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M006271200v1
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Papers In Press, published online ahead of print October 19, 2000
J. Biol. Chem, 10.1074/jbc.M006271200
Submitted on July 14, 2000
Revised on October 18, 2000
Accepted on October 19, 2000

Identification and Characterization of the Carboxy-terminal Region of Rat Dentin Sialoprotein (DSP)

Chunlin Qin, Richard G. Cook, Ralph S. Orkiszewski, and William T. Butler

Department of Basic Sciences, University of Texas-Houston Dental Branch, Houston, Texas 77030

Corresponding Author: cqin{at}mail.db.uth.tmc.edu

SUMMARY Two acidic proteins, dentin sialoprotein (DSP) and dentin phosphoprotein (DPP), are present in the extracellular matrix of dentin, but not in bone. These two proteins are expressed in odontoblasts and preameloblasts as a single cDNA transcript coding a large precursor protein termed dentin sialophosphoprotein (DSPP). DSPP is specifically cleaved into two unique proteins, DSP and DPP. However, the cleavage site(s) of DSPP, and the mechanisms for regulating the cleavages are unknown. To identify the specific site(s) of DSPP that are cleaved when the initial translation product is converted to DSP and DPP, we performed a detailed analysis (Edman degradation and mass spectrometry) on selected tryptic peptides of a size originating from the COOH-terminal region of rat DSP. Following cleavage with trypsin, the DSP fragments were separated by a two-dimensional method (size-exclusion chromatography followed by reversed-phase HPLC). We characterized thirteen peptides from various regions of DSP. The analyses showed that peptide Ile409-Tyr421 was the major COOH-terminal fragment, ending at Tyr421 only nine residues from the NH2-terminus of DPP. Peptide Gln385-His406 represented a second, minor COOH-terminal peptide that terminated at His406. Both of these residues are well beyond the COOH-terminus predicted previously by two independent studies estimating that rat DSP contained 360-370 amino acids. Careful studies on two peptides showed that, among nine potential casein kinase II phosphorylation sites, two serines were phosphorylated. We found that rat DSP was heterogeneous with respect to phosphorylation since this same peptide sequence eluted in two discrete peaks, one with two phosphoserines and the other having one. The finding that three lysines just preceding the COOH-termini were modified by a 43 Da substituent (possibly a carbamoyl substituent) suggests that the lysines in this region were particularly susceptible to attachment of this substituent.


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