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Medin寡聚体膜孔形成:血管功能障碍的一种潜在机制。

Medin Oligomer Membrane Pore Formation: A Potential Mechanism of Vascular Dysfunction.

作者信息

Younger Scott, Jang Hyunbum, Davies Hannah A, Niemiec Martin J, Garcia Joe G N, Nussinov Ruth, Migrino Raymond Q, Madine Jillian, Arce Fernando T

机构信息

Department of Biomedical Engineering, University of Arizona, Tucson, Arizona.

Computational Structural Biology Section, Basic Science Program, Frederick National Laboratory for Cancer Research, Frederick, Maryland.

出版信息

Biophys J. 2020 Jun 2;118(11):2769-2782. doi: 10.1016/j.bpj.2020.04.026. Epub 2020 May 1.

Abstract

Medin, a 50-amino-acid cleavage product of the milk fat globule-EGF factor 8 protein, is one of the most common forms of localized amyloid found in the vasculature of individuals older than 50 years. Medin induces endothelial dysfunction and vascular inflammation, yet despite its prevalence in the human aorta and multiple arterial beds, little is known about the nature of its pathology. Medin oligomers have been implicated in the pathology of aortic aneurysm, aortic dissection, and more recently, vascular dementia. Recent in vitro biomechanical measurements found increased oligomer levels in aneurysm patients with altered aortic wall integrity. Our results suggest an oligomer-mediated toxicity mechanism for medin pathology. Using lipid bilayer electrophysiology, we show that medin oligomers induce ionic membrane permeability by pore formation. Pore activity was primarily observed for preaggregated medin species from the growth-phase and rarely for lag-phase species. Atomic force microscopy (AFM) imaging of medin aggregates at different stages of aggregation revealed the gradual formation of flat domains resembling the morphology of supported lipid bilayers. Transmission electron microscopy images showed the coexistence of compact oligomers, largely consistent with the AFM data, and larger protofibrillar structures. Circular dichroism spectroscopy revealed the presence of largely disordered species and suggested the presence of β-sheets. This observation and the significantly lower thioflavin T fluorescence emitted by medin aggregates compared to amyloid-β fibrils, along with the absence of amyloid fibers in the AFM and transmission electron microscopy images, suggest that medin aggregation into pores follows a nonamyloidogenic pathway. In silico modeling by molecular dynamics simulations provides atomic-level structural detail of medin pores with the CNpNC barrel topology and diameters comparable to values estimated from experimental pore conductances.

摘要

Medin是乳脂肪球表皮生长因子8蛋白的一种由50个氨基酸组成的裂解产物,是在50岁以上个体的脉管系统中发现的最常见的局部淀粉样蛋白形式之一。Medin会诱导内皮功能障碍和血管炎症,然而,尽管它在人类主动脉和多个动脉床中普遍存在,但对其病理学本质却知之甚少。Medin寡聚体与主动脉瘤、主动脉夹层的病理学有关,最近还与血管性痴呆有关。最近的体外生物力学测量发现,主动脉壁完整性改变的动脉瘤患者中寡聚体水平升高。我们的结果表明Medin病理学存在一种寡聚体介导的毒性机制。使用脂质双层电生理学方法,我们发现Medin寡聚体通过形成孔道诱导离子膜通透性。孔道活性主要在生长阶段的预聚集Medin物种中观察到,而在滞后阶段的物种中很少观察到。对Medin聚集体在不同聚集阶段的原子力显微镜(AFM)成像显示,逐渐形成了类似于支撑脂质双层形态的扁平结构域。透射电子显微镜图像显示紧密寡聚体与较大的原纤维结构共存,这在很大程度上与AFM数据一致。圆二色光谱显示存在大量无序物种,并表明存在β-折叠。这一观察结果以及与淀粉样β纤维相比,Medin聚集体发出的硫黄素T荧光显著较低,再加上AFM和透射电子显微镜图像中没有淀粉样纤维,表明Medin聚集成孔遵循非淀粉样生成途径。通过分子动力学模拟进行的计算机模拟提供了具有CNpNC桶状拓扑结构且直径与根据实验孔道电导率估计的值相当的Medin孔道的原子级结构细节。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2a95/7264854/89fb8b064ad9/gr1.jpg

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