Bradshaw J P, Miller A
Ann Rheum Dis. 1986 Sep;45(9):750-6. doi: 10.1136/ard.45.9.750.
The use of x ray fibre diffraction to study the molecular architecture of healthy and diseased human tendon is described. The three dimensional structure of human (finger) tendon is derived to high resolution and is shown to be very similar to that reported for rat tail tendon. In particular the presence of the 38 A row line in the diffraction pattern suggests that a high degree of lateral order within the collagen fibrils is a more widespread feature of tendon tissue than was formerly realised. Axially projected electron density maps of the 670 A unit repeat of the collagen fibrils of this tissue, and of tendon tissue from three cases of osteogenesis imperfecta (OI), are calculated and compared. The results are in agreement with recent biochemical studies in suggesting that type I (Sillence) OI is principally a quantitative, rather than a qualitative, defect of type I collagen biosynthesis. The features by which a molecular lesion may be recognised and characterised from diffraction data are discussed.
本文描述了利用X射线纤维衍射研究健康和患病人类肌腱的分子结构。推导得到了人类（手指）肌腱的三维高分辨率结构，结果表明其与大鼠尾腱的结构非常相似。特别是衍射图谱中38埃行线的存在表明，胶原纤维内高度的侧向有序性是肌腱组织比之前认识到的更为普遍的特征。计算并比较了该组织胶原纤维670埃单位重复的轴向投影电子密度图，以及三例成骨不全症（OI）患者的肌腱组织的轴向投影电子密度图。结果与最近的生化研究一致，表明I型（Sillence）OI主要是I型胶原生物合成的定量缺陷，而非定性缺陷。讨论了从衍射数据中识别和表征分子损伤的特征。
