Montes G S, Becerra J, Toledo O M, Gordilho M A, Junqueira L C
Histochemistry. 1982;75(3):363-76. doi: 10.1007/BF00496739.
Ultrastructural and histochemical studies performed on the skeletal elements of the tail fins of six representative species of teleosts enabled the following observations to be made. The electron microscopic pattern of amorphous substance deposition, and the diameter of the collagen fibrils, in lepidotrichia closely resemble those which are typical of cartilage. In addition, lepidotrichia contain chondroitin sulfate AC as the only sulfated glycosaminoglycan, and this glycosaminoglycan shows high levels of interaction with collagen, both features being characteristic of cartilage. Furthermore, the histochemical data presented in this paper suggest that not all of the glycosaminoglycans present in lepidotrichia are bound to protein cores to form proteoglycans. Each actinotrichium consists of a single ultrastructural entity of remarkable width and, thus, is not composed of a bundle of discretely separated collagen fibrils but rather of hyperpolymerized collagen molecules. This aspect differs from the arrangement pattern of all the other interstitial collagens, suggesting that actinotrichia may contain a new type of collagen.
对六种有代表性的硬骨鱼的尾鳍骨骼成分进行的超微结构和组织化学研究得出了以下观察结果。在鳍条中,无定形物质沉积的电子显微镜模式以及胶原纤维的直径与软骨的典型模式非常相似。此外,鳍条含有硫酸软骨素AC作为唯一的硫酸化糖胺聚糖,并且这种糖胺聚糖与胶原表现出高水平的相互作用,这两个特征都是软骨的特征。此外,本文提供的组织化学数据表明,鳍条中存在的并非所有糖胺聚糖都与蛋白核心结合形成蛋白聚糖。每根鳍条由一个宽度显著的单一超微结构实体组成,因此,它不是由一束离散分离的胶原纤维组成,而是由超聚合的胶原分子组成。这一方面与所有其他间质胶原的排列模式不同,表明鳍条可能含有一种新型胶原。