LC-MS-based phosphoproteomic profiling of the acute phase of myocardial infarction in mice
10.12025/j.issn.1008-6358.2025.20250210
- VernacularTitle:基于液相色谱-质谱的心肌梗死急性期小鼠磷酸化修饰蛋白质组学分析
- Author:
Yang GAO
1
;
Jian ZHANG
1
;
Shiyu HU
1
;
Jingpu WANG
1
;
Yiwen WANG
1
;
Jiatian CAO
1
;
Feng ZHANG
1
Author Information
1. Department of Cardiology, Zhongshan Hospital, Fudan University, Shanghai Institute of Cardiovascular Disease, Shanghai 200032, China.
- Publication Type:Originalarticle
- Keywords:
myocardial infarction;
phosphorylation;
liquid chromatography-mass spectrometry;
proteomics
- From:
Chinese Journal of Clinical Medicine
2025;32(3):392-402
- CountryChina
- Language:Chinese
-
Abstract:
Objective To investigate dynamic changes in myocardial protein phosphorylation during the acute phase of myocardial infarction (MI) in mice. Methods Six 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. Results LC-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). Conclusions This study delineates MI-associated phosphorylation dynamics, providing mechanistic insights and potential therapeutic targets for acute MI intervention.