Key Laboratory of Cell Biology of Ministry of Public Health of China, Laboratory of Cell Engineering and Therapy of Institute of Tissue Engineering, China Medical University, Shenyang, PR China.
J Alzheimers Dis. 2010;20(1):323-31. doi: 10.3233/JAD-2010-1363.
The presence of senile plaques containing abundant amyloid-beta (Abeta) peptide is one of the major pathological hallmarks of Alzheimer's disease (AD). Recent studies support the notion that overexpression of zinc transporters (ZnT) is involved in zinc metabolic disturbances and Abeta aggregation in AD brains. Here we present data showing an elevated expression of zinc transporter 3 (ZnT3) protein, revealed by immunoblotting assay, in the cerebellum of the amyloid-beta protein precursor (AbetaPP)/presenilin 1 (PS1) transgenic mouse. Confocal microscopic and autometallographic results showed that ZnT3 immunofluorescence and zinc ions were predominantly located in the amyloid plaques. ZnT3 protein was abundantly distributed throughout the plaques, whereas zinc ions were mainly located in the peripheral parts of rosette-shaped plaques with a lightly stained center. Collectively, our results suggest that ZnT3 protein is involved in the Abeta aggregation in the cerebellum of the AbetaPP/PS1 mouse.
淀粉样斑块中富含淀粉样β肽(Abeta)是阿尔茨海默病(AD)的主要病理学特征之一。最近的研究支持这样一种观点,即锌转运体(ZnT)的过度表达与 AD 大脑中的锌代谢紊乱和 Abeta 聚集有关。在这里,我们提供的数据显示,淀粉样前体蛋白(AbetaPP)/早老素 1(PS1)转基因小鼠小脑中的锌转运蛋白 3(ZnT3)蛋白表达升高,通过免疫印迹检测证实。共聚焦显微镜和自动金属成像结果表明,ZnT3 免疫荧光和锌离子主要位于淀粉样斑块中。ZnT3 蛋白在斑块中广泛分布,而锌离子主要位于玫瑰花结状斑块的外周部分,中心染色较浅。总之,我们的结果表明,ZnT3 蛋白参与了 AbetaPP/PS1 小鼠小脑的 Abeta 聚集。