JBC Invitrogen Ultrasensitive Cytokine Assays

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Volume 271, Number 36, Issue of September 6, 1996 pp. 21695-21698
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Sequence Determination of an Extremely Acidic Rat Dentin Phosphoprotein

(Received for publication, May 17, 1996, and in revised form, July 9, 1996)

Helena H. Ritchie Dagger and Lee-Ho Wang

From the Dagger  Department of Pediatrics, the University of Iowa, Iowa City, Iowa 52242 and the  Division of Hematology, the Department of Internal Medicine, the University of Texas Medical School, Houston, Texas 77030

The mineralization process associated with the conversion of predentin to dentin is believed to be initiated and controlled by a set of acidic regulatory noncollagenous proteins (NCPs) which include phosphophoryn, the major NCP in dentin. Phosphophoryn binds tightly to collagen and is believed to initiate the formation of apatite crystals which play a central role in the mineralization process. During the process of analyzing the 3' end of an odontoblast-specific cDNA which codes for dentin sialoprotein (Ritchie, H. H., Hou, H., Veis, A., and Butler, W. T. (1994) J. Biol. Chem. 269, 3698-3702), we discovered a 801-base pair open reading frame. This downstream open reading frame encodes a putative leader sequence and a very acidic mature protein sequence having a deduced amino acid composition containing high percentages of both Ser (43%) and Asp (31%) residues which closely coincides with the amino acid composition of phosphophoryns from human, bovine, rat, and rabbit (i.e. Asp (30-40%) and Ser (38-50%)). This newly identified cDNA therefore encodes a protein with characteristics similar to phosphophoryn. Here we present the cDNA sequence, the deduced amino acid sequence, and the prospective Ser residue-specific casein kinase I and II phosphorylation sites for this putative phosphophoryn.




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