Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits
Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits
复制标题
DOI：
10.1073/pnas.1523496113
复制
发表时间：
2016-05-17
影响因子：
11.1
通讯作者：
Faendrich, Marcus
中科院分区：
文献类型：
--
作者：
Kollmer, Marius;Meinhardt, Katrin;Faendrich, Marcus
电子断层扫描是研究大分子复合物或细胞结构详细结构的一种日益强大的方法。应用于系统性淀粉样蛋白a淀粉样变性的细胞培养模型中形成的淀粉样蛋白沉积物，我们可以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，根据纤维的相对取向，我们可以区分成纤维网状、纤维束和淀粉样星形。这些网络经常被泡状脂质包涵体浸润，这可能源于淀粉样形成细胞的死亡。我们的数据支持非纤维成分在构建纤维沉积物中的作用，并提供了不同类型的脂质-纤维相互作用的结构视图。
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.