DENTIN MATRIX PROTEINS - COMPOSITION AND POSSIBLE FUNCTIONS IN CALCIFICATION
DENTIN MATRIX PROTEINS - COMPOSITION AND POSSIBLE FUNCTIONS IN CALCIFICATION
复制标题
DOI：
10.1002/ar.1092240206
复制
发表时间：
1989-06-01
影响因子：
--
通讯作者：
LINDE, A
中科院分区：
文献类型：
--
作者：
LINDE, A
牙本质可被视为矿化结缔组织。牙本质的组成和形成方式与骨有一些相似之处，但也有明显的差异。牙本质有机相（基质）决定其形态，并被认为有助于矿物相的形成。 I 型胶原蛋白的纤维网在有机基质中占主导地位。此外，还可能存在少量其他类型的胶原蛋白。非胶原蛋白 (NCP) 约占基质的 10%，分为几类：磷蛋白、骨钙素类型的 Gla 蛋白以及基质 Gla 蛋白、蛋白聚糖、不同的酸性糖蛋白和血清蛋白。其中一些 NCP 具有独特的化学成分，赋予它们特定的性质。牙本质发生通过两个同时发生的过程：在前牙本质中形成胶原网，随后在矿化前沿形成无机相。牙本质前有机基质的组成与牙本质不同，因为一些 NCP 成分恰好在矿化前沿之前分泌到细胞外。此外，前牙本质的一些成分似乎会被代谢。NCPs可能对牙本质发生过程中的几个过程很重要。许多证据表明基质中的非胶原成分有助于矿物质的形成。新数据表明，当磷蛋白和蛋白聚糖等聚阴离子 NCP 固定在固体支持物上时，会在生理条件下诱导磷灰石形成。这些数据表明聚阴离子 NCP 可以在体内充当矿物成核剂。它们还可以充当结晶的尺寸和速率调节剂并促进钙离子在组织中的扩散。此外，NCP 还可调节胶原纤维生成。
Dentin may be regarded as a mineralized connective tissue. In its composition as well as its mode of formation, dentin exhibits several similarities with bone, but also definite differences. The dentin organic phase,the matrix, determines its morphology and is believed to be instrumental in the formation of the mineral phase. A fibrous web of collagen type I dominates the organic matrix. Also, minor amounts of other collagen types may be present. The noncollagenous proteins (NCPs), which constitute about 10% of the matrix, fall into several categories: phosphoproteins, Gla‐proteins of the osteocalcin type as well as matrix Gla‐protein, proteoglycans, different acidic glycoproteins, and serum proteins. Some of these NCPs have unique chemical compositions that give them specific properties.Dentinogenesis occurs by two simultaneous processes: the formation of a collagenous web in predentin, which is followed by the formation of the inorganic phase at the mineralization front. The composition of the predentin organic matrix differs from that of dentin, as some NCP components are secreted extracellularly just in advance of the mineralization front. In addition, some constituents of predentin seem to be metabolized.The NCPs may be important to several processes during dentinogenesis. Much evidence indicates that noncollagenous components in the matrix are instrumental in mineral formation. New data show that polyanionic NCPs, such as phosphoprotein and proteoglycans, when immobilized on a solid support, induce apatite for‐mation under physiological conditions. These data indicate that polyanionic NCPs may function as mineral nucleators in vivo. They may also act as size and rate regulators for crystallization and promote calcium ion diffusion in the tissue. In addition, NCPs may regulate collagen fibrillogenesis.