Recombinant Human Dentin sialophosphoprotein (DSPP), partial

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. PMID: 30309696
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. PMID: 30015841
3. mutations c.3085A > G and c.3087C > T resulted in p.N1029D and co-segregated with deafness phenotype in Chinese family PMID: 29741433
4. The levels of DSPP silencing-induced downregulation differed amongst CSC markers, with ABCG2 and CD44 showing more pronounced downregulations. PMID: 30002682
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. PMID: 29672573
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. PMID: 27430624
7. This study expands the spectrum of DSPP variants, highlighting their associated phenotypic continuum. PMID: 27973701
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. PMID: 27881474
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. PMID: 27666430
10. BMP2 and RUNX2 are expressed exclusively by osteoblasts whereas DSPP and LOXL2 are expressed exclusively by odontoblasts. (Review) PMID: 27784228
11. A novel pathogenic splicing-mutation c.52-1G>A of DSPP is associated with dentinogenesis imperfecta shields type II. PMID: 26829730
12. Adhesive and migratory effects of phosphophoryn are modulated by flanking peptides of the integrin binding motif. PMID: 25396425
13. expression of MMP-20 and co-expression and potential interaction with DSPP in human major salivary gland tissues PMID: 25805840
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 PMID: 25158199
15. Domain of dentine sialoprotein mediates proliferation and differentiation of human periodontal ligament stem cells. PMID: 24400037
16. analysis of a mutation in DSPP causing dentinogenesis imperfecta and characterization of the mutational effect PMID: 23509818
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. PMID: 23589294
18. efficiency of dentin sialoprotein-phosphophoryn processing is affected by mutations both flanking and distant from the cleavage site PMID: 23297400
19. 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. PMID: 22521702
20. This study presents evidence of a shared underlying mechanism of capturing of normal DSPP by two different classes of DSPP mutations. PMID: 22392858
21. DSPP, OPN, or MMP-9 expressions at histologically-negative surgical margins predict Oral squamous cell carcinoma recurrence with MMP-9 being the preferred predictor. PMID: 22410369
22. The P17 residue of DSPP is a mutational hotspot in a Chinese family with Dentinogenesis Imperfecta type II. PMID: 22310900
23. study concludes that enamel defects can be part of the dental phenotype caused by DSPP mutations, although DSPP is not critical for dental enamel formation PMID: 22243242
24. Data shows all known DSPP mutations (except Y6D) cause nonsyndromic dentin dysplasia,DD-II, and dentinogenesis imperfecta, DGI II & III, by retention of mutant proteins in the endoplasmic reticulum with associated decreased secretion of normal DSPP. PMID: 22392858
25. Data show that the novel dentin sialophosphoprotein (DSPP) mutation was considered as the causation of dentinogenesis imperfecta type II (DGI-II). PMID: 22125647
26. predictions of exon 3 skipping in specific DSPP mutations have been validated; cryptic splicing donor site has been identified. possible insight into DSPP mutations in the pathogenesis and genotype-phenotype correlations of hereditary dentin defects. PMID: 21736673
27. Results suggest that DSPP is regulated post-transcriptionally by mir32, mir885-5p and mir586 during odontoblast differentiation. PMID: 21687927
28. Frameshift mutations in the part of the DSPP gene coding for DPP explain a significant part of inherited and isolated dentin diseases, i.e., dentin dysplasia type II and dentinogenesis imperfecta variants. PMID: 20949630
29. DSPP gene mutation not only influences dentinogenesis but also affects early stage amelogenesis. PMID: 21029264
30. Data identified novel single bp deletional DSPP mutations in three Korean families with DGI type II. PMID: 20618350
31. This review of genetic studies demonstrates that mutations in, or knockout of the Dspp gene result in mineralization defects in dentin and/or bone. PMID: 20367116
32. Data show there was a direct correlation between the degree of DSPP-silencing and suppression of MMP-2, MMP-3 and MMP-9. PMID: 21103065
33. High dentin expression is associated with dental caries. PMID: 20802180
34. Mutation analysis revealed mutation (c.53T>A, p.V18D, g.1192T>A) involving 2nd nucleotide of 1st codon within exon 3 of DSPP gene. This is 7th mutation in DSPP V18 residue. Only 1 other was shown as de novo mutation; it also affected V18 AA residue. PMID: 20121932
35. Direct DNA sequencing identified a novel A-->G transition mutation adjacent to the donor splicing site within intron 3 in all affected individuals. PMID: 20146806
36. A novel mutation in the first exon of the DSPP gene were found in all dentinogenesis imperfecta patients in a Chinese family. PMID: 19806576
37. Transient DSPP expression was seen in the presecretory ameloblasts with continuous expression in the odontoblasts. PMID: 11856645
38. there is a novel signaling function for phosphophoryn in cell differentiation beyond the hypothesized role of PP in biomineralization PMID: 15371433
39. Dentin sialophosphoprotein expressed by transgenic presecretory ameloblasts contributes to the unique properties of the dentino-enamel junction. PMID: 16014627
40. study shows for the first time that DSPP is ectopically expressed in human prostate cancer; expression of this SIBLING protein strongly correlates with conventional histopathological prognostic indicators of prostate cancer progression PMID: 16108038
41. Mutational analyses identified no coding or intron junction sequence variations associated with affection status in DMP1, MEPE, or the DSP portion of DSPP. The defects in the permanent dentition were typically mild and consistent with DD-II. PMID: 16567553
42. 2 mutation hotspots may be causative for multiple unrelated dentinogenesis imperfecta families with different clinical phenotypes PMID: 16920545
43. mutation p.Pro17Ser causes type II dentinogenesis imperfecta in the Chinese family PMID: 17686168
44. The results show high expression levels of DSPP in human tooth germs indicating that it may play an essential role for physiological and pathological events in tooth development. PMID: 18211748
45. Data provide the first evidence that DPP mutations can cause hereditary dentin disorders and suggest that in-frame length variations and missense SNPs in DPP have no obvious pathogenetic effects on dentin formation. PMID: 18456718
46. Within 9 dentin dysplasia (type II) and dentinogenesis imperfecta (type II and III) patient/families, 7 have 1 of 4 net -1 deletions within the a 2-kb coding repeat domain of the DSPP gene while the remaining 2 patients have splice-site mutations. PMID: 18521831
47. The aim of this study was to perform phenotype analysis and dentin sialophosphoprotein (DSPP) mutational analysis on 3 Brazilian families diagnosed with dentinogenesis imperfecta type II. PMID: 18797159
48. Identification of DSPP splice junction mutation (IVS2-6T>G) in a family with dentin dysplasia type II. Mutation is in 6th nucleotide from the end of intron 2, perfectly segregates with the disease phenotype. PMID: 19026876
49. A novel -1 bp frameshift (c.3141delC) falls within the portion of the DSPP repeat domain previously associated solely with the DGI phenotype. This new frameshift mutation shows that overlapping DSPP mutations can give rise to either DGI or DD phenotypes. PMID: 19029076
50. The heterozygous deletion mutation in DSPP contributed to the pathogenesis of dentinogenesis imperfecta type II. PMID: 19103209

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HGNC: 3054

OMIM: 125420

KEGG: hsa:1834

STRING: 9606.ENSP00000282478

UniGene: Hs.678914