蛋白磷酸酶2A催化亚基PP-2Aca过表达的蛋白质组学及其功能研究
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摘要
蛋白磷酸酯酶2A(Protein phosphatase 2A,PP2A)是一种真核生物中最保守的丝氨酸/苏氨酸磷酸酯酶,也是真核生物中含量最丰富的酶之一。它能够对激酶、信号分子等大量细胞内蛋白质进行去磷酸化,并且参与了与细胞分裂、细胞凋亡、基因调控、蛋白质合成及细胞骨架组织相关的一系列重要生物学进程。典型的PP2A全酶以异三聚体形式存在,由催化亚基C、结构亚基A以及调节亚基B组成。
有关B亚基对细胞转化的研究有较多的报道,最近实验也证明A亚基与肿瘤的生成有直接的关系,为PP2A作为肿瘤抑制因子提供了确凿的证据。但是关于C亚基与癌症发生之间关系的报道则很少。
为了研究PP-2A催化亚基在癌症中的可能作用,我们研究小组在前期的工作中建立了PP-2A催化亚基C过表达的两种癌细胞的稳定克隆,即小鼠上皮细胞JB6(pCI-PP2Aca-JB6)和人的肺癌细胞H1299(pCI-PP2Aca-H1299)。利用这两种稳定的细胞系以及转染了载体的稳定细胞系(pCI-Neo-JB6;pCI-Neo-H1299),我们通过蛋白质组学技术、基因芯片技术及其它分子生物学技术对过表达外源性PP-2Aca可能对细胞产生的影响进行了研究。
本论文通过基于胶的双向电泳/质谱偶联蛋白质组学研究技术及基于稳定同位素标记与质谱偶联蛋白质组学定量技术对pCI-PP2Aca-JB6细胞和pCI-neo-JB6细胞在蛋白质组水平的差异表达进行了分析。另外本课题组其他研究人员采用基因芯片技术获得pCI-PP2Aca-JB6细胞在mRNA水平的差异表达数据。这些数据显示虽然下游基因在蛋白水平及mRNA水平的表达存在一些不一致的地方,但是我们发现无论是通过基因芯片所得到的pCI-PP2Aca-JB6细胞与pCI-neo-JB6细胞在mRNA水平的差异表达数据还是通过蛋白质组技术得到的蛋白质水平的差异表达数据都表明pCI-PP2Aca过表达引起了下游基因表达的显著变化。我们发现,与对照相比,pCI-PP2Aca-JB6细胞中包括氧化应激、蛋白质代谢及转运、碳水化合物及能量代谢、蛋白质折叠、转录调控、信号转导、细胞骨架等多条信号通路的发生了变化。结果显示,过氧化氢酶、过氧化物酶、醛脱氢酶、视黄醛脱氢酶、硫氧还蛋白、硫氧还蛋白2、硫氧还蛋白4、硫氧还蛋白6及谷胱甘肽S-转移酶等这些在细胞中清除细胞产生的活性氧、活性氮以及一些醛类活性中间产物等有害物质的酶类和蛋白明显出现了下调,从而通过一些未知机制增强了细胞的转化。相应地,与蛋白质折叠相关的一些蛋白如splicing isoform 1 of smallglutamine-rich tetratricopeptide repeat-containing protein A,calreticulinprecursor,protein disulfide-isomerase precursor和tetratricopeptiderepeat protein表达上调,这表明分子伴侣的活性增强是pCI-PP2Aca-JB6细胞转化所必须的。而Prohibitin(phb)和annexin Al这些种肿瘤抑制因子的表达下调也支持PP2Aca的肿瘤生成功能。总之,这些结果提示我们pCI-PP2Aca-JB6细胞显示出一些转化的癌细胞的特征。
本实验通过过表达PP-2Aca及用OA抑制PP2A的活性的实验证明,PP-2A通过直接对P-p53-ser-15的磷酸化状态的调控来调节p53的活性。另外,我们的实验显示,通过负调控直接控制Cathepsin基因Ctsb的启动子p53,PP-2A正调控Cathepsin B的表达水平从而促进了细胞的转化。这个结论在H1299细胞中也得到证实。
综上所述,我们的实验结果显示,PP-2Aca的稳定过表达引起了JB6细胞蛋白质表达方式的显著变化,从而促进了细胞转化。同时结果也显示PP-2A可能是通过调节p53-cathepsin B信号通路促进了细胞的转化。
Protein phosphatase 2A(PP-2A) is one of the most abundant and conserved serine/threonine phosphatase hin eukaryotes.It dephosphorylates a panel of cellular proteins such as kinases and other signal molecules,and participates in many cellular processes including cell division,cell apoptosis,gene regulation,protein synthesis, cytoskeleton organization and so on.The PP-2A holoenzyme exists as a heterotrimer,consisting of a catalytic C subunit,a structural A subunit and a regulatory B subunit.
Previous studies have shown that the regulatory B subunit of PP-2A plays a crucial role in cell transformation.In addition,recent studies have also demonstrated that the structural A subunit of PP-2A is also implicated in carcinogenesis.Whether the catalytic C subunits of this phosphatase play a role in cancer remains to be explored.
To explore the possible function of the catalytic subunit of PP-2A in cancer,our group has previously established the stable clones overexpressing the catalytic C subunit of PP-2A in both mouse skin cancer,JB6 cells(pCI-PP2Aca-JB6) and human lung cancer,H1299 cells (pCI-PP2Aca-H1299).Using these stable cell lines and also vector-transfected control cell lines(pCI-Neo-JB6;pCI-Neo-H1299),we have investigated the possible effects of the overexpressed exogenous PP-2Aca in these cells using proteomics,cDNA microarray and other molecular biology techniques.
The differential expression patterns of total proteins between pCI-Neo-JB6 and pCI-PP2Aca-JB6 were analyzed using proteomics which was based on 2-D gel separation coupled with mass spectrum analysis or the samples labeled by ~(18)O coupled with mass spectrum analysis.At the same time,the differential transcription of the downstream genes affected by PP2Aca overexpression was also examined through cDNA microarray analysis by our collaborators. Although the differential expression patterns of the downstream genes display some inconsistency between the mRNA and protein levels,it is easy to detect the changes in the expression patterns of the downstream genes between vector and PP2Aac-transfected JB6 cells.Our results demonstrate that the proteins involved in oxidative stress,protein metablism,membrane transport,carbohydrate and energy metabolism, protein folding,transcriptional regulation,cell signaling and cytoskeleton dynamics and some other minor aspects are differentially expressed. The anti-oxidative stress system components including catalase,aldehyde dehydrogenase,retinal dehydrogenase-1,glutathione S-transferase Mu1 and Mu2,thioredoxin 2,4 & 6 are all downregulated in pCI-PP2Aca-JB6 cells compared with the control cells(pCI-Neo-JB6).The downregulation of the above proteins and enzymes likely leads to an attenuated defense against toxic active substance such as active O,N,and aldehyde but enhanced cell transformation through some unknown mechanism.In contrast,factors involved in protein folding such as splicing isoform 1 of small glutamine-rich tetratricopeptide repeat-containing protein A,calreticulin precursor,protein disulfide-isomerase precursor and tetratricopeptide repeat protein are upregulated,which explain the enhanced chaperone activities necessary for cell transformation in pCI-PP2Aca-JB6 cells.The downregulation of the tumor suppression factors including both prohibitin and annexin Al in pCI-PP2Aca-JB6 cells also supports the tumorigenesity function of PP-2Aac.Together,these results suggest that the pCI-PP2Aca-JB6 cells display some characteristics of transformed cancer cells.
Through the manipulations of the intracellular levels of PP-2Aac by okadaic acid treatment and overexpression of the exogenous PP-2Aac,we have demonstrated that PP-2A directly regulates p53 activity through its dephosphorylation at Ser-15.Furthermore,we demonstrate that through negative regulation of p53,which directly controls the expression of the Cathepsin gene promoter,Ctsb,PP-2A positively regulates Cathepsin B level to promote cell transformation.This conclusion is also confirmed in lung cancer cell,1299 line.
In summary,our results reveal that stable overexpression of PP-2Aca causes significant changes in the protein expression patterns of the JB6 cells,which favor the promotion of cell transformation.Our results also suggest that PP-2A may promote cell transformation via regulation of the n53-cathensin B nathway.
有关B亚基对细胞转化的研究有较多的报道,最近实验也证明A亚基与肿瘤的生成有直接的关系,为PP2A作为肿瘤抑制因子提供了确凿的证据。但是关于C亚基与癌症发生之间关系的报道则很少。
为了研究PP-2A催化亚基在癌症中的可能作用,我们研究小组在前期的工作中建立了PP-2A催化亚基C过表达的两种癌细胞的稳定克隆,即小鼠上皮细胞JB6(pCI-PP2Aca-JB6)和人的肺癌细胞H1299(pCI-PP2Aca-H1299)。利用这两种稳定的细胞系以及转染了载体的稳定细胞系(pCI-Neo-JB6;pCI-Neo-H1299),我们通过蛋白质组学技术、基因芯片技术及其它分子生物学技术对过表达外源性PP-2Aca可能对细胞产生的影响进行了研究。
本论文通过基于胶的双向电泳/质谱偶联蛋白质组学研究技术及基于稳定同位素标记与质谱偶联蛋白质组学定量技术对pCI-PP2Aca-JB6细胞和pCI-neo-JB6细胞在蛋白质组水平的差异表达进行了分析。另外本课题组其他研究人员采用基因芯片技术获得pCI-PP2Aca-JB6细胞在mRNA水平的差异表达数据。这些数据显示虽然下游基因在蛋白水平及mRNA水平的表达存在一些不一致的地方,但是我们发现无论是通过基因芯片所得到的pCI-PP2Aca-JB6细胞与pCI-neo-JB6细胞在mRNA水平的差异表达数据还是通过蛋白质组技术得到的蛋白质水平的差异表达数据都表明pCI-PP2Aca过表达引起了下游基因表达的显著变化。我们发现,与对照相比,pCI-PP2Aca-JB6细胞中包括氧化应激、蛋白质代谢及转运、碳水化合物及能量代谢、蛋白质折叠、转录调控、信号转导、细胞骨架等多条信号通路的发生了变化。结果显示,过氧化氢酶、过氧化物酶、醛脱氢酶、视黄醛脱氢酶、硫氧还蛋白、硫氧还蛋白2、硫氧还蛋白4、硫氧还蛋白6及谷胱甘肽S-转移酶等这些在细胞中清除细胞产生的活性氧、活性氮以及一些醛类活性中间产物等有害物质的酶类和蛋白明显出现了下调,从而通过一些未知机制增强了细胞的转化。相应地,与蛋白质折叠相关的一些蛋白如splicing isoform 1 of smallglutamine-rich tetratricopeptide repeat-containing protein A,calreticulinprecursor,protein disulfide-isomerase precursor和tetratricopeptiderepeat protein表达上调,这表明分子伴侣的活性增强是pCI-PP2Aca-JB6细胞转化所必须的。而Prohibitin(phb)和annexin Al这些种肿瘤抑制因子的表达下调也支持PP2Aca的肿瘤生成功能。总之,这些结果提示我们pCI-PP2Aca-JB6细胞显示出一些转化的癌细胞的特征。
本实验通过过表达PP-2Aca及用OA抑制PP2A的活性的实验证明,PP-2A通过直接对P-p53-ser-15的磷酸化状态的调控来调节p53的活性。另外,我们的实验显示,通过负调控直接控制Cathepsin基因Ctsb的启动子p53,PP-2A正调控Cathepsin B的表达水平从而促进了细胞的转化。这个结论在H1299细胞中也得到证实。
综上所述,我们的实验结果显示,PP-2Aca的稳定过表达引起了JB6细胞蛋白质表达方式的显著变化,从而促进了细胞转化。同时结果也显示PP-2A可能是通过调节p53-cathepsin B信号通路促进了细胞的转化。
Protein phosphatase 2A(PP-2A) is one of the most abundant and conserved serine/threonine phosphatase hin eukaryotes.It dephosphorylates a panel of cellular proteins such as kinases and other signal molecules,and participates in many cellular processes including cell division,cell apoptosis,gene regulation,protein synthesis, cytoskeleton organization and so on.The PP-2A holoenzyme exists as a heterotrimer,consisting of a catalytic C subunit,a structural A subunit and a regulatory B subunit.
Previous studies have shown that the regulatory B subunit of PP-2A plays a crucial role in cell transformation.In addition,recent studies have also demonstrated that the structural A subunit of PP-2A is also implicated in carcinogenesis.Whether the catalytic C subunits of this phosphatase play a role in cancer remains to be explored.
To explore the possible function of the catalytic subunit of PP-2A in cancer,our group has previously established the stable clones overexpressing the catalytic C subunit of PP-2A in both mouse skin cancer,JB6 cells(pCI-PP2Aca-JB6) and human lung cancer,H1299 cells (pCI-PP2Aca-H1299).Using these stable cell lines and also vector-transfected control cell lines(pCI-Neo-JB6;pCI-Neo-H1299),we have investigated the possible effects of the overexpressed exogenous PP-2Aca in these cells using proteomics,cDNA microarray and other molecular biology techniques.
The differential expression patterns of total proteins between pCI-Neo-JB6 and pCI-PP2Aca-JB6 were analyzed using proteomics which was based on 2-D gel separation coupled with mass spectrum analysis or the samples labeled by ~(18)O coupled with mass spectrum analysis.At the same time,the differential transcription of the downstream genes affected by PP2Aca overexpression was also examined through cDNA microarray analysis by our collaborators. Although the differential expression patterns of the downstream genes display some inconsistency between the mRNA and protein levels,it is easy to detect the changes in the expression patterns of the downstream genes between vector and PP2Aac-transfected JB6 cells.Our results demonstrate that the proteins involved in oxidative stress,protein metablism,membrane transport,carbohydrate and energy metabolism, protein folding,transcriptional regulation,cell signaling and cytoskeleton dynamics and some other minor aspects are differentially expressed. The anti-oxidative stress system components including catalase,aldehyde dehydrogenase,retinal dehydrogenase-1,glutathione S-transferase Mu1 and Mu2,thioredoxin 2,4 & 6 are all downregulated in pCI-PP2Aca-JB6 cells compared with the control cells(pCI-Neo-JB6).The downregulation of the above proteins and enzymes likely leads to an attenuated defense against toxic active substance such as active O,N,and aldehyde but enhanced cell transformation through some unknown mechanism.In contrast,factors involved in protein folding such as splicing isoform 1 of small glutamine-rich tetratricopeptide repeat-containing protein A,calreticulin precursor,protein disulfide-isomerase precursor and tetratricopeptide repeat protein are upregulated,which explain the enhanced chaperone activities necessary for cell transformation in pCI-PP2Aca-JB6 cells.The downregulation of the tumor suppression factors including both prohibitin and annexin Al in pCI-PP2Aca-JB6 cells also supports the tumorigenesity function of PP-2Aac.Together,these results suggest that the pCI-PP2Aca-JB6 cells display some characteristics of transformed cancer cells.
Through the manipulations of the intracellular levels of PP-2Aac by okadaic acid treatment and overexpression of the exogenous PP-2Aac,we have demonstrated that PP-2A directly regulates p53 activity through its dephosphorylation at Ser-15.Furthermore,we demonstrate that through negative regulation of p53,which directly controls the expression of the Cathepsin gene promoter,Ctsb,PP-2A positively regulates Cathepsin B level to promote cell transformation.This conclusion is also confirmed in lung cancer cell,1299 line.
In summary,our results reveal that stable overexpression of PP-2Aca causes significant changes in the protein expression patterns of the JB6 cells,which favor the promotion of cell transformation.Our results also suggest that PP-2A may promote cell transformation via regulation of the n53-cathensin B nathway.
引文
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