| Literature DB >> 10978503 |
Abstract
Phosphoproteins or phosphophoryns (PPs) are the most abundant (>50%) non-collagenous proteins (NCPs) in dentin. PPs bind to calcium and hydroxyapatite and are believed to play a crucial role in dentin mineralization. Dentin sialoprotein (DSP), a highly glycosylated protein, comprised 5-8% of NCPs in dentin. The coding sequences for these two major NCPs are known to be contiguously located (i.e. DSP-PP) at the cDNA and genomic DNA levels in both rat and mouse. Previous studies have demonstrated the presence of multiple DSP-PP transcripts in the total RNA of adult rat incisors. To further understand the nature of these multiple transcripts, we performed reverse transcription-PCR and obtained a PP cDNA variant which encoded a 171 amino acid peptide (PP(171)) that shares many of the same characteristics as that of the published rat PP(240) sequence [Ritchie, H.H. and Wang, L.-H., J. Biol. Chem. 271 (1996) 21695-21698]. Due to its reduced size, as compared to PP(240), this cDNA encodes a phosphorylated protein with a reduced negative charge that may differentially affect mineralization processes. We provide evidence that there are multiple DSP-PP transcripts with various sizes of PP sequences in rat.Entities:
Mesh:
Substances:
Year: 2000 PMID: 10978503 DOI: 10.1016/s0167-4781(00)00150-0
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002