MassIVE MSV000096622

Partial Public PXD058703

In-depth Characterization of S-Glutathionylation of Ventricular Myosin Light Chain 1 Across Species by Top-Down Proteomics

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Description

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. [doi:10.25345/C5794162C] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: top-down proteomics ; s-glutathionylation ; sarcomere ; myosin light chain ; PTM ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Ying Ge, University of Wisconsin - Madison, United States of America
Submitting User: eachapman2
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