STRUCTURAL STUDY OF THE CALCIFYING COLLAGEN IN TURKEY LEG TENDONS
STRUCTURAL STUDY OF THE CALCIFYING COLLAGEN IN TURKEY LEG TENDONS
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DOI：
10.1016/0022-2836(79)90362-0
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发表时间：
1979-01-01
影响因子：
5.6
通讯作者：
WHITE, SW
中科院分区：
文献类型：
--
作者：
BERTHETCOLOMINAS, C;MILLER, A;WHITE, SW
钙化的火鸡腿腱代表了一种简单的骨样组织，非常适合用衍射法进行分析。本文报道了未钙化、完全钙化和部分钙化状态下肌腱胶原的一些结构研究。未钙化肌腱的低角度子午线X射线图像与大鼠尾部肌腱非常相似，由此产生的胶原原纤维的一维结构没有表现出可能与其最终钙化有关的特征。X射线和中子衍射分析相结合确定的完全钙化肌腱的结构表明，这种矿物与胶原在孔洞或缝隙区域的水平上是相关的。在钙化肌腱中，第一次和第二次X射线经向反射幅度的增加与胶原矿物质含量的增加有关。在简单模型的基础上，这种模式的变化可以用钙化成核机制来解释。当胶原蛋白钙化时，矿物质会渗透到整个纤维中，在孔洞区域是结晶的，但在胶原分子之间是无定形的。讨论了钙化的机制和完全钙化结构的力学含义。
The calcified turkey leg tendon represents a simple bone-like tissue ideally suited to analysis by diffraction methods. Some structural studies of the tendon collagen in the uncalcified, fully calcified and partially calcified states are reported. The low-angle meridional X-ray pattern from the uncalcified tendon is very similar to that of the rat tail tendon, and the resulting 1-dimensional structure of the collagen fibril exhibits no feature that could be related to its eventual calcification. The structure of the fully calcified tendon, as determined by a combination of X-ray and neutron diffraction analyses, shows that the mineral is associated with the collagen at the level of the hole or gap region. In the calcifying tendon increases in the amplitudes of the 1st and 2nd X-ray meridional reflections are correlated with an increase in the mineral content of the collagen. On the basis of simple models, it is shown that this change in the pattern can be explained by a nucleation mechanism of calcification. When collagen becomes calcified, the mineral penetrates throughout the fibril and is crystalline in the hole region but amorphous between the collagen molecules. The mechanism of calcification and the mechanical implications of the fully calcified structure are discussed.