anti-Dentin Sialophosphoprotein (DSPP) Antibodies

Human Dentin Sialophosphoprotein (DSPP) interaction partners

1. Taken together, these findings indicate that knockdown of DSPP inhibits glioma cells migration and invasion, suggesting that targeting DSPP might be a potentially effective therapeutic strategy for treating glioma.

2. Study provide evidence to suggest that DSPP may be involved in endoplasmic reticulum (ER) stress mechanisms in oral squamous cell carcinoma, since its downregulation in OSC2 cells led to significant alterations in the levels of major ER stress-associated proteins, and subsequent collapse of the unfolded protein response system.

3. mutations c.3085A > G and c.3087C > T resulted in p.N1029D and co-segregated with deafness phenotype in Chinese family

4. The levels of DSPP silencing-induced downregulation differed amongst CSC markers, with ABCG2 and CD44 showing more pronounced downregulations.

5. the transgenic expression of DPP significantly improved the dentin defects in Dspp-null mice. These data provide in vivo evidence that DPP may promote the deposition of hydroxyapatite crystals during the formation and mineralization of dentin, which is in agreement with the in vitro findings described in earlier reports.

6. Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP domain regulates DSPP expression and odontoblast homeostasis via a positive feedback loop.

7. This study expands the spectrum of DSPP variants, highlighting their associated phenotypic continuum.

8. These data indicate that secretome derived from salivary gland cancer cells can influence the expression of two potential biomarkers of oral cancer-namely, bone sialoprotein (BSP) and dentin sialoprotein (DSP)-in normal salivary gland cells.

9. DSPP-MMP20 pair may play a role in the normal turnover of cell surface proteins and/or repair of pericellular matrix proteins of the basement membranes in the metabolically active duct epithelial system of the nephrons.

10. BMP2 and RUNX2 are expressed exclusively by osteoblasts whereas DSPP and LOXL2 are expressed exclusively by odontoblasts. (Review)

11. A novel pathogenic splicing-mutation c.52-1G>A of DSPP is associated with dentinogenesis imperfecta shields type II.

12. Adhesive and migratory effects of phosphophoryn are modulated by flanking peptides of the integrin binding motif.

13. expression of MMP-20 and co-expression and potential interaction with DSPP in human major salivary gland tissues

14. mutations of the DSP-PP P4 to P4' cleavage site can block, impair or accelerate dentin sialoprotein phosphophoryn cleavage, and suggest that its Bone morphogenic protein 1 cleavage site is conserved in order to regulate its cleavage efficiency

15. DMP1 and DSPP were more abundant in carious than in sound samples.

16. Domain of dentine sialoprotein mediates proliferation and differentiation of human periodontal ligament stem cells.

17. analysis of a mutation in DSPP causing dentinogenesis imperfecta and characterization of the mutational effect

18. DSS domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo.

19. efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site

20. A review of hereditary dentine diseases resulting from mutations in DSPP gene suggests that the localization of mutation in the sequence of the DSPP gene might result in a different phenotype due to the diverse cellular fate of the mutated protein.

Pig (Porcine) Dentin Sialophosphoprotein (DSPP) interaction partners

1. The porcine dentin sialophosphoprotein has an N-terminal domain with at least six N-glycosylations and a C-terminal domain with two glycosaminoglycan attachments and at least two O-glycosylations.

2. Astacins in the predentin matrix cleave Dspp.

3. isolation of DSP from pig dentin and demonstration that it is a proteoglycan

4. isolation and characterization of a third domain of DSPP, designated dentin glycoprotein (DGP)

5. correspondence between DSPP cleavage sites that occur in vivo and those generated in vitro demonstrates that MMP-2 and MMP-20 process DSPP into smaller subunits in the dentin matrix during odontogenesis

6. DPP length variations are polymorphic and are not associated with dentin defects

7. porcine DPP-derived arginyl-glycyl-aspartic acid peptide, but not its mutant arginyl-alanyl-aspartic acid peptide, significantly promoted cell migration

Mouse (Murine) Dentin Sialophosphoprotein (DSPP) interaction partners

1. our findings demonstrate that MMP9 is important for tooth development and DSP is a novel target of MMP9 during dentinogenesis.

2. The C-terminal DSP domain induced phosphorylation of occludin Ser(490) and focal adhesion kinase (FAK) Ser(722) and Tyr(576). Coexpression of DSP, occludin and FAK was detected in dental mesenchymal cells during tooth development. Occludin physically interacts with FAK, and occludin and FAK phosphorylation can be blocked by DSP and occludin antibodies.

3. stable Hey1overexpressing cells expressed higher levels of dentin sialophosphoprotein (DSPP) and exhibited higher mineralization capabilities following stimulation by differentiation medium. Furthermore, RNA interferencemediated knockdown of Hey1 downregulated the expression levels of DSPP in OLCs stimulated by differentiation medium.

4. Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP domain regulates DSPP expression and odontoblast homeostasis via a positive feedback loop.

5. Results show that transgenic expression of Dspp partially rescued the long bone defects of Dmp1-null mice and suggest that DSPP and DMP1 may function synergistically within the complex milieu of bone matrices.

6. Data show provide evidence that DSPP is important for normal mineralization of both dentin and enamel.

7. no significant dentin malformation was observed in Mep1b (-/-) or Mep1a (-/-) deficient mice.

8. overexpressing DPP inhibited skeletal development, suggesting that the balanced actions between the NH2- and COOH-terminal fragments of DSPP may be required for normal skeletal development.

9. Klf10 is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 and Dspp transcription.

10. DMOG can enhance Dspp expression through VEGF-induced stabilization of Runx2 protein.

11. total dentin volume in DSPP KO animals significant changes in the ultrastructural organization exist

12. the expression of DSPP precursor protein is required for normal odontoblast lineage differentiation

13. DPP is essential for the formation of well-defined tooth structures with mineralized dentin matrix.

14. continuous DSPP action is required for the growth and/or maintenance of the mandibular condylar cartilage

15. Data indicate that that Wnt10a regulates Dspp expression in mesenchymal cells.

16. Inactivation of DSPP leads to loss of alveolar bone and cementum in PDL of Dspp null mice. loss of DSPP results in periodontal diseases indicates that this molecule plays vital role in maintaining health of periodontium.

17. DSS domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo.

18. Results indicate that dentin sialophosphoprotein (DSPP) is a downstream effector molecule that mediates the roles of dentin matrix protein 1 (DMP1) in dentinogenesis.

19. In addition to the peptide bond Gly(451)-Asp(452), there must be a cryptic cleavage site or sites close to Asp(452) in the mouse DSPP that can be cleaved by BMP1.

20. The distribution profiles of the dentin sialophosphoprotein NH(2)-terminal and COOH-terminal fragments and osteopontin (OPN) were investigated in mouse teeth at different ages by immunohistochemistry.

Guinea Pig Dentin Sialophosphoprotein (DSPP) interaction partners

1. The results showed that the concentrations of F ion in F and F+Al groups were increased significantly. F induced the mottled enamel and irregular abrasion of teeth, which might occur as a consequence of depressed DSPP mRNA and DPP protein expression.