电子断层扫描揭示了淀粉样沉积物中的纤维结构和脂质相互作用。
Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits.
作者信息
Kollmer Marius, Meinhardt Katrin, Haupt Christian, Liberta Falk, Wulff Melanie, Linder Julia, Handl Lisa, Heinrich Liesa, Loos Cornelia, Schmidt Matthias, Syrovets Tatiana, Simmet Thomas, Westermark Per, Westermark Gunilla T, Horn Uwe, Schmidt Volker, Walther Paul, Fändrich Marcus
机构信息
Institute of Protein Biochemistry, Ulm University, 89081 Ulm, Germany;
Institute of Stochastics, Ulm University, 89081 Ulm, Germany;
出版信息
Proc Natl Acad Sci U S A. 2016 May 17;113(20):5604-9. doi: 10.1073/pnas.1523496113. Epub 2016 May 2.
Electron tomography is an increasingly powerful method to study the detailed architecture of macromolecular complexes or cellular structures. Applied to amyloid deposits formed in a cell culture model of systemic amyloid A amyloidosis, we could determine the structural morphology of the fibrils directly in the deposit. The deposited fibrils are arranged in different networks, and depending on the relative fibril orientation, we can distinguish between fibril meshworks, fibril bundles, and amyloid stars. These networks are frequently infiltrated by vesicular lipid inclusions that may originate from the death of the amyloid-forming cells. Our data support the role of nonfibril components for constructing fibril deposits and provide structural views of different types of lipid-fibril interactions.
电子断层扫描是一种用于研究大分子复合物或细胞结构详细架构的功能日益强大的方法。应用于系统性淀粉样蛋白A淀粉样变性细胞培养模型中形成的淀粉样沉积物，我们能够直接确定沉积物中原纤维的结构形态。沉积的原纤维排列成不同的网络，根据原纤维的相对取向，我们可以区分原纤维网络、原纤维束和淀粉样星状体。这些网络经常被可能源自形成淀粉样蛋白的细胞死亡的囊泡脂质内含物浸润。我们的数据支持非原纤维成分在构建原纤维沉积物中的作用，并提供了不同类型脂质-原纤维相互作用的结构视图。
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