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目的：体外条件下研究淀粉样蛋白膜内片段（intramembranous fragments of amyloid -β，IF-Aβ)对Aβ42 成纤维和神经毒性的影响。方法：（1）硫磺素T 法检测IF-Aβ 对Aβ42 成纤维性的影响；（2）MTT 法和荧光分光光度计检测IF-Aβ 对经过Aβ42 预处理的体外培养神经元的活性和胞浆钙离子浓度影响。结果：（1）IF-Aβ 本身无成纤维性，而且可以抑制或解聚Aβ42 成纤维；（2）相对于单独经Aβ42 预处理的体外培养神经元，IF-Aβ 的加入可以提高神经元的活性和降低胞浆钙离子的浓度。结论：IF-Aβ 具有保护体外培养神经元免受Aβ42 毒性作用的功能，为阿尔茨海默病（Alzheimer's disease，AD）的在体治疗研究奠定了基础。

英文摘要:

Objective: To study the effect of intramembranous fragments of amyloid- (IF-A ) on fibroplastic and neurotoxic activities of Aβ42 in vitro. Methods: Thioflavin T was applied to detect IF-A effect on Aβ42 assembly. The biological activity of the IF-A was assessed by the CellTiter 96 Cell Proliferation Assay (MTT assay). The calcium ion concentration in cell were also detected, as well as the mixtures of Aβ42: IF-A. Results: (1) IF-A showed no aggregation at concentrations up to 750 μM but substantial inhibition to Aβ42 fibril growth; (2)Compared with the in vitro cultured neuron which were treated only by Aβ42, that treated by IF-Aβ and Aβ42 (at a 1:1 concentration ratio) showed an increased activities and a decreased calcium ion concentration. Conclusion: IF-A could protect neuron viability from toxic damage by Aβ42 in vitro. It provides a foundation for the clinical treatment of Alzheimer's disease in vivo.

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