Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization.
Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization.
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DOI：
10.1021/bm2005214
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发表时间：
2011-08-08
影响因子：
6.2
通讯作者：
Beniash, Elia
中科院分区：
文献类型：
--
作者：
Deshpande, Atul Suresh;Fang, Ping-An;Zhang, Xiaoyuan;Jayaraman, Thottala;Sfeir, Charles;Beniash, Elia
SIBLING（小整合素结合配体 N 连接糖蛋白）家族是骨骼和牙本质中主要的非胶原蛋白类别。这些极度酸性和高度磷酸化的细胞外蛋白在胶原矿化组织的形成中发挥着关键作用。虽然单个 SIBLING 的缺乏会导致体内显着的矿化缺陷，但它们都不会导致矿化完全停止，这表明这些蛋白质具有重叠的功能。为了评估不同的 SIBLING 是否以相似的方式调节生物矿化，以及磷酸化如何影响其活性，我们研究了两种 SIBLING：牙本质基质蛋白 1 (DMP1) 和牙本质磷酸蛋白 (DPP) 对体外矿物质形态和组织的影响。我们的结果表明这些蛋白质对矿化的影响存在明显差异。我们表明磷酸化对两种蛋白质的矿化调节具有深远的影响。具体而言，两种磷酸化蛋白均促进胶原原纤维的有组织矿化，而磷酸化 DMP1 在没有胶原蛋白的情况下诱导有组织矿物质束的形成。总之，这些结果表明一级结构和磷酸化独特地决定了单个 SIBLING 在矿物形态和组织调节中的功能。
SIBLING (Small Integrin-Binding Ligand N-linked Glycoproteins) family is the major group of noncollagenous proteins in bone and dentin. These extremely acidic and highly phosphorylated extracellular proteins play critical roles in the formation of collagenous mineralized tissues. While the lack of individual SIBLINGs causes significant mineralization defects in vivo, none of them led to a complete cessation of mineralization suggesting that these proteins have overlapping functions. To assess whether different SIBLINGs regulate biomineralization in a similar manner, and how phosphorylation impacts their activity, we studied the effects of two SIBLINGs, dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP), on mineral morphology and organization in vitro. Our results demonstrate distinct differences in the effects of these proteins on mineralization. We show that phosphorylation has a profound effect on the regulation of mineralization by both proteins. Specifically, both phosphorylated proteins facilitated organized mineralization of collagen fibrils and phosphorylated DMP1 induced formation of organized mineral bundles in the absence of collagen. In summary, these results indicate that the primary structure and phosphorylation uniquely determine functions of individual SIBLINGs in regulation of mineral morphology and organization.
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影响因子：
3.8
作者：
Deshpande, Atul S.;Beniash, Elia
通讯作者：
Beniash, Elia
影响因子：
3.9
作者：
Gupta, Himadri S.;Fratzl, Peter;Kirchner, Helmut O. K.
通讯作者：
Kirchner, Helmut O. K.
影响因子：
5.1
作者：
Almushayt, A;Narayanan, K;George, A
通讯作者：
George, A
影响因子：
7.6
作者：
Feng, JQ;Huang, H;Mishina, Y
通讯作者：
Mishina, Y
影响因子：
5.6
作者：
BONAR, LC;LEES, S;MOOK, HA
通讯作者：
MOOK, HA