文章摘要
尹力 叶雪瑞 刘新新 刘芳 于波.Sirt3对过氧化氢诱导的骨髓间充质干细胞凋亡的保护作用[J].,2015,15(31):6039-6042
Sirt3对过氧化氢诱导的骨髓间充质干细胞凋亡的保护作用
Protective Effect of Sirt3 on Mesenchymal StemCells Injured by HydrogenPeroxide
  
DOI:
中文关键词: 去乙酰化酶3  亲环蛋白d  骨髓间充质干细胞  凋亡  过氧化氢
英文关键词: Sirt3  Cyclophilin d  Mesenchymal stemcells  Apoptosis  Hydrogen peroxide
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作者单位
尹力 叶雪瑞 刘新新 刘芳 于波 哈尔滨医科大学附属第二医院心内科心肌缺血省部共建教育部重点实验室 
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中文摘要:
      目的:通过调控骨髓间充质干细胞(mesenchymal stemcells, MSCs)中的Sirtuin-3(Sirt3)蛋白的表达水平,阐明Sirt3对过氧化 氢(H2O2)诱导MSCs 凋亡的保护作用及其机制。方法:将大鼠MSCs 分为正常对照组、H2O2刺激组、H2O2+ Sirt3 转染组、H2O2 + Sirt3 siRNA 转染组。利用Western blot法检测Sirt3 及cyclophilin d 蛋白的表达水平、利用免疫沉淀法检测cyclophilin d乙酰化水 平、利用流式细胞仪检测细胞凋亡。结果:①H2O2刺激使MSCs 中Sirt3 表达水平降低。②转染Sirt3 可减少H2O2诱导的MSCs的 凋亡,而转染Sirt3 siRNA可增加H2O2诱导的MSCs的凋亡。③Sirt3蛋白的含量并不影响cyclophilin d的表达,但影响cyclophilin d 的乙酰化水平。结论:Sirt3 可能通过减少线粒体通透性转换孔(mitochondrial permeablity transition pore,mPTP)中的关键蛋 白cyclophilin d的乙酰化水平,进一步抑制mPTP的开放,从而减少H2O2诱导的MSCs 的凋亡。
英文摘要:
      Objective:To investigate the protective effect and mechanism of Sirt3 on apoptosis induced by hydrogen peroxide (H2O2) in MSCs by regulating the protein Sirt3 expression level.Methods:The rat MSCs were divided into 4 groups, respectively as normal control group, H2O2 stimulation group, H2O2 + Sirt3 transfection group, H2O2 + Sirt3 siRNA transfection group. The protein expression levels of Sirt3 and cyclophilin d were examined by Western blot and the acetylation level of cyclophlin d was examined by immunoprecipitation assay. Cells apoptosis was measured by flow cytometry.Results:① The expression of Sirt3 decreased compared with control group after H2O2 stimulation. ② The apoptotic ratio of cells was decreased after transfection of Sirt3, meanwhile, the apoptotic ratio of cells was improved after transfection of Sirt3 siRNA. ③ The acetylation level of cyclophilin d but not the expression level of protein cyclophilin d was influenced by regulating the protein Sirt3 expression level.Conclusion:Sirt3 might have an apoptosis-protective effect on MSCs induced by H2O2 though reducing opening of mPTP by deacetylateing cyclophilin d.
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