In vitro mineralization of collagen in demineralized fish bone
In vitro mineralization of collagen in demineralized fish bone
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DOI：
10.1002/macp.200400066
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发表时间：
2005-01-05
影响因子：
2.5
通讯作者：
Glimcher, MJ
中科院分区：
文献类型：
--
作者：
Chen, JL;Burger, C;Glimcher, MJ
同时在体外钙化的高度有序的脱钙鲱鱼骨胶原的小角度和广角X射线衍射已经确定了磷酸钙（Ca-P）晶体，形成为结晶度差的磷灰石，和它们的高度有序的空间，轴向分布相对于超分子包装的胶原纤维。体外钙化的程度显着减少时，超分子胶原蛋白包装被破坏。这些发现是类似的电子显微镜和小角X射线散射（SAXS）研究的本地沙德和其他物种的鱼骨和其他动物物种和体外实验的钙化纯化和重建的本地型胶原纤维。结果强调了胶原纤维的超分子包装在磷灰石晶体的非均质成核引发钙化中的重要作用。无机晶体的精细空间关系和天然胶原纤维的超分子堆积也形成两相复合物质，为骨物质和组织提供独特的机械性能和其他生理功能。
Simultaneous small- and wide-angle X-ray diffraction of in vitro calcified highly ordered decalcified shad fish bone collagen have identified the calcium phosphate (Ca-P) crystals, formed as poorly crystalline apatite, and their highly ordered spatial, axial distribution with respect to the supramolecular packing of collagen fibrils. The extent of in vitro calcification was significantly diminished when the supramolecular collagen packing was disrupted. These findings are similar to both electron microscopic and small angle X-ray scattering (SAXS) studies of native shad and other species of fish bone and other animal species and of in vitro experiments of the calcification of purified and reconstituted native type collagen fibrils. The results emphasize the important role of the supramolecular packing of collagen fibrils in the heterogeneous nucleation of apatite crystals initiating calcification. The exquisite spatial relationships of the inorganic crystal and the supramolecular packing of native collagen fibrils also form a two-phase composite substance, providing distinct mechanical properties and other physiological functions to bone substance and tissue.