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“…Two studies reported the isolation of cDNA clones that coded only for DSP in rat [27] and porcine [28]. No studies have ever shown convincing evidence that a DSPP transcript undergoes alternative splicing.…”

Section: Gene Structure and Regulationmentioning

confidence: 99%

Dentin sialophosphoprotein in biomineralization

Prasad

Butler

Qin

2010

Connective Tissue Research

158

139

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Two of the proteins found in significant quantity in the extracellular matrix (ECM) of dentin are dentin phosphoprotein (DPP) and dentin sialoprotein (DSP). DPP, the most abundant of the non-collagenous proteins in dentin is an unusually polyanionic protein, containing a large number of aspartic acids (Asp) and phosphoserines (Pse) in the repeating sequences of (Asp-Pse)n. and (Asp-Pse-Pse)n. The many negatively charged regions of DPP are thought to promote mineralization by binding calcium and presenting it to collagen fibers at the mineralization front during the formation of dentin. This purported role of DPP is supported by a sizeable pool of in vitro mineralization data showing that DPP is an important initiator and modulator for the formation and growth of hydroxyapatite crystals. Quite differently, DSP is a glycoprotein, with little or no phosphate. DPP and DSP are the cleavage products of dentin sialophosphoprotein (DSPP). Human and mouse genetic studies have demonstrated that mutations in, or knockout of, the Dspp gene result in mineralization defects in dentin and/or bone. The discoveries in the past 40 years with regard to DPP, DSP and DSPP have greatly enhanced our understanding of biomineralization and set a new stage for future studies. In this review, we summarize the important and new developments made in the past four decades regarding the structure and regulation of the DSPP gene, the biochemical characteristics of DSPP, DPP and DSP, as well as the cell/tissue localizations and functions of these molecules.

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“…DSPP in the dentin and bone is present as the proteolytically processed fragments: dentin sialoprotein (DSP) and dentin phosphoprotein (DPP), which originate from the N‐terminal and C‐terminal regions of the DSPP amino acid sequence respectively (Macdougall et al , 1997). The major cleavage sites of DSPP are also at the N‐termini of aspartyl residues (Macdougall et al , 1997; Qin et al , 2001; Ritchie and Li, 2001), as in the case of DMP1 processing. DSPP mutation studies in humans and gene ablation experiments in mice have demonstrated that DSPP and/or its processed fragments (DSP and DPP) are critical for the mineralization of dentin (Xiao et al , 2001; Zhang et al , 2001; Sreenath et al , 2003; Suzuki et al , 2009) and bone (Verdelis et al , 2008).…”

Section: Introductionmentioning

confidence: 99%

Expression and distribution of SIBLING proteins in the predentin/dentin and mandible of hyp mice

et al. 2010

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OBJECTIVES-Human X-linked hypophosphatemia (XLH) and its murine homologue, Hyp are caused by inactivating mutations in PHEX gene. The protein encoded by PHEX gene is an endopeptidase whose physiological substrate(s) has not been identified. Dentin matrix protein 1 (DMP1) and dentin sialophosphoprotein (DSPP), two members of the Small Integrin-Binding LIgand, N-linked Glycoprotein (SIBLING) family are proteolytically processed. It has been speculated that PHEX endopeptidase may be responsible for the proteolytic cleavage of DMP1 and DSPP. To test this hypothesis and to analyse the distribution of SIBLING proteins in the predentin/ dentin complex and mandible of Hyp mice, we compared the expression of four SIBLING proteins, DMP1, DSPP, bone sialoprotein (BSP) and osteopontin (OPN) between Hyp and wild-type mice.METHODS-These SIBLING proteins were analysed by protein chemistry and immunohistochemistry. RESULTS-(1)Dentin matrix protein 1 and DSPP fragments are present in the extracts of Hyp predentin/dentin and bone; (2) the level of DMP1 proteoglycan form, BSP and OPN is elevated in the Hyp bone.CONCLUSIONS-The PHEX protein is not the enzyme responsible for the proteolytic processing of DMP1 and DSPP. The altered distribution of SIBLING proteins may be involved in the pathogenesis of bone and dentin defects in Hyp and XLH.Keywords dentin matrix protein 1; dentin sialophosphoprotein; bone sialoprotein; osteopotin; X-linked hypophosphatemic rickets

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A novel rat dentin mRNA coding only for dentin sialoprotein

Cited by 14 publications

References 23 publications

Porcine Dentin Sialoprotein Is a Proteoglycan with Glycosaminoglycan Chains Containing Chondroitin 6-Sulfate

Porcine Dentin Sialoprotein Is a Proteoglycan with Glycosaminoglycan Chains Containing Chondroitin 6-Sulfate

Dentin sialophosphoprotein in biomineralization

Expression and distribution of SIBLING proteins in the predentin/dentin and mandible of hyp mice

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