Hickey D S, Hukins D W
Spine (Phila Pa 1976). 1982 May-Jun;7(3):234-42. doi: 10.1097/00007632-198205000-00007.
The macromolecular organization, in particular the collagen fibril network, of annulus fibrosus has been investigated, in humans and a strain of mice reared for aging research, by X-ray diffraction and electron microscopy. Collagen fibrils are arranged into fibers which are tilted so that the disc can perform its mechanical function. In neither mice nor humans did the tilt change with age, despite abnormal spinal curvature observed in aging mice. The spread of fibrils appears to decrease with age in anterior human annulus, but this is unlikely to affect function. Elastic fibers are associated with the collagen in mouse and human material of all ages. Aging is associated with the appearance of larger collagen fibrils, especially in human annulus. Increased radius and the biochemical changes which occur during aging may increase the likelihood of an overstressed region of annulus tearing.
通过X射线衍射和电子显微镜，对人类以及为衰老研究而饲养的某品系小鼠的纤维环的大分子结构，特别是胶原纤维网络进行了研究。胶原纤维排列成纤维束，这些纤维束呈倾斜状，以便椎间盘能够发挥其机械功能。尽管在衰老小鼠中观察到脊柱异常弯曲，但无论是小鼠还是人类，这种倾斜度都不会随年龄而改变。在人类纤维环前部，纤维束的分散似乎随年龄增长而减少，但这不太可能影响功能。在所有年龄段的小鼠和人类组织中，弹性纤维都与胶原相关联。衰老与更大的胶原纤维的出现有关，尤其是在人类纤维环中。半径增加以及衰老过程中发生的生化变化可能会增加纤维环过度受力区域撕裂的可能性。
