Different forms of DMP1 play distinct roles in mineralization.
Different forms of DMP1 play distinct roles in mineralization.
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DOI：
10.1177/0022034510363250
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发表时间：
2010-04
影响因子：
7.6
通讯作者：
Boskey AL
中科院分区：
文献类型：
--
作者：
Gericke A;Qin C;Sun Y;Redfern R;Redfern D;Fujimoto Y;Taleb H;Butler WT;Boskey AL
牙本质基质蛋白-1（Dentin matrix protein-1，DMP 1）是肥大软骨细胞和骨细胞的主要合成产物。先前的体外研究表明，全长DMP 1抑制羟基磷灰石（HA）的形成和生长，而其N端片段（37 K）促进HA的形成。由于矿化组织中有3个片段[N-末端、C-末端（57 K）和硫酸软骨素连接的N-末端片段（DMP 1-PG）]，我们预测每个片段对与HA相互作用相关的矿化具有不同的影响。在明胶-凝胶体系中，37 K和57 K片段都是HA形成和生长的促进剂，而DMP 1-PG是抑制剂。FTIR分析表明，在Ca ~（2+）和HA存在和不存在的情况下，3个片段和全长蛋白的二级结构发生了轻微的变化，而37 K、57 K和DMP 1-PG的二级结构没有发生变化。这些发现表明，不同形式的DMP 1可能共同控制矿化过程。
Dentin matrix protein-1 (DMP1) is a major synthetic product of hypertrophic chondrocytes and osteocytes. Previous in vitro studies showed full-length DMP1 inhibits hydroxyapatite (HA) formation and growth, while its N-terminal fragment (37K) promotes HA formation. Since there are 3 fragments within the mineralized tissues [N-terminal, C-terminal (57K), and a chondroitinsulfate-linked N-terminal fragment (DMP1-PG)], we predicted that each would have a distinct effect on mineralization related to its interaction with HA. In a gelatin-gel system, 37K and 57K fragments were both promoters of HA formation and growth; DMP1-PG was an inhibitor. The secondary structures of the 3 fragments and the full-length protein in the presence and absence of Ca2+ and HA determined by FTIR showed that the full-length protein undergoes slight conformational changes on binding to HA, while 37K, 57K, and DMP1-PG do not change conformation. These findings indicate that distinct forms of DMP1 may work collectively in controlling the mineralization process.
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影响因子：
2.9
作者：
HEINONEN, JK;LAHTI, RJ
通讯作者：
LAHTI, RJ
影响因子：
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作者：
Feng, Jian Q.;Scott, Greg;Mishina, Yuji
通讯作者：
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影响因子：
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作者：
He, G;Dahl, T;George, A
通讯作者：
George, A
影响因子：
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作者：
BOSKEY, AL
通讯作者：
BOSKEY, AL
影响因子：
4.8
作者：
Steiglitz, BM;Ayala, M;Greenspan, DS
通讯作者：
Greenspan, DS