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盖膜中蛋白聚糖的超微结构

Ultrastructure of proteoglycans in the tectorial membrane.

作者信息

Santi P A, Lease M K, Harrison R G, Wicker E M

机构信息

Department of Otolaryngology, University of Minnesota Medical School, Minneapolis 55414.

出版信息

J Electron Microsc Tech. 1990 Jul;15(3):293-300. doi: 10.1002/jemt.1060150308.

Abstract

The ultrastructure of proteoglycans (PGs) in the tectorial membrane (TM) of the mature chinchilla cochlea was investigated using the cationic dye Cuprolinic blue. When used at a high critical electrolyte concentration, Cuprolinic blue has been shown specifically to bind to the glycosaminoglycan residues of sulfated PGs. After Cuprolinic blue treatment, PGs were observed in the TM which were represented as rod-shaped, electron-dense structures. A perifibrillar, primarily orthogonal, array of PGs was associated with the type A protofibrils. These PGs were distributed in 50 nm intervals along the length of the type A protofibrils. A less common orientation was parallel to the axis of the type A protofibrils. PGs did not appear to be associated with the type B protofibrils. Based upon previous results by other investigators, the TM contains types II and IX collagen, and it appears likely that the type A protofibrils are composed of collagen type II. PGs visualized in the TM in this study thus may represent the glycosaminoglycan residue of type IX collagen which is associated with the type II collagen fibrils. Alternatively, the TM PGs may be small dermatan or chondroitin sulfate PGs.

摘要

使用阳离子染料铜叶绿酸蓝对成熟毛丝鼠耳蜗盖膜(TM)中蛋白聚糖(PGs)的超微结构进行了研究。当在高临界电解质浓度下使用时,铜叶绿酸蓝已被证明能特异性结合硫酸化PGs的糖胺聚糖残基。经铜叶绿酸蓝处理后,在TM中观察到PGs呈现为杆状、电子致密结构。PGs的原纤维周围(主要是正交)排列与A型原纤维相关。这些PGs沿A型原纤维的长度以50nm的间隔分布。一种不太常见的取向是与A型原纤维的轴平行。PGs似乎与B型原纤维无关。根据其他研究者先前的结果,TM含有II型和IX型胶原蛋白,并且A型原纤维似乎由II型胶原蛋白组成。因此,本研究中在TM中可视化的PGs可能代表与II型胶原纤维相关的IX型胶原蛋白的糖胺聚糖残基。或者,TM PGs可能是小的硫酸皮肤素或硫酸软骨素PGs。

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