INTERACTIONS OF MATRIX PROTEINS FROM MINERALIZED TISSUES WITH OCTACALCIUM PHOSPHATE
INTERACTIONS OF MATRIX PROTEINS FROM MINERALIZED TISSUES WITH OCTACALCIUM PHOSPHATE
复制标题
DOI：
10.3109/03008209409015041
复制
发表时间：
1994-01-01
影响因子：
2.9
通讯作者：
ADDADI, L
中科院分区：
文献类型：
--
作者：
FUREDIMILHOFER, H;MORADIANOLDAK, J;ADDADI, L
酸性基质大分子存在于许多矿化组织中，包括脊椎动物的那些，被认为参与控制晶体的形成。然而，很少有人知道他们在体内的功能，特别是在有关磷酸钙含晶体。研究了各种合成和天然酸性大分子在体外与磷酸八钙（OCP）晶体相互作用的方式。通过检查晶体形态的变化来评估相互作用，所述晶体形态的变化由添加剂与一些晶面而不是其他晶面的优先相互作用引起。富含酸性氨基酸的大分子，有或没有多糖，如聚天冬氨酸和软体动物壳蛋白，分别被证明优先与OCP晶体的水合板表面上暴露的Ca离子行相互作用。相比之下，磷酸化蛋白质磷酸蛋白和卵黄高磷蛋白与OCP侧面的磷灰石样基序特异性相互作用。在所用的实验条件下，BSP不与OCP发生特异性相互作用。在评价矿化组织中酸性基质大分子的功能时，应考虑到这些酸性大分子识别不同晶蜂的观察结果。
Acidic matrix macromolecules, present in many mineralized tissues, including those of vertebrates, are thought to be involved in controlling crystal formation. Little, however, is known about their in vivo functions; particularly in relation to calcium-phosphate-containing crystals. The manner in which a variety of synthetic and natural acidic macromolecules interact in vitro with crystals of octacalcium phosphate (OCP) has been studied. Interactions were assessed by examining changes in morphology of the crystals resulting from preferential interaction of the additive with some crystal faces and not others. Macromolecules rich in acidic amino acids, with or without polysaccharides, such as polyaspartate and mollusk shell proteins respectively, were shown to interact preferentially with rows of Ca ions exposed on the hydrated plate surface of OCP crystals. In contrast, the phosphorylated proteins, phosphophoryn and phosvitin, interacted specifically with the apatite-like motifs on the OCP side faces. BSP did not interact specifically with OCP, under the experimental conditions used. The observation that these classes of acidic macromolecules recognize different crystal bees should be taken into account when evaluating functions of acidic matrix macromolecules in mineralized tissues.