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TNF-α诱导的信号转导中乙酰化蛋白质全谱及其功能的探索 被引量：1

Global Protein Acetylation and Its Function in TNF-α-Induced Signal Transduction
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摘要 通过将体内稳定同位素标记细胞培养技术(AACT/SILAC)与LC-MS/MS联用,对哺乳动物细胞中TNF-α/NF-κB信号通路相关蛋白在TNF-α及TSA存在情况下乙酰化变化情况进行了研究.在TSA协同处理的、TNF-α刺激的细胞中鉴定到3个乙酰化蛋白,其中核糖体蛋白L4(60SRibosomal Protein L4,RPL4)已被报道存在乙酰化的后修饰,转铁蛋白受体1(Transferrin Receptor Protein 1,TfR1)和凋亡诱导因子3(ApoptosisInducing Factor,Mitochondrion-associated,3,AIFM3)尚未见报道. Using mass spectrometry based on AACT/SILAC quantitative proteomics strategy, we investigated theglobal protein acetylation in TNF-induced signal transduction with TSA treatment. As a result, we have identifiedthree acetylated proteins in the cytosol part among which TfR1 and AIFM3 haven＇t been reported. Biologicalprocess and molecular function analysis of the identified proteins provides us a more clear picture about globalprotein aeetylation through signal transduction.
作者 张晓夕 左帅 唐思伟 陈先
机构地区 复旦大学生物医学研究院 北卡罗来纳大学生物化学与生物物理系
出处 《复旦学报（自然科学版）》 CAS CSCD 北大核心 2015年第2期123-136,共14页 Journal of Fudan University：Natural Science
基金 国家高技术研究发展计划资助项目(2006AA02A310)
关键词 同位素氨基酸定量技术 定量蛋白质组学 TNF-Α LC-MS/MS RPL4 TFRC AIFM3 AACT/SILAC quantitative proteomics TNF-a LC-MS/MS RPL4 TfR1 AIFM3
分类号 O65 [理学—分析化学]
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复旦学报（自然科学版）
2015年 第2期

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