Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein.
Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein.
复制标题
牙本质唾液酸磷蛋白的结构特征、加工机制和基因剪接变异体。
DOI：
10.1016/j.jdsr.2018.03.006
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Simmer,JamesP
中科院分区：
文献类型：
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作者：
Yamakoshi,Yasuo;Simmer,JamesP
牙本质涎磷蛋白(DSPP)在牙本质的形成中起重要作用。了解其结构和功能将为牙本质矿化的调控提供重要的信息。在过去的15年里，我们一直在研究从猪牙本质中分离出的DSPP衍生蛋白。猪DSPP由成牙本质细胞合成和分泌，在骨形态发生蛋白1和基质金属蛋白酶-20和-2作用下被加工成牙本质唾液蛋白(DSP)、牙本质糖蛋白(DGP)和牙本质磷酸蛋白(DPP)三种蛋白。DSP是一种形成共价二聚体的蛋白多糖，DGP是一种磷酸化的糖蛋白，DPP是一种高度磷酸化的内在无序蛋白，具有遗传多态。此外，在牙髓中未检测到DPP。这可能是由于DSPP基因的两个mRNA变体的存在：一个单独编码DSP区域，另一个编码全长DSPP。编码DSPP的mRNA变体仅在牙髓和成牙本质细胞中表达，而编码全长DSPP的变体主要在成牙本质细胞中表达，在牙髓中几乎不表达。
Dentin sialophosphoprotein (DSPP) plays an important role in the formation of dentin. Understanding its structure and function would provide important insights into the regulation of dentin mineralization. For the past 15 years, we have been studying DSPP-derived proteins isolated from pig dentin. Porcine DSPP is synthesized and secreted by odontoblasts and processed into three proteins, i.e., dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP), by bone morphogenetic protein 1 and matrix metalloproteinase-20 and -2. DSP is a proteoglycan that forms covalent dimers, DGP is a phosphorylated glycoprotein, and DPP is a highly phosphorylated intrinsically disordered protein with genetic polymorphisms. Furthermore, DPP is not detected in dental pulp. This is possibly due to the existence of two mRNA variants of theDSPPgene: one that encodes the DSP region alone and another that encodes full-length DSPP. The mRNA variant encoding DSP alone is expressed in dental pulp and odontoblasts, but the variant encoding full-length DSPP is predominantly expressed in odontoblasts and barely in dental pulp.