Lawson D
J Cell Biol. 1984 Oct;99(4 Pt 1):1451-60. doi: 10.1083/jcb.99.4.1451.
In this study I describe the ultrastructural distribution of epinemin (Lawson, D., 1983, J. Cell Biol., 97:1891-1905) in antibody-labelled, helium-cooled, quick-frozen, deep-etched cytoskeletons. This technique reveals that epinemin is expressed asymmetrically at discrete sites on the vimentin core polymer and that usually one (occasionally two or three) antiepinemin molecules are found at each of these discrete foci. Single receptor-bound antiepinemin (IgM) molecules are easily identified in deep-etched cytoskeletons by the use of colloidal gold. Epinemin does not cross-link adjacent intermediate filaments and is not associated with the many 2-3-nm filaments found associated with intermediate filaments in these preparations. The directional changes and interactions undergone by microtubules in taxol-stabilized, antibody-labelled cytoskeletons are also discussed.
在本研究中,我描述了表皮纤丝蛋白(劳森,D.,1983年,《细胞生物学杂志》,97:1891 - 1905)在抗体标记、氦冷却、快速冷冻、深度蚀刻的细胞骨架中的超微结构分布。该技术揭示,表皮纤丝蛋白在波形蛋白核心聚合物的离散位点不对称表达,并且通常在每个这些离散位点发现一个(偶尔两个或三个)抗表皮纤丝蛋白分子。通过使用胶体金,在深度蚀刻的细胞骨架中很容易识别单个受体结合的抗表皮纤丝蛋白(IgM)分子。表皮纤丝蛋白不交联相邻的中间丝,并且与在这些制剂中发现的与中间丝相关的许多2 - 3纳米细丝无关。还讨论了在紫杉醇稳定、抗体标记的细胞骨架中微管所经历的方向变化和相互作用。