Key proteolytic cleavage site and full-length form of DSPP

Y. Sun, Y. Lu, S. Chen, M. Prasad, X. Wang, Q. Zhu, J. Zhang, H. Ball, J. Feng, W. T. Butler, C. Qin

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


It is known that dentin sialophosphoprotein (DSPP) is processed into NH2- and COOHterminal fragments, but its key cleavage site has not been identified, nor has its full-length form been discovered. The objectives of this study were to identify the key cleavage site during DSPP processing and to search for full-length DSPP in vivo. We generated a construct encoding DSPP, in which Asp452, a cleavage site residue, was replaced by Ala 452. The pulp-odontoblast complex and dentin were extracted, chromatographically separated, and assessed by Stains-All staining, Western immunoblotting, and mass spectrometry. These studies showed that the substitution of Asp452 by Ala452 completely blocks the cleavage of mouse DSPP in the transfected cells, indicating that the NH 2-terminal peptide bond of Asp452 is essential for the initiation of DSPP proteolytic processing. The results of this study revealed the presence of full-length DSPP and its processed fragments in extracts from the pulp/odontoblast and dentin.

Original languageEnglish (US)
Pages (from-to)498-503
Number of pages6
JournalJournal of dental research
Issue number5
StatePublished - May 2010


  • Dentin extracellular matrix
  • Dentin phosphoprotein
  • Dentin sialophosphoprotein
  • Dentin sialoprotein
  • Proteolytic processing

ASJC Scopus subject areas

  • Dentistry(all)


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