The Dentin Sialoprotein (DSP) Domain Regulates Dental Mesenchymal Cell Differentiation through a Novel Surface Receptor

Dentin sialophosphoprotein Bone sialoprotein
DOI: 10.1038/srep29666 Publication Date: 2016-07-19T09:20:38Z
ABSTRACT
Abstract Dentin sialophosphoprotein (DSPP) is a dentin extracellular matrix protein that processed into sialoprotein (DSP), glycoprotein (DGP) and phosphoprotein (DPP). DSP mainly expressed in odontoblasts. We hypothesized interacts with cell surface receptors subsequently activates intracellular signaling. Using as bait for screening library, we demonstrate acts ligand binds to integrin β6. The 36 amino acid residues of are sufficient bind This peptide promoted attachment, migration, differentiation mineralization dental mesenchymal cells. In addition, aa183-219 stimulated phosphorylation ERK1/2 P38 kinases. activation was inhibited by an anti-integrin β6 antibody siRNA. Furthermore, this fragment induces SMAD1/5/8 nuclear translocation via SMAD binding elements (SBEs) the DSPP gene promoter. SBE mutations result decrease transcriptional activity. Endogenous expression up-regulated data current study first time domain RGD-independent manner involved signaling interacting regulates odontoblast homeostasis positive feedback loop.
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