Abstract
Dentin sialophosphoprotein (DSPP) plays an important role in the formation of dentin. Understanding its structure and function would provide important insights into the regulation of dentin mineralization. For the past 15 years, we have been studying DSPP-derived proteins isolated from pig dentin. Porcine DSPP is synthesized and secreted by odontoblasts and processed into three proteins, i.e., dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP), by bone morphogenetic protein 1 and matrix metalloproteinase-20 and -2. DSP is a proteoglycan that forms covalent dimers, DGP is a phosphorylated glycoprotein, and DPP is a highly phosphorylated intrinsically disordered protein with genetic polymorphisms. Furthermore, DPP is not detected in dental pulp. This is possibly due to the existence of two mRNA variants of the DSPP gene: one that encodes the DSP region alone and another that encodes full-length DSPP. The mRNA variant encoding DSP alone is expressed in dental pulp and odontoblasts, but the variant encoding full-length DSPP is predominantly expressed in odontoblasts and barely in dental pulp.