Proteomics

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Identification of enriched O-GlcNAc proteins in hypertrophic mouse hearts

ABSTRACT: We used C57/Bl6 mice subjected to sham or transverse aortic constriction (TAC) to create pressure-overload hypertrophy (POH). From the hearts, we stabilized and labelled the O-GlcNAc moiety with tetramethylrhodamine azide (TAMRA) before enriching by TAMRA immunoprecipitation (files with "TAMRAIP"). Global proteomics were performed on the non-enriched matching samples (files with "GlobalDigest"). Sham sample IDs: 529, 545, 547, 551, 552. TAC sample IDs: 524, 528, 562, 563, 564. O-GlcNAc proteins were labeled with a click chemistry kit with TAMRA tag (ThermoFisher Scientific), then the labeled proteins were enriched with TAMRA antibody for proteomics experiments. Data was searched against the UniProt mouse database using PEAKS Studio for label free quantitation. Protein abundances were log2 transformed, normalized to median, and missing values imputed using Perseus.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Aaron Olson  

PROVIDER: MSV000088797 | MassIVE | Mon Feb 07 20:50:00 GMT 2022

REPOSITORIES: MassIVE

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First comprehensive identification of cardiac proteins with putative increased O-GlcNAc levels during pressure overload hypertrophy.

Zhu Wei Zhong WZ   Palazzo Teresa T   Zhou Mowei M   Ledee Dolena D   Olson Heather M HM   Paša-Tolić Ljiljana L   Olson Aaron K AK  

PloS one 20221026 10

Protein posttranslational modifications (PTMs) by O-GlcNAc globally rise during pressure-overload hypertrophy (POH). However, a major knowledge gap exists on the specific proteins undergoing changes in O-GlcNAc levels during POH primarily because this PTM is low abundance and easily lost during standard mass spectrometry (MS) conditions used for protein identification. Methodologies have emerged to enrich samples for O-GlcNAcylated proteins prior to MS analysis. Accordingly, our goal was to iden  ...[more]

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