Tsuprun V, Santi P
Department of Otolaryngology, University of Minnesota, Minneapolis 55455, USA.
Hear Res. 1997 Aug;110(1-2):107-18. doi: 10.1016/s0378-5955(97)00068-3.
The molecular and supramolecular structure of the tectorial membrane (TM) was studied by transmission electron microscopy (TEM). Collagen (type A) fibrils in the TM were found associated with proteoglycans (PGs) and type B fibrils. Most PGs were orthogonally oriented and attached D-periodically to collagen fibrils. Computer averaged projections of PG particles and linear aggregates of PGs in crystalline arrays, stained with Cuprolinic blue, showed an elongated, electron-dense structure 50-65 nm in length and 10 nm in width. Image analysis of type B fibrils showed that they are constructed of globular domains arranged with a periodicity of 12-14 nm. Each globular domain contains two thin 'arms', extended in opposite directions, which contact the 'arms' of adjacent fibrils. Numerous type B fibrils were found between collagen fibrils. They are attached to adjacent collagen fibrils by the 'arms' of their globular domains. An association of type B fibrils and PGs with collagen seems to result in the local ordered arrangement of the TM matrix. A hypothetical model of the TM matrix supramolecular structure is presented.
通过透射电子显微镜（TEM）研究了盖膜（TM）的分子和超分子结构。发现TM中的A型胶原纤维与蛋白聚糖（PGs）和B型纤维相关。大多数PGs呈正交取向，并以D周期方式附着于胶原纤维。用铜蓝染色的PG颗粒和PG晶体阵列中的线性聚集体的计算机平均投影显示，其为细长的电子致密结构，长度为50 - 65 nm，宽度为10 nm。对B型纤维的图像分析表明，它们由周期性排列为12 - 14 nm的球状结构域构成。每个球状结构域包含两条向相反方向延伸的细“臂”，这些“臂”与相邻纤维的“臂”接触。在胶原纤维之间发现了大量B型纤维。它们通过球状结构域的“臂”附着于相邻的胶原纤维。B型纤维和PGs与胶原的结合似乎导致了TM基质的局部有序排列。本文提出了TM基质超分子结构的假设模型。
