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DMP1 gene seems to be involved in genetic predisposition to Ankylosing spondylitis (AS).
DMP-1 immunostaining was higher for MTA (show DNMT1 ELISA Kits) and PC, confirming the reparative and bioinductive capacity of these materials.
This review will focus on the aberrant splicing of tumor suppressor/oncogenes that belong to the DMP1-ARF-MDM2 (show MDM2 ELISA Kits)-p53 (show TP53 ELISA Kits) pathway
Expressions of dentin matrix protein (DMP)-1 and osteopontin (OPN (show SPP1 ELISA Kits)) were observed in both normal dentin and dentin from DGI (show DSG1 ELISA Kits)-I affected patients, without significant differences
identify alternative splicing as a mechanism utilized by cancer cells to modulate the DMP1 locus through diminishing DMP1alpha tumour suppressor expression
The findings indicate that DMP-1 is a useful marker of osteogenic differentiation and mineralisation in soft tissue tumours
A family of autosomal recessive form of Hypophosphatemic rickets secondary to a DMP1 mutation located in the first coding exon of the gene, is reported.
Results suggest that FAM20C (show FAM20C ELISA Kits) suppresses FGF23 (show FGF23 ELISA Kits) production by enhancing DMP1 expression, and inactivating mutations in FAM20C (show FAM20C ELISA Kits) cause FGF23 (show FGF23 ELISA Kits)-related hypophosphatemia by decreasing transcription of DMP1.
DMP1 may play an important role in maintaining the chondrogenic phenotype and its possible involvement in altered cartilage matrix remodelling and degradation in disease conditions like osteoarthritis.
DMP1 and DSPP (show DSPP ELISA Kits) were more abundant in carious than in sound samples.
phosphorylated DMP1 expressed in marrow stromal cells was an inhibitor of hydroxyapatite formation; the highly phosphorylated C-terminal 57-kDa fragment apparently arising from proteolytic cleavage, like the non-phosphorylated DMP1, was an HA nucleator
This study was designed to investigate the effect of dentin phosphoprotein (show DSPP ELISA Kits) on apoptosis of the cells.
mutation creates a lower set point for extracellular phosphate and maintains it through the regulation of Fgf23 (show FGF23 ELISA Kits) cleavage and expression
Data show that the phenotype of Notch (show NOTCH1 ELISA Kits) activation in osteocytes was prevented in matrix protein 1 (Dmp1)-Cre;Rosa(Notch (show NOTCH1 ELISA Kits)) mice hemizygous for the Dmp1-sclerostin (SOST (show SOST ELISA Kits)) transgene.
Klf10 is involved in tooth development and promotes odontoblastic differentiation via the up-regulation of Dmp1 and Dspp (show DSPP ELISA Kits) transcription.
These findings indicate that glycosylation of DMP1 is a key posttranslational modification process during development and that DMP1-PG functions as an indispensable proteoglycan (show Vcan ELISA Kits) in osteogenesis.
the hypophosphatemia induced osteomalacia phenotype in Dmp1 KO mice is contributed by at least two factors: the low Pi level and the DMP1 local function in mineralization
These results suggest that the LPV motif is essential for the efficient export of secretory DMP1 from the ER to the Golgi complex.
An in situ hybridization study of perlecan (show HSPG2 ELISA Kits), DMP1, and MEPE (show MEPE ELISA Kits) in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage.
It was concluded that endogenously secreted PTH (show PTH ELISA Kits) and GHR (show GHR ELISA Kits) signaling in bone are necessary to establish radial bone growth and optimize mineral acquisition during growth.
This study demonstrates the sequential involvement of Wnt5, MMP-3, DMP-1 expression, and DMP-1 degradation products by MMP-3, in effecting IL-1beta-induced proliferation of ESC-derived odontoblast-like cells.
We conclude that DMP-1 may be involved in regulating the temporal expression at embryonic stages in the mouse tongue
Dentin matrix acidic phosphoprotein is an extracellular matrix protein and a member of the small integrin binding ligand N-linked glycoprotein family. This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. The protein contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation the protein becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in the gene are known to cause autosomal recessive hypophosphatemia, a disease that manifests as rickets and osteomalacia. The gene structure is conserved in mammals. Two transcript variants encoding different isoforms have been described for this gene.
dentin matrix acidic phosphoprotein 1
, dentin matrix protein 1
, serine rich acidic phosphoprotein