Kokanova N A, Mikhaĭlova G Z, Shtanchaev R Sh, Tiras N R, Bezgina E N, Moshkov D A
Morfologiia. 2009;136(6):43-7.
The influence of aggregated beta-amyloid peptide fragment 25-35 application on three-dimensional structure and volume of Mauthner cells (MCs), as determined by reconstruction from serial histological sections, and on goldfish motor asymmetry was studied. It was shown that in intact and control goldfish motor asymmetry was stable and strongly correlated with structural asymmetry of neurons. But under the influence of beta-amyloid, motor asymmetry appeared to be strongly changed or inverted, did not correlate with structural asymmetry and frequently even was opposite to it. This resulted from strong dystrophy or, on the contrary, hypertrophy of individual neurons and their separate dendrites with the change in the proportions between them. It is suggested that injurious effect of beta-amyloid peptide on MCs structure, discordant with ("irregular") fish behavior, could be the result of mechanical deformation, induced by ribbon-like fibrils of amyloid peptide. These findings collectively suggest that MCs are the adequate object for the study of the structural aspects of amyloidosis.
通过对连续组织学切片进行重建，研究了聚集的β-淀粉样肽片段25-35的应用对金鱼Mauthner细胞（MCs）三维结构和体积的影响，以及对金鱼运动不对称性的影响。结果表明，在完整和对照金鱼中，运动不对称性是稳定的，并且与神经元的结构不对称性密切相关。但是在β-淀粉样蛋白的影响下，运动不对称性似乎发生了强烈变化或反转，与结构不对称性不相关，甚至常常与之相反。这是由于单个神经元及其单独的树突发生强烈营养不良或相反的肥大，以及它们之间比例的变化所致。有人认为，β-淀粉样肽对MCs结构的损伤作用与（“不规则”）鱼类行为不一致，可能是由淀粉样肽的带状纤维引起的机械变形所致。这些发现共同表明，MCs是研究淀粉样变性结构方面的合适对象。
