Knupp C, Chew M, Squire J
The Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, SW7 2BZ, United Kingdom.
J Struct Biol. 1998;122(1-2):101-10. doi: 10.1006/jsbi.1998.3994.
The collagen which forms the egg case of the dogfish, Scyliorhinus canicula, is assembled in a three-dimensional network that results in a very resistant capsule. The capsule presumably accomplishes both a protective and a filtering role for the embryo contained within it. In the present work we have obtained electron micrographs of metal-shadowed, deep-etched replicas of the egg case and we have analyzed the micrographs using computer-based Fourier methods. The replicas provide details of the three-dimensional structure that have not been recorded before, allowing us to add particulars to the [1,0,0], [1,1,0], and [0,0,1] views previously obtained from plastic sections (C. Knupp et al., 1996, J. Struct. Biol. 117, 209-221). A molecular packing arrangement consistent with all of the present data is proposed. Although this collagen type is unique and is substantially shorter (45 nm) than other collagens, investigations into its structure may give an insight into related collagen types. The role of this collagen as both a protective structure and one with filtering properties controlling permeability is discussed in terms of other collagens with similar functions.
形成角鲨(Scyliorhinus canicula)卵鞘的胶原蛋白组装成三维网络结构,形成了一个非常坚韧的囊。这个囊大概对其中所含的胚胎起到保护和过滤的作用。在本研究中,我们获得了卵鞘的金属阴影、深度蚀刻复制品的电子显微照片,并使用基于计算机的傅里叶方法对这些显微照片进行了分析。这些复制品提供了以前未记录的三维结构细节,使我们能够为先前从塑料切片获得的[1,0,0]、[1,1,0]和[0,0,1]视图补充细节(C. Knupp等人,1996年,《结构生物学杂志》117卷,209 - 221页)。提出了一种与所有现有数据一致的分子堆积排列方式。尽管这种胶原蛋白类型独特,且比其他胶原蛋白短得多(45纳米),但对其结构的研究可能有助于深入了解相关的胶原蛋白类型。本文从具有类似功能的其他胶原蛋白的角度,讨论了这种胶原蛋白作为保护结构以及具有控制渗透性的过滤特性的作用。