Journal
JOURNAL OF DENTAL RESEARCH
Volume 89, Issue 5, Pages 498-503Publisher
SAGE PUBLICATIONS INC
DOI: 10.1177/0022034510363109
Keywords
dentin sialophosphoprotein; dentin sialoprotein; dentin phosphoprotein; proteolytic processing; dentin extracellular matrix
Categories
Funding
- NIH [DE005092]
Ask authors/readers for more resources
It is known that dentin sialophosphoprotein (DSPP) is processed into NH2- and COOH-terminal 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 Asp(452), 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 Asp(452) by Ala(452) completely blocks the cleavage of mouse DSPP in the transfected cells, indicating that the NH2-terminal peptide bond of Asp(452) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available