Proteomics

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


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.

INSTRUMENT(S): maXis II, impact II, solariX

ORGANISM(S): Sus Scrofa (ncbitaxon:9823) Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090)

SUBMITTER: Ying Ge  

PROVIDER: MSV000096622 | MassIVE | Mon Dec 09 11:58:00 GMT 2024

SECONDARY ACCESSION(S): PXD058703

REPOSITORIES: MassIVE

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