南方医科大学学报 ›› 2026, Vol. 46 ›› Issue (10): 2384-2392.doi: 10.12122/j.issn.1673-4254.2026.10.08

• • 上一篇    

铅暴露通过线粒体钙单向转运体介导的线粒体钙蓄积加重Aβ1-42处理的小胶质细胞活化

陈丽旋1(), 龙谚培1, 黄定帮1, 郑刚2, 孟晓静1()   

  1. 1.南方医科大学公共卫生学院职业卫生与职业医学系,广东 广州 510515
    2.空军军医大学军事预防医学系,特殊作业环境危害评估与防治教育部重点实验室,陕西 西安 710032
  • 收稿日期:2026-02-06 出版日期:2026-10-20 发布日期:2026-10-26
  • 通讯作者: 孟晓静 E-mail:923585950@qq.com;xiaojingmeng@smu.edu.cn
  • 作者简介:陈丽旋,在读硕士研究生,E-mail: 923585950@qq.com
  • 基金资助:
    国家自然科学基金(82473665);广东省自然科学基金(2024A1515012722)

Lead exposure aggravates Aβ1-42-induced microglial activation through mitochondrial calcium uniporter-mediated mitochondrial calcium accumulation

Lixuan CHEN1(), Yanpei LONG1, Dingbang HUANG1, Gang ZHENG2, Xiaojing MENG1()   

  1. 1.Department of Occupational Health and Occupational Medicine, School of Public Health, Southern Medical University, Guangzhou 510515, China
    2.Department of Military Preventive Medicine, Air Force Medical University, Ministry of Education Key Laboratory of Hazard Assessment and Control in Special Operational Environment, Xi'an 710032, China
  • Received:2026-02-06 Online:2026-10-20 Published:2026-10-26
  • Contact: Xiaojing MENG E-mail:923585950@qq.com;xiaojingmeng@smu.edu.cn
  • Supported by:
    National NaturalScience Foundation of China(82473665)

摘要:

目的 探讨线粒体钙单向转运体(MCU)在铅(Pb)暴露加重β淀粉样蛋白1-42(Aβ1-42)处理的小胶质细胞活化的作用,以揭示铅加重阿尔兹海默症(AD)样变的调控机制。 方法 将BV2细胞分为Control组(不予任何处理)、Aβ1-42组(10 μmol/L的Aβ1-42处理12 h)、Pb组(10 μmol/L铅处理细胞12 h)、Aβ1-42+Pb组(10 μmol/L的Aβ1-42处理1 h后加入10 μmol/L铅处理12 h)。ICP-MS检测BV2细胞的钙含量,相差显微镜观察BV2细胞的形态变化,细胞免疫荧光检测iNOS释放与氧化应激情况,Western blotting检测MCU蛋白表达量,CCK-8检测细胞活力。 结果 相比于Aβ1-42组,Aβ1-42+Pb组的细胞线粒体钙含量显著升高(P<0.001),MCU蛋白表达增多(P<0.05)。当下调MCU表达后,Pb与Aβ1-42联合处理的BV2细胞上清液对HT22细胞生长活力的损伤得到缓解(P>0.05)。铅与Aβ1-42联合处理可使BV2细胞活化,表现为胞体增大、突起增多,且Iba1与iNOS荧光信号均升高。下调MCU表达后,siMCU+Aβ1-42+Pb组的BV2细胞活化程度降低,显著缓解了氧化应激水平、线粒体钙超载及膜电位水平。 结论 铅暴露通过上调Aβ1-42处理的BV2细胞的MCU表达增加,使钙离子蓄积,引发氧化应激,加重了Aβ1-42处理的小胶质细胞活化引起的神经元损伤。

关键词: 铅, 线粒体钙单向转运体, 线粒体钙, β淀粉样蛋白1-42, 小胶质细胞活化

Abstract:

Objective To investigate the role of mitochondrial calcium uniporter (MCU) in lead (Pb)‑potentiated microglial activation induced by amyloid β‑protein (1-42) (Aβ1-42) and the regulatory mechanism by which Pb exacerbates Alzheimer disease (AD)-like pathology. Methods Cultured BV2 cells treated with 10 μmol/L Aβ1-42 for 12 h (Aβ1-42 group), 10 μmol/L Pb for 12 h (Pb group), or 10 μmol/L Aβ1-42 for 1 h followed by 10 μmol/L Pb for 12 h (Aβ1-42+Pb group) were examined for changes in intracellular calcium levels using ICP-MS. Morphological changes of the treated cells were observed, and iNOS release and oxidative stress were assessed with immunofluorescence staining. The changes in cellular MCU protein expression was determined with Western blotting, and cell viability was evaluated using CCK-8 assay. Results Compared with Aβ1-42-treated cells, the cells with the combined treatment showed significantly elevated mitochondrial Ca²⁺ content and increased MCU protein expression. Downregulation of MCU expression obviously alleviated the reduction of viability of HT22 cells treated with the supernatant from BV2 cells co-treated with Pb and Aβ1-42. The combined treatment with lead and Aβ1-42 caused activation of BV2 cells, manifested by increased cell volume and number of protrusions and intensified fluorescence signals of both Iba1 and iNOS. Downregulation of MCU expression significantly suppressed activation of BV2 cells in the siMCU+Aβ1-42+Pb group, and obviously lowered oxidative stress level, mitochondrial calcium overload, and membrane potential level in the cells. Conclusion Pb exposure exacerbates neuronal injury mediated by Aβ1-42-activated microglia through upregulation of MCU expression, which causes mitochondrial calcium accumulation to trigger oxidative stress.

Key words: lead (Pb), mitochondrial calcium uniporter, mitochondrial calcium, Aβ1-42, microglial activation