Department of Human Morphology, Insubria University, Varese, Italy.
Biomacromolecules. 2011 Dec 12;12(12):4344-7. doi: 10.1021/bm201314e. Epub 2011 Nov 16.
The collagen fibrils of cornea, blood vessel walls, skin, gut, interstitial tissues, the sheath of tendons and nerves, and other connective tissues are known to be made of helically wound subfibrils winding at a constant angle to the fibril axis. A critical aspect of this model is that it requires the axial microfibrils to warp in an implausible way. This architecture lends itself quite naturally to an epitaxial layout where collagen microfibrils envelop a central core of a different nature. Here we demonstrate an axial domain in collagen fibrils from rabbit nerve sheath and tendon sheath by means of transmission electron microscopy after a histochemical reaction designed to evidence all polysaccharides and by tapping-mode atomic force microscopy. This axial domain was consistently found in fibrils with helical microfibrils but was not observed in tendon, whose microfibrils run longitudinal and parallel.
众所周知，角膜、血管壁、皮肤、肠道、间质组织、肌腱和神经鞘以及其他结缔组织的胶原原纤维是由螺旋缠绕的亚纤维组成的，这些亚纤维以恒定的角度缠绕在纤维轴上。该模型的一个关键方面是，它要求轴向微纤维以一种不太可能的方式扭曲。这种结构非常适合于外延排列，其中胶原微纤维包裹着不同性质的中心核。在这里，我们通过设计用于证明所有多糖的组织化学反应和敲击模式原子力显微镜，展示了来自兔神经鞘和肌腱鞘的胶原原纤维中的轴向结构域。在具有螺旋微纤维的原纤维中始终发现了这个轴向结构域，但在肌腱中没有观察到，肌腱的微纤维是纵向和平行的。
