Yamakoshi Yasuo
Department of Biologic and Materials Sciences, University of Michigan Dental Research Lab, 1210 Eisenhower Place, Ann Arbor, MI 48108, Tel: 734-975-9358 (Office); Tel: 734-975-9326 (Lab); 734-975-9329 (Fax),
J Oral Biosci. 2009 Sep 10;51(3):134. doi: 10.2330/joralbiosci.51.134.
Dentin sialophosphoprotein (DSPP) is critical for proper mineralization of tooth dentin, and understanding its structure and function should yield important insights into how dentin biomineralization is controlled. During the recent six years, I have focused on characterizing DSPP-derived proteins isolated from developing porcine teeth. Porcine DSPP is expressed and secreted by odontoblasts and is processed by BMP-1, MMP-20 and MMP-2 into three main parts: dentin sialoprotein (DSP), dentin glycoprotein (DGP), and dentin phosphoprotein (DPP). We have learned that DSP is a proteoglycan that forms covalent dimers, DGP is a phosphorylated glycoprotein, and DPP is a highly phosphorylated intrinsically disordered protein that shows extensive length polymorphisms due to the genetic heterogeneity of its coding region.
牙本质涎磷蛋白（DSPP）对牙齿牙本质的正常矿化至关重要，了解其结构和功能应能为牙本质生物矿化的控制方式提供重要见解。在过去六年中，我专注于对从发育中的猪牙中分离出的DSPP衍生蛋白进行表征。猪DSPP由成牙本质细胞表达和分泌，并被骨形态发生蛋白-1（BMP-1）、基质金属蛋白酶-20（MMP-20）和基质金属蛋白酶-2（MMP-2）加工成三个主要部分：牙本质涎蛋白（DSP）、牙本质糖蛋白（DGP）和牙本质磷蛋白（DPP）。我们了解到，DSP是一种形成共价二聚体的蛋白聚糖，DGP是一种磷酸化糖蛋白，而DPP是一种高度磷酸化的内在无序蛋白，由于其编码区的遗传异质性，它表现出广泛的长度多态性。
