Xinhang Wang, Shen Tang, Fu Qin, Yuyang Liu, Ziwei Liang, Haiqing Cai, Laiming Mo, Deqiang Xiao, Songcao Guo, Yiqiang Ouyang, Bin Sun, Cailing Lu, Xiyi Li
{"title":"LCMT1过表达与氧化应激的蛋白质组学和磷酸化蛋白质组学研究:LCMT1过表达可阻止h2o2诱导的细胞活力丧失。","authors":"Xinhang Wang, Shen Tang, Fu Qin, Yuyang Liu, Ziwei Liang, Haiqing Cai, Laiming Mo, Deqiang Xiao, Songcao Guo, Yiqiang Ouyang, Bin Sun, Cailing Lu, Xiyi Li","doi":"10.1080/13510002.2019.1595332","DOIUrl":null,"url":null,"abstract":"<p><strong>Objectives: </strong>Protein phosphatase 2A (PP2A), a major serine/threonine phosphatase, is also known to be a target of ROS. The methylation of PP2A can be catalyzed by leucine carboxyl methyltransferase-1 (LCMT1), which regulates PP2A activity and substrate specificity.</p><p><strong>Methods: </strong>In the previous study, we have showed that LCMT1-dependent PP2Ac methylation arrests H<sub>2</sub>O<sub>2</sub>-induced cell oxidative stress damage. To explore the possible protective mechanism, we performed iTRAQ-based comparative quantitative proteomics and phosphoproteomics studies of H<sub>2</sub>O<sub>2</sub>-treated vector control and LCMT1-overexpressing cells.</p><p><strong>Results: </strong>A total of 4480 non-redundant proteins and 3801 unique phosphopeptides were identified by this means. By comparing the H<sub>2</sub>O<sub>2</sub>-regulated proteins in LCMT1-overexpressing and vector control cells, we found that these differences were mainly related to protein phosphorylation, gene expression, protein maturation, the cytoskeleton and cell division. Further investigation of LCMT1 overexpression-specific regulated proteins under H<sub>2</sub>O<sub>2</sub> treatment supported the idea that LCMT1 overexpression induced ageneral dephosphorylation of proteins and indicated increased expression of non-erythrocytic hemoglobin, inactivation of MAPK3 and regulation of proteins related to Rho signal transduction, which were known to be linked to the regulation of the cytoskeleton.</p><p><strong>Discussion: </strong>These data provide proteomics and phosphoproteomics insights into the association of LCMT1-dependent PP2Ac methylation and oxidative stress and indirectly indicate that the methylation of PP2A plays an important role against oxidative stress.</p>","PeriodicalId":21096,"journal":{"name":"Redox Report","volume":"24 1","pages":"1-9"},"PeriodicalIF":5.2000,"publicationDate":"2019-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/13510002.2019.1595332","citationCount":"8","resultStr":"{\"title\":\"Proteomics and phosphoproteomics study of LCMT1 overexpression and oxidative stress: overexpression of LCMT1 arrests H<sub>2</sub>O<sub>2</sub>-induced lose of cells viability.\",\"authors\":\"Xinhang Wang, Shen Tang, Fu Qin, Yuyang Liu, Ziwei Liang, Haiqing Cai, Laiming Mo, Deqiang Xiao, Songcao Guo, Yiqiang Ouyang, Bin Sun, Cailing Lu, Xiyi Li\",\"doi\":\"10.1080/13510002.2019.1595332\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Objectives: </strong>Protein phosphatase 2A (PP2A), a major serine/threonine phosphatase, is also known to be a target of ROS. The methylation of PP2A can be catalyzed by leucine carboxyl methyltransferase-1 (LCMT1), which regulates PP2A activity and substrate specificity.</p><p><strong>Methods: </strong>In the previous study, we have showed that LCMT1-dependent PP2Ac methylation arrests H<sub>2</sub>O<sub>2</sub>-induced cell oxidative stress damage. To explore the possible protective mechanism, we performed iTRAQ-based comparative quantitative proteomics and phosphoproteomics studies of H<sub>2</sub>O<sub>2</sub>-treated vector control and LCMT1-overexpressing cells.</p><p><strong>Results: </strong>A total of 4480 non-redundant proteins and 3801 unique phosphopeptides were identified by this means. By comparing the H<sub>2</sub>O<sub>2</sub>-regulated proteins in LCMT1-overexpressing and vector control cells, we found that these differences were mainly related to protein phosphorylation, gene expression, protein maturation, the cytoskeleton and cell division. Further investigation of LCMT1 overexpression-specific regulated proteins under H<sub>2</sub>O<sub>2</sub> treatment supported the idea that LCMT1 overexpression induced ageneral dephosphorylation of proteins and indicated increased expression of non-erythrocytic hemoglobin, inactivation of MAPK3 and regulation of proteins related to Rho signal transduction, which were known to be linked to the regulation of the cytoskeleton.</p><p><strong>Discussion: </strong>These data provide proteomics and phosphoproteomics insights into the association of LCMT1-dependent PP2Ac methylation and oxidative stress and indirectly indicate that the methylation of PP2A plays an important role against oxidative stress.</p>\",\"PeriodicalId\":21096,\"journal\":{\"name\":\"Redox Report\",\"volume\":\"24 1\",\"pages\":\"1-9\"},\"PeriodicalIF\":5.2000,\"publicationDate\":\"2019-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/13510002.2019.1595332\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Redox Report\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1080/13510002.2019.1595332\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Redox Report","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1080/13510002.2019.1595332","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Proteomics and phosphoproteomics study of LCMT1 overexpression and oxidative stress: overexpression of LCMT1 arrests H2O2-induced lose of cells viability.
Objectives: Protein phosphatase 2A (PP2A), a major serine/threonine phosphatase, is also known to be a target of ROS. The methylation of PP2A can be catalyzed by leucine carboxyl methyltransferase-1 (LCMT1), which regulates PP2A activity and substrate specificity.
Methods: In the previous study, we have showed that LCMT1-dependent PP2Ac methylation arrests H2O2-induced cell oxidative stress damage. To explore the possible protective mechanism, we performed iTRAQ-based comparative quantitative proteomics and phosphoproteomics studies of H2O2-treated vector control and LCMT1-overexpressing cells.
Results: A total of 4480 non-redundant proteins and 3801 unique phosphopeptides were identified by this means. By comparing the H2O2-regulated proteins in LCMT1-overexpressing and vector control cells, we found that these differences were mainly related to protein phosphorylation, gene expression, protein maturation, the cytoskeleton and cell division. Further investigation of LCMT1 overexpression-specific regulated proteins under H2O2 treatment supported the idea that LCMT1 overexpression induced ageneral dephosphorylation of proteins and indicated increased expression of non-erythrocytic hemoglobin, inactivation of MAPK3 and regulation of proteins related to Rho signal transduction, which were known to be linked to the regulation of the cytoskeleton.
Discussion: These data provide proteomics and phosphoproteomics insights into the association of LCMT1-dependent PP2Ac methylation and oxidative stress and indirectly indicate that the methylation of PP2A plays an important role against oxidative stress.
期刊介绍：
Redox Report is a multidisciplinary peer-reviewed open access journal focusing on the role of free radicals, oxidative stress, activated oxygen, perioxidative and redox processes, primarily in the human environment and human pathology. Relevant papers on the animal and plant environment, biology and pathology will also be included.
While emphasis is placed upon methodological and intellectual advances underpinned by new data, the journal offers scope for review, hypotheses, critiques and other forms of discussion.
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