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  

Global Protein Acetylation and Its Function in TNF-α-Induced Signal Transduction

作　　者：张晓夕[1] 左帅[1] 唐思伟[1] 陈先[1,2] 

机构地区：[1]复旦大学生物医学研究院,上海200032 [2]北卡罗来纳大学生物化学与生物物理系,美国北卡罗来纳州教堂山27599

出　　处：《复旦学报（自然科学版）》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)

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.

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 

分 类 号：O65[理学—分析化学]