Franc S
Laboratory of Molecular Cytology, Claude Bernard University, Villeurbanne, France.
J Submicrosc Cytol Pathol. 1993 Jan;25(1):85-91.
The structure of collagen fibrils of tail tendon in young and mature rats was investigated by transmission (TEM) electron microscopy after cytochemical methods associated with special procedures of dehydration and fixation. All the collagen fibrils show a central condensed material of 4 nm in diameter which remains preserved even when fibrils have been swollen and partly disorganized by the ethyl glycol dehydration. A cytochemical characterization using PTA and TCH treatments strongly suggests the glycoprotein nature of this central compact material and reveals the heterogeneous structure of each fibril. The first morphological evidence that the construction of the collagen fibrils must take place around a condensed material which serves as a scaffolding is obtained. These observations are in agreement with the now well established existence of heterotypic collagen fibrils in many extracellular matrices.
通过与特殊脱水和固定程序相关的细胞化学方法，利用透射电子显微镜（TEM）研究了幼年和成年大鼠尾腱胶原纤维的结构。所有胶原纤维均显示出直径为4 nm的中央凝聚物质，即使在胶原纤维因乙二醇脱水而肿胀并部分解体时，该物质仍能保留。使用磷钨酸（PTA）和硫堇（TCH）处理进行的细胞化学表征有力地表明了这种中央致密物质的糖蛋白性质，并揭示了每条纤维的异质结构。获得了第一个形态学证据，即胶原纤维的构建必定围绕作为支架的凝聚物质进行。这些观察结果与现在已充分证实的许多细胞外基质中异型胶原纤维的存在相一致。
