Thalmann I
Department of Otolaryngology, Washington University School of Medicine, St. Louis, MO 63110.
Connect Tissue Res. 1993;29(3):191-201. doi: 10.3109/03008209309016826.
It was previously demonstrated that about 40% of the protein of the tectorial membrane of the guinea pig consists of collagen type II, with lesser amounts of type IX and XI. In this paper we extend these studies on the tectorial membrane to the basilar membrane and to other accessory structures, the spiral ligament and spiral limbus. Earlier immunohistochemical data indicated that no collagen type II is present in the basilar membrane of the newborn guinea pig, but that it is present in the area of the basilar membrane in the embryo. However, by means of stringent extraction procedures we have determined biochemically that collagen type II and lesser amounts of type XI are present in the basilar membrane of the adult guinea pig, at similar levels (on the basis of total protein) to the tectorial membrane. Levels of collagen type II are much lower in the spiral ligament and spiral limbus. The presented studies demonstrate that classical techniques of collagen chemistry can be applied at the microscale on minute tissue elements. The significance of the presence of collagen in the tectorial membrane and basilar membrane is discussed in the light of known mechanical properties of these structures.
先前的研究表明，豚鼠盖膜中约40%的蛋白质由II型胶原蛋白组成，IX型和XI型胶原蛋白的含量较少。在本文中，我们将对盖膜的这些研究扩展到基底膜以及其他附属结构，即螺旋韧带和螺旋缘。早期的免疫组织化学数据表明，新生豚鼠的基底膜中不存在II型胶原蛋白，但在胚胎期基底膜区域存在该型胶原蛋白。然而，通过严格的提取程序，我们已经通过生化方法确定，成年豚鼠的基底膜中存在II型胶原蛋白和少量的XI型胶原蛋白，其含量（基于总蛋白）与盖膜相似。螺旋韧带和螺旋缘中的II型胶原蛋白水平要低得多。本文的研究表明，经典的胶原蛋白化学技术可以应用于微小组织成分的微观尺度研究。根据这些结构已知的力学特性，讨论了盖膜和基底膜中胶原蛋白存在的意义。
