VARIATIONS IN COLLAGEN FIBRIL STRUCTURE IN TENDONS
VARIATIONS IN COLLAGEN FIBRIL STRUCTURE IN TENDONS
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DOI：
10.1002/bip.360210507
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发表时间：
1982-01-01
期刊：
影响因子：
2.9
通讯作者：
STERLING, K
中科院分区：
文献类型：
--
作者：
BRODSKY, B;EIKENBERRY, EF;STERLING, K
用X射线衍射仪观察肌腱内胶原原纤维结构的变化。对单个物种的肌腱以及不同物种的肌腱进行了解剖研究，以确定胶原纤维的轴向和侧向结构中存在的差异。经向衍射图来源于轴向胶原原纤维结构。特定物种的肌腱在解剖上截然不同，给出了在实验误差内无法区分的经络模式。不同哺乳动物肌腱的经向衍射图相似，但显示出物种特有的微小差异，最明显的是在第14-18级。鸟类的肌腱也给出了彼此相似的经线图案，但鸟类的图案与哺乳动物的图案有很大的不同。禽腱给出更强的奇数和更弱的甚至低阶数，这一特征与减小的间隙：重叠率一致，并且在较高的子午级具有独特的强度模式。使用生化数据、纯化胶原蛋白重组纤维的衍射和傅立叶变换分析对这些差异进行了解释。从这些方法看来，在低级(2-8级)和较高级(29-52级)中观察到的变化可能与I型胶原的初级结构在不同物种中发现的差异有关。在14-18级观察到的变化似乎与分子的三螺旋结构域内的特征无关。赤道衍射提供了胶原分子在纤维中的侧向堆积的信息，并且在不同的肌腱中可以看到相当大的差异。大鼠尾腱发出尖锐的Bragg反射，表明原纤维中存在分子的结晶侧向排列。首次在非尾腱包括大鼠跟腱、兔腿腱和鹌鹑的翼、腿腱中观察到与大鼠尾肌腱类似的尖锐晶格反射。在兔和鹌鹑肌腱中，缺乏大鼠肌腱模式的强赤道反射之一，在1.26 nm处。赤道极大值是分子间间距的量度，其位置变化很大，在显示结晶堆积的样品中是最小的。鸡和火鸡腿部肌腱的分子间距离比哺乳动物肌腱或鸟类翅膀肌腱中的要长，这支持了钙化肌腱具有较大分子间距离的假设。X-射线衍射仪显示不同肌腱之间胶原纤维的轴向和侧向结构存在可复制的差异。肌腱是一种主要成分几乎完全含有I型胶原的组织，这项工作应该作为分析其他结缔组织结构的基础，其他结缔组织包含不同类型的胶原和更多的非胶原成分。
Variation of collagen fibril structure in tendon was investigated by X-ray diffraction. Anatomically distinct tendons from single species, as well as tendons from different species, were examined to determine the variations that exist in the axial and lateral structure of the collagen fibrils. The meridional diffraction is derived from the axial collagen fibril structure. Anatomically distinct tendons of a particular species give meridional patterns that are indistinguishable within experimental error. The meridional diffraction patterns from tendons of different mammals are similar but show small species-specific variations, most noticeably in the 14th-18th orders. Tendons of birds also give meridional patterns that are similar to each other, but the avian patterns differ considerably from the mammalian ones. Avian tendons give stronger odd and weaker even low orders, a feature consistent with a reduced gap:overlap ratio, and have a distinctive intensity pattern for the higher meridional orders. Interpretation of these differences was approached using biochemical data, diffraction by reconstituted fibers of purified collagen, and Fourier transform analysis. From these methods, it appears that the variations observed in the lower orders (2nd-8th) and in the higher orders (29th-52nd) are probably related to differences in the primary structure of the Type I collagen found in the different species. The variations observed in the 14th-18th orders appear not to be related to features within the triple-helical domain of the molecule. Equatorial diffraction yields information on the lateral packing of collagen molecules in the fibrils, and considerable variation was seen in different tendons. Rat tail tendon gives sharp Bragg reflections, demonstrating the presence of a crystalline lateral arrangement of molecules in the fibril. For the first time, sharp lattice reflections similar to those in rat tail tendon were observed in nontail tendons, including rat achilles tendon, rabbit leg tendon and wing and leg tendons of quail. In the rabbit and quail tendons, one of the strong equatorial reflections characteristic of the rat tendon pattern, at 1.26 nm, was absent. The positions of the equatorial maxima, which are a measure of intermolecular spacing, varied considerably, being smallest in the specimens displaying crystalline packing. The intermolecular distance in chicken and turkey leg tendons is longer than that found in mammalian tendons, or in avian wing tendons, which supports the hypothesis that a larger intermolecular spacing is characteristic of tendons that calcify. X-ray diffraction indicates there are reproducible differences in the axial and lateral structure of collagen fibrils among different tendons. This work on tendon, a tissue containing almost exclusively Type I collagen as its major component, should serve as a basis for analyzing the structure of other connective tissues, which contain different genetic types of collagen and larger amounts of noncollagenous components.