anti-Dentin Sialophosphoprotein (DSPP) Antibodies

Human Dentin Sialophosphoprotein (DSPP) interaction partners

1. 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.

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

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

4. 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 (show CRISP1 Antibodies) (BSP (show KLK6 Antibodies)) and dentin sialoprotein (DSP)-in normal salivary gland cells.

5. DSPP-MMP20 (show MMP20 Antibodies) 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.

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

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

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

9. 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

10. DMP1 (show DMP1 Antibodies) and DSPP were more abundant in carious than in sound samples.

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 (show Vcan Antibodies)

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 (show MMP2 Antibodies) 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. 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.

2. 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 (show HEY1 Antibodies) downregulated the expression levels of DSPP in OLCs stimulated by differentiation medium.

3. Data demonstrate for the first time that the dentin sialoprotein (DSP) domain acts as a ligand in a Arg-Gly-Asp (show C3 Antibodies) (RGD)-independent manner and is involved in intracellular signaling via interacting with integrin beta6. The DSP (show DSP Antibodies) domain regulates DSPP expression and odontoblast homeostasis via a positive feedback loop.

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

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

6. no significant dentin malformation was observed in Mep1b (show MEP1B Antibodies) (-/-) or Mep1a (show MEP1A Antibodies) (-/-) deficient mice.

7. 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.

8. Klf10 (show KLF10 Antibodies) is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 (show DMP1 Antibodies) and Dspp transcription.

9. DMOG can enhance Dspp expression through VEGF (show VEGFA Antibodies)-induced stabilization of Runx2 (show RUNX2 Antibodies) protein.

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

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 (show ATP7A Antibodies) enamel and irregular abrasion of teeth, which might occur as a consequence of depressed DSPP mRNA and DPP protein expression.