当前位置: X-MOL 学术Metallomics › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction
Metallomics ( IF 3.4 ) Pub Date : 2018-07-03 , DOI: 10.1039/c8mt00091c
Hyuck Jin Lee 1, 2, 3, 4 , Masha G. Savelieff 5, 6, 7 , Juhye Kang 1, 1, 2, 3, 4 , Megan Brunjes Brophy 1, 7, 8, 9 , Toshiki G. Nakashige 1, 7, 8, 9 , Shin Jung C. Lee 1, 4, 10, 11 , Elizabeth M. Nolan 1, 7, 8, 9 , Mi Hee Lim 1, 2, 3, 4
Affiliation  

Proteins from the S100 family perform numerous functions and may contribute to Alzheimer's disease (AD). Herein, we report the effects of S100A8/S100A9 heterooligomer calprotectin (CP) and the S100B homodimer on metal-free and metal-bound amyloid-β (Aβ; Aβ40 and Aβ42) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for Aβ40 in both the absence and presence of metal ions [i.e., Zn(II) and Cu(II)]. Moreover, the detection of Aβ40–CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in Aβ40 aggregation. Although the interaction of CP-Ser with Aβ40 impacts Aβ40 aggregation in vitro, the protein does not attenuate Aβ-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of Aβ. Overall, this work supports a potential association of CP with Aβ in the absence and presence of metal ions in AD.

中文翻译:

钙卫蛋白通过直接相互作用影响无金属和金属结合的淀粉样β的聚集

S100家族的蛋白质具有多种功能,可能会导致阿尔茨海默氏病(AD)。在本文中,我们报道了S100A8 / S100A9异寡聚钙卫蛋白(CP)和S100B同型二聚体在体外对无金属和金属结合的淀粉样β(Aβ; Aβ40Aβ42)聚集的影响。用CP-Ser [S100A8(C42S)/ S100A9(C3S)低聚物]进行的研究表明,该蛋白质会在不存在和存在金属离子(Zn(II)和Cu(II))的情况下影响Aβ40的聚集曲线。]。此外,Aβ40的检测质谱分析表明,CP-Ser复合物的直接相互作用是CP参与Aβ40聚集的一种可能机制。尽管CP-Ser与Aβ40的相互作用在体外会影响Aβ40的聚集,但该蛋白并不能减弱Aβ诱导的SH-SY5Y细胞毒性。相反,S100B对Aβ的聚集有轻微影响。总体而言,这项工作支持在AD中不存在和存在金属离子的情况下CP与Aβ的潜在关联。
更新日期:2018-08-15
down
wechat
bug