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来自心脏和神经的ATTRv-V30M粉样纤维呈现结构均性

Binh An Nguyen¹, Shumaila Afrin¹, Anna Yakubovska¹

¹Center for Alzheimer's and Neurodegenerative Diseases, University of Texas Southwestern Medical Center (UTSW), Dallas, TX 75390, USA; Department of Biophysics, University of Texas Southwestern Medical Center (UTSW), Dallas, TX 75390, USA; Peter O'Donnell Jr Brain Institute, University of Texas Southwestern Medical Center (UTSW), Dallas, TX 75390, USA.

Structure (London, England : 1993)

|October 18, 2024

概括

在ATTRv-V30M患者的心脏和神经组织中,amyloidogenic transthyretin amyloidosis (ATTR) 纤维结构一致. 这表明当 transthyretin 来自肝脏时,纤维结构是均的.

科学领域:

生物物理学的生物物理.
分子生物学分子生物学
医学研究医学研究

背景情况:

氨基基氨酸转原蛋白 (ATTR) 氨基化症涉及转原蛋白氨酸纤维的沉积.
晶氨酸主要由肝脏产生,影响心脏和神经.
ATTRv-V30M是一种特定的遗传变异,会导致全身性粉症.

研究的目的:

研究来自不同组织的ATTR粉样纤维的结构特征.
为了比较ATTRv-V30M患者心脏和神经组织中的纤维结构.
了解组织起源对ATTR氨基粉症中的纤维结构的影响.

主要方法:

使用冷电子显微镜 (cryo-EM) 分析提取的粉样纤维.
从单个ATTRv-V30M患者的心脏和外围神经组织中获得纤维.
结构性比较与以前描述的ATTR纤维素进行了比较.

主要成果:

在心脏和神经组织中观察到一致的纤维结构.
这些结构与之前描述的心脏ATTR纤维相似.
与同一个基因型的玻璃体纤维相比,观察到一个差异.

结论:

当transthyretin来自肝脏时,ATTR纤维结构在不同组织中看起来是一致的.
这种统一性适用于ATTRv-V30M变种.
了解纤维结构是ATTR氨基粉症病原体的关键.

关键词:

在ATTR上,ATTR就是ATTR.这就是V30M突变.低温电磁波冷却器 (Cryo-EM) 是一个非常好的方法.螺旋式重建螺旋式重建周围神经纤维的纤维.系统性氨基粉症.转胺氨基粉症的发生.

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相关概念视频

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...