Emily A. Chapman , Holden T. Rogers , Zhan Gao , Hsin-Ju Chan , Francisco J. Alvarado , Ying Ge
{"title":"In-depth characterization of S-glutathionylation in ventricular myosin light chain 1 across species by top-down proteomics","authors":"Emily A. Chapman , Holden T. Rogers , Zhan Gao , Hsin-Ju Chan , Francisco J. Alvarado , Ying Ge","doi":"10.1016/j.yjmcc.2025.03.012","DOIUrl":null,"url":null,"abstract":"<div><div>S-glutathionylation (SSG) is increasingly recognized as a critical signaling mechanism in the heart, yet SSG modifications in cardiac sarcomeric proteins remain understudied. Here we identified SSG of the ventricular isoform of myosin light chain 1 (MLC-1v) in human, swine, and mouse cardiac tissues using top-down mass spectrometry (MS)-based proteomics. Our results enabled the accurate identification, quantification, and site-specific localization of SSG in MLC-1v across different species. Notably, the endogenous SSG of MLC-1v was observed in human and swine cardiac tissues but not in mice. Treating non-reduced cardiac tissue lysates with GSSG elevated MLC-1v SSG levels across all three species.</div></div>","PeriodicalId":16402,"journal":{"name":"Journal of molecular and cellular cardiology","volume":"203 ","pages":"Pages 1-6"},"PeriodicalIF":4.7000,"publicationDate":"2025-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of molecular and cellular cardiology","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0022282825000586","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CARDIAC & CARDIOVASCULAR SYSTEMS","Score":null,"Total":0}
引用次数: 0
Abstract
S-glutathionylation (SSG) is increasingly recognized as a critical signaling mechanism in the heart, yet SSG modifications in cardiac sarcomeric proteins remain understudied. Here we identified SSG of the ventricular isoform of myosin light chain 1 (MLC-1v) in human, swine, and mouse cardiac tissues using top-down mass spectrometry (MS)-based proteomics. Our results enabled the accurate identification, quantification, and site-specific localization of SSG in MLC-1v across different species. Notably, the endogenous SSG of MLC-1v was observed in human and swine cardiac tissues but not in mice. Treating non-reduced cardiac tissue lysates with GSSG elevated MLC-1v SSG levels across all three species.
s -谷胱甘肽酰化（SSG）越来越被认为是心脏的一个关键信号机制，但SSG在心肌蛋白中的修饰仍未得到充分研究。在这里，我们使用基于自上而下质谱（MS）的蛋白质组学方法在人、猪和小鼠心脏组织中鉴定了肌球蛋白轻链1 （MLC-1v）心室异构体的SSG。我们的研究结果使不同物种的MLC-1v中SSG的准确鉴定、定量和位点特异性定位成为可能。值得注意的是，在人和猪心脏组织中观察到内源性MLC-1v的SSG，而在小鼠中没有。用GSSG处理未还原的心脏组织裂解物可提高所有三个物种的MLC-1v SSG水平。
期刊介绍：
The Journal of Molecular and Cellular Cardiology publishes work advancing knowledge of the mechanisms responsible for both normal and diseased cardiovascular function. To this end papers are published in all relevant areas. These include (but are not limited to): structural biology; genetics; proteomics; morphology; stem cells; molecular biology; metabolism; biophysics; bioengineering; computational modeling and systems analysis; electrophysiology; pharmacology and physiology. Papers are encouraged with both basic and translational approaches. The journal is directed not only to basic scientists but also to clinical cardiologists who wish to follow the rapidly advancing frontiers of basic knowledge of the heart and circulation.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
