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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.
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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.
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mutations c.3085A > G and c.3087C > T resulted in p.N1029D and co-segregated with deafness phenotype in Chinese family
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The levels of DSPP silencing-induced downregulation differed amongst CSC markers, with ABCG2 and CD44 showing more pronounced downregulations.
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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.
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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.
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This study expands the spectrum of DSPP variants, highlighting their associated phenotypic continuum.
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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.
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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.
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BMP2 and RUNX2 are expressed exclusively by osteoblasts whereas DSPP and LOXL2 are expressed exclusively by odontoblasts. (Review)
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A novel pathogenic splicing-mutation c.52-1G>A of DSPP is associated with dentinogenesis imperfecta shields type II.
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Adhesive and migratory effects of phosphophoryn are modulated by flanking peptides of the integrin binding motif.
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expression of MMP-20 and co-expression and potential interaction with DSPP in human major salivary gland tissues
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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
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DMP1 and DSPP were more abundant in carious than in sound samples.
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Domain of dentine sialoprotein mediates proliferation and differentiation of human periodontal ligament stem cells.
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analysis of a mutation in DSPP causing dentinogenesis imperfecta and characterization of the mutational effect
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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.
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efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site
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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.