LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice
ObjectiveTo investigate dynamic changes in myocardial protein phosphorylation during the acute phase of myocardial infarction (MI) in mice. MethodsSix 8-week-old C57BL/6J mice were randomly assigned to MI model (n＝3) or sham-operated control (n＝3) groups. Cardiac tissues were harvested 72 hours post...
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| Format: | Article |
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Shanghai Chinese Clinical Medicine Press Co., Ltd.
2025-06-01
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| Series: | Zhongguo Linchuang Yixue |
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| Online Access: | https://www.c-jcm.com/article/doi/10.12025/j.issn.1008-6358.2025.20250210 |
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| author | Yang GAO Jian ZHANG Shiyu HU Jingpu WANG Yiwen WANG Jiatian CAO Feng ZHANG |
| author_facet | Yang GAO Jian ZHANG Shiyu HU Jingpu WANG Yiwen WANG Jiatian CAO Feng ZHANG |
| author_sort | Yang GAO |
| collection | DOAJ |
| description | ObjectiveTo investigate dynamic changes in myocardial protein phosphorylation during the acute phase of myocardial infarction (MI) in mice. MethodsSix 8-week-old C57BL/6J mice were randomly assigned to MI model (n＝3) or sham-operated control (n＝3) groups. Cardiac tissues were harvested 72 hours post-intervention for proteomic analysis. Phosphorylation modifications were systematically characterized using liquid chromatography-mass spectrometry (LC-MS). Bioinformatics analyses included differential phosphorylation screening, functional enrichment, hierarchical clustering, and protein-protein interaction network. ResultsLC-MS identified 1 921 differentially phosphorylated sites (20 tyrosine and 1 901 serine/threonine sites) across 851 proteins. Compared with controls, MI hearts exhibited significant phosphorylation upregulation at 1 545 sites and downregulation at 376 sites (P＜0.05). ConclusionsThis study delineates MI-associated phosphorylation dynamics, providing mechanistic insights and potential therapeutic targets for acute MI intervention. |
| format | Article |
| id | doaj-art-670130f8ed3f4a079a476b4958e795b7 |
| institution | OA Journals |
| issn | 1008-6358 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Shanghai Chinese Clinical Medicine Press Co., Ltd. |
| record_format | Article |
| series | Zhongguo Linchuang Yixue |
| spelling | doaj-art-670130f8ed3f4a079a476b4958e795b72025-08-20T02:36:15ZengShanghai Chinese Clinical Medicine Press Co., Ltd.Zhongguo Linchuang Yixue1008-63582025-06-0132339240210.12025/j.issn.1008-6358.2025.2025021020250210LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in miceYang GAO0Jian ZHANG1Shiyu HU2Jingpu WANG3Yiwen WANG4Jiatian CAO5Feng ZHANG6Department of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaDepartment of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, ChinaObjectiveTo investigate dynamic changes in myocardial protein phosphorylation during the acute phase of myocardial infarction (MI) in mice. MethodsSix 8-week-old C57BL/6J mice were randomly assigned to MI model (n＝3) or sham-operated control (n＝3) groups. Cardiac tissues were harvested 72 hours post-intervention for proteomic analysis. Phosphorylation modifications were systematically characterized using liquid chromatography-mass spectrometry (LC-MS). Bioinformatics analyses included differential phosphorylation screening, functional enrichment, hierarchical clustering, and protein-protein interaction network. ResultsLC-MS identified 1 921 differentially phosphorylated sites (20 tyrosine and 1 901 serine/threonine sites) across 851 proteins. Compared with controls, MI hearts exhibited significant phosphorylation upregulation at 1 545 sites and downregulation at 376 sites (P＜0.05). ConclusionsThis study delineates MI-associated phosphorylation dynamics, providing mechanistic insights and potential therapeutic targets for acute MI intervention.https://www.c-jcm.com/article/doi/10.12025/j.issn.1008-6358.2025.20250210myocardial infarctionphosphorylationliquid chromatography-mass spectrometryproteomics |
| spellingShingle | Yang GAO Jian ZHANG Shiyu HU Jingpu WANG Yiwen WANG Jiatian CAO Feng ZHANG LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice Zhongguo Linchuang Yixue myocardial infarction phosphorylation liquid chromatography-mass spectrometry proteomics |
| title | LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| title_full | LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| title_fullStr | LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| title_full_unstemmed | LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| title_short | LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| title_sort | lc ms based phosphoproteomic profiling of the acute phase of myocardial infarction in mice |
| topic | myocardial infarction phosphorylation liquid chromatography-mass spectrometry proteomics |
| url | https://www.c-jcm.com/article/doi/10.12025/j.issn.1008-6358.2025.20250210 |
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