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Truncation of the N-terminus of cardiac troponin I initiates adaptive remodeling of the myocardial proteosome via phosphorylation of mechano-sensitive signaling pathways

ABSTRACT: We employed isobaric labeled peptides to do bottom-up proteomics to quantify both non-enriched total peptides and enriched phospho-peptides obtained from hearts of control mice expressing wild-type cardiac troponin I and transgenic mice expressing the truncated N-terminal cardiac troponin I.

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: R. John Solaro

PROVIDER: MSV000087049 | MassIVE | Mon Mar 15 09:52:00 GMT 2021

REPOSITORIES: MassIVE

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Truncation of the N-terminus of cardiac troponin I initiates adaptive remodeling of the myocardial proteosome via phosphorylation of mechano-sensitive signaling pathways.

Warren Chad M CM Halas Monika M Goldspink Paul H PH Feng Han-Zhong HZ Herren Anthony W AW Wolska Beata M BM de Tombe Pieter P PP Jin Jian-Ping JP Solaro R John RJ

Molecular and cellular biochemistry 20220322 6

The cardiac isoform of troponin I has a unique N-terminal extension (~ 1-30 amino acids), which contributes to the modulation of cardiac contraction and relaxation. Hearts of various species including humans produce a truncated variant of cardiac troponin I (cTnI-ND) deleting the first ~ 30 amino acids as an adaption in pathophysiological conditions. In this study, we investigated the impact of cTnI-ND chronic expression in transgenic mouse hearts compared to wildtype (WT) controls (biological n ...[more]

PMID: 35316461

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