Mauger A, Kieny M, Goetinck P F
J Exp Zool. 1984 Nov;232(2):343-58. doi: 10.1002/jez.1402320221.
The immunofluorescent distribution of types I and III collagen, fibronectin, and laminin during muscle morphogenesis of the crooked neck dwarf mutant chick embryo differs from that of the normal chick. The drastic difference is related to the inability of the mutant embryo to maintain a harmonious muscle pattern. The first sign of the defect is the disaggregation of type I collagen fibers of the tendons and the disorganization of the intermuscular spaces. The organization of the connective tissue never proceeds beyond the appearance of an epimysial envelope, rich in types I and III collagen, which becomes disorganized shortly after. No perimysial envelopes displaying types I and III collagen fibers and fibronectin, nor endomysial sheaths develop. Only large spaces filled with types I and III collagen fibers subdivide groups of muscle cells irregularly. On the whole, type III collagen is less abundant than type I collagen. Fibronectin disappears from the periphery of the muscle cell. Laminin is more thickly deposited in the basal lamina around irregularly sized muscle cells than around the normal muscle cell. The results are discussed in terms of morphogenetic interactions between connective tissue cells and muscle cells, and in terms of fibrosis, which characterizes some muscle diseases.
在歪脖侏儒突变型鸡胚肌肉形态发生过程中,I型和III型胶原蛋白、纤连蛋白和层粘连蛋白的免疫荧光分布与正常鸡胚不同。这种显著差异与突变型胚胎无法维持和谐的肌肉模式有关。缺陷的第一个迹象是肌腱的I型胶原纤维解体以及肌间空间紊乱。结缔组织的组织化从未超过富含I型和III型胶原蛋白的肌外膜包膜的出现,而该包膜在不久后就会变得紊乱。没有出现显示I型和III型胶原纤维以及纤连蛋白的肌束膜包膜,也没有形成肌内膜鞘。只有充满I型和III型胶原纤维的大空间不规则地细分肌肉细胞群。总体而言,III型胶原蛋白比I型胶原蛋白含量少。纤连蛋白从肌肉细胞周边消失。层粘连蛋白在大小不规则的肌肉细胞周围的基膜中比在正常肌肉细胞周围沉积得更厚。本文从结缔组织细胞与肌肉细胞之间的形态发生相互作用以及一些肌肉疾病所特有的纤维化方面对结果进行了讨论。