Jiménez J L, Tennent G, Pepys M, Saibil H R
Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
J Mol Biol. 2001 Aug 10;311(2):241-7. doi: 10.1006/jmbi.2001.4863.
Cryo-electron microscopy studies are presented on amyloid fibrils isolated from amyloidotic organs of two patients with different forms of hereditary non-neuropathic systemic amyloidosis, caused, respectively, by Leu60Arg apolipoprotein AI and Asp67His lysozyme. Although ex vivo amyloid fibrils were thought to be more uniform in structure than those assembled in vitro, our findings show that these fibrils are also quite variable in structure. Structural disorder and variability of the fibrils have precluded three-dimensional reconstruction, but averaged cryo-electron microscopy images suggest models for protofilament packing in the lysozyme fibrils. We conclude that ex vivo amyloid fibrils, although variable, assemble as characteristic structures according to the identity of the precursor protein.
本文展示了对从两名患有不同形式遗传性非神经性系统性淀粉样变性患者的淀粉样变性器官中分离出的淀粉样纤维进行的冷冻电子显微镜研究。这两名患者的疾病分别由Leu60Arg载脂蛋白AI和Asp67His溶菌酶引起。尽管人们认为离体淀粉样纤维在结构上比体外组装的纤维更均匀，但我们的研究结果表明，这些纤维在结构上也存在很大差异。纤维的结构无序和变异性妨碍了三维重建，但平均冷冻电子显微镜图像为溶菌酶纤维中原丝堆积提供了模型。我们得出结论，离体淀粉样纤维尽管存在变异性，但会根据前体蛋白的特性组装成特征性结构。
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