{"title":"探索环孢素治疗再生障碍性贫血的机制：数据独立获取蛋白质组学方法","authors":"Mingxin Guo, Ting Dai, Lin Wan, Xiang Sun, Zhiqiang Hu, Yanchun Chen","doi":"10.1002/rcm.10085","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> Rationale</h3>\n \n <p>Clinically, cyclosporine (CsA) plays a crucial role in the treatment of aplastic anemia (AA) and has demonstrated significant therapeutic efficacy. We applied DIA-based quantitative proteomics to analyze plasma protein profiles in AA patients, aiming to identify proteins and pathways modulated by CsA, thereby elucidating its therapeutic mechanisms.</p>\n </section>\n \n <section>\n \n <h3> Methods</h3>\n \n <p>Plasma samples from three AA patients pre– and post–CsA treatment underwent data-independent acquisition proteomics. DEPs were identified using fold-change thresholds. Gene Ontology, KEGG, and STRING analyses revealed functional pathways and hub proteins, which were validated by ELISA in 13 AA patients. Molecular docking assessed CsA-core protein binding affinities.</p>\n </section>\n \n <section>\n \n <h3> Results</h3>\n \n <p>Compared to healthy people, AA patients exhibited 303 differential proteins, enriched in pathways related to oxidative stress, cellular adhesion, and energy dysregulation. Post–CsA treatment, 107 DEPs were identified, linked to redox balance and structural remodeling. Forty-eight proteins overlapped, with GAPDH, SOD1, CFL1, and ACTG1 as core targets. ELISA confirmed expression differences, and molecular docking showed strong CsA binding affinities to these proteins.</p>\n </section>\n \n <section>\n \n <h3> Conclusions</h3>\n \n <p>Significant protein expression differences between AA patients and healthy controls suggest immune-related pathways, including metabolism, oxidative stress, and cell structure, as key treatment targets. CsA may regulate these to intervene in AA progression.</p>\n </section>\n </div>","PeriodicalId":225,"journal":{"name":"Rapid Communications in Mass Spectrometry","volume":"39 17","pages":""},"PeriodicalIF":1.8000,"publicationDate":"2025-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring the Mechanisms of Cyclosporine Therapy in Aplastic Anemia: A Data-Independent Acquisition Proteomics Approach\",\"authors\":\"Mingxin Guo, Ting Dai, Lin Wan, Xiang Sun, Zhiqiang Hu, Yanchun Chen\",\"doi\":\"10.1002/rcm.10085\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n \\n <section>\\n \\n <h3> Rationale</h3>\\n \\n <p>Clinically, cyclosporine (CsA) plays a crucial role in the treatment of aplastic anemia (AA) and has demonstrated significant therapeutic efficacy. We applied DIA-based quantitative proteomics to analyze plasma protein profiles in AA patients, aiming to identify proteins and pathways modulated by CsA, thereby elucidating its therapeutic mechanisms.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Methods</h3>\\n \\n <p>Plasma samples from three AA patients pre– and post–CsA treatment underwent data-independent acquisition proteomics. DEPs were identified using fold-change thresholds. Gene Ontology, KEGG, and STRING analyses revealed functional pathways and hub proteins, which were validated by ELISA in 13 AA patients. Molecular docking assessed CsA-core protein binding affinities.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Results</h3>\\n \\n <p>Compared to healthy people, AA patients exhibited 303 differential proteins, enriched in pathways related to oxidative stress, cellular adhesion, and energy dysregulation. Post–CsA treatment, 107 DEPs were identified, linked to redox balance and structural remodeling. Forty-eight proteins overlapped, with GAPDH, SOD1, CFL1, and ACTG1 as core targets. ELISA confirmed expression differences, and molecular docking showed strong CsA binding affinities to these proteins.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Conclusions</h3>\\n \\n <p>Significant protein expression differences between AA patients and healthy controls suggest immune-related pathways, including metabolism, oxidative stress, and cell structure, as key treatment targets. CsA may regulate these to intervene in AA progression.</p>\\n </section>\\n </div>\",\"PeriodicalId\":225,\"journal\":{\"name\":\"Rapid Communications in Mass Spectrometry\",\"volume\":\"39 17\",\"pages\":\"\"},\"PeriodicalIF\":1.8000,\"publicationDate\":\"2025-05-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Rapid Communications in Mass Spectrometry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/rcm.10085\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Rapid Communications in Mass Spectrometry","FirstCategoryId":"92","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/rcm.10085","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
Exploring the Mechanisms of Cyclosporine Therapy in Aplastic Anemia: A Data-Independent Acquisition Proteomics Approach
Rationale
Clinically, cyclosporine (CsA) plays a crucial role in the treatment of aplastic anemia (AA) and has demonstrated significant therapeutic efficacy. We applied DIA-based quantitative proteomics to analyze plasma protein profiles in AA patients, aiming to identify proteins and pathways modulated by CsA, thereby elucidating its therapeutic mechanisms.
Methods
Plasma samples from three AA patients pre– and post–CsA treatment underwent data-independent acquisition proteomics. DEPs were identified using fold-change thresholds. Gene Ontology, KEGG, and STRING analyses revealed functional pathways and hub proteins, which were validated by ELISA in 13 AA patients. Molecular docking assessed CsA-core protein binding affinities.
Results
Compared to healthy people, AA patients exhibited 303 differential proteins, enriched in pathways related to oxidative stress, cellular adhesion, and energy dysregulation. Post–CsA treatment, 107 DEPs were identified, linked to redox balance and structural remodeling. Forty-eight proteins overlapped, with GAPDH, SOD1, CFL1, and ACTG1 as core targets. ELISA confirmed expression differences, and molecular docking showed strong CsA binding affinities to these proteins.
Conclusions
Significant protein expression differences between AA patients and healthy controls suggest immune-related pathways, including metabolism, oxidative stress, and cell structure, as key treatment targets. CsA may regulate these to intervene in AA progression.
期刊介绍：
Rapid Communications in Mass Spectrometry is a journal whose aim is the rapid publication of original research results and ideas on all aspects of the science of gas-phase ions; it covers all the associated scientific disciplines. There is no formal limit on paper length ("rapid" is not synonymous with "brief"), but papers should be of a length that is commensurate with the importance and complexity of the results being reported. Contributions may be theoretical or practical in nature; they may deal with methods, techniques and applications, or with the interpretation of results; they may cover any area in science that depends directly on measurements made upon gaseous ions or that is associated with such measurements.
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