Raspanti M, Ottani V, Ruggeri A
Istituto di Anatomia Umana Normale, Bologna, Italy.
J Anat. 1990 Oct;172:157-64.
Collagen fibrils from different rat tendons have been investigated by freeze-fracture and transmission electron microscopy. In all cases, marked differences in both fibril morphology and subfibrillar organisation have been consistently found between the tendon core (composed of large and heterogeneous fibrils comprising tightly-packed, straight, parallel molecules) and sheath (showing small, uniform collagen fibrils with a helical arrangement of the molecules). The bio-mechanical requirements to which these tissues are subjected suggest, as do previous observations on other tissues, that a causal correlation exists between substructure and collagen fibril function.
通过冷冻断裂和透射电子显微镜对来自不同大鼠肌腱的胶原纤维进行了研究。在所有情况下，始终发现肌腱核心（由包含紧密排列、笔直、平行分子的大且异质的纤维组成）和鞘（显示具有分子螺旋排列的小而均匀的胶原纤维）之间在纤维形态和亚纤维组织方面存在明显差异。这些组织所承受的生物力学要求以及先前对其他组织的观察结果表明，亚结构与胶原纤维功能之间存在因果关系。
