Tomin, Tamara

Hofreither, Dominik

Jahnel, Stefan

Brandl, Katharina

Sedej, Simon

Mendjan, Sasha

Sattler, Susanne

Schittmayer-Schantl, Matthias

Birner-Grünberger, Ruth

2025-09-15T10:35:28Z

2025-09-15T10:35:28Z

2025-05-11

<div class="csl-bib-body"> <div class="csl-entry">Tomin, T., Hofreither, D., Jahnel, S., Brandl, K., Sedej, S., Mendjan, S., Sattler, S., Schittmayer-Schantl, M., &#38; Birner-Grünberger, R. (2025, May 11). <i>Alterations of Redox Proteome and Thiol Metabolome in Acute Oxidative Injury</i> [Poster Presentation]. ISHR 2025, Nara, Japan.</div> </div>

http://hdl.handle.net/20.500.12708/219094

https://www.ishr2025nara.jp/

Introduction Oxidative stress contributes to the functional decline of the myocardium and is correlated with unfavourable metabolic perturbations, including the switch from oxidative metabolism to glycolysis, branched chain amino acids and ketone bodies for energy production. Oxidative post-translational modifications (oxPTMs) might play a significant role in this process as they can influence both structure as well as the function of proteins. Methods We already demonstrated that end-stage failing human hearts endure higher levels of oxidative stress and exhibit higher oxidation of several different enzymes, namely related to glucose metabolism. We next aimed to unravel which oxidative changes might be connected with the early onset of oxidative damage. To that end, we simulated reperfusion injury (I/R) using cultured stem-cell derived and metabolically matured cardioids, followed by “one-pot” redox proteomics and small thiol analysis. The findings from cardioids were further corroborated in mouse model of myocardial infarction (MI), where the samples were carefully collected either thirty minutes or a week after the procedure from MI affected area (MI) of the left ventricle (LV); or remote, non-infarcted area of the same LV (R) or sham control (N=5 per condition/group). Results As a result, we report protein targets of acute oxidative damage - overlap of significantly redox affected cysteine residues between MI vs. R, MI vs. Sham and I/R vs. Control cardioids - many of which metabolic enzymes (Figure 1). In addition, we describe early perturbations of (metabolic) proteome in the infarcted area compared to its surroundings (and/or sham control), including downregulation of (oxidative) metabolic enzymes, and the rise of, among others, branched chain amino acid transaminase (Bcat1) as well as lysosomal acid lipase (Lipa). Lastly, we provide a unique insight into glutathione metabolism (including its precursors and intermediates) of both cardioids upon simulated I/R injury as well as LV tissue affected by MI, experimentally demonstrating the attempts of oxidation affected cardiomyocytes and the cardiac tissue to restore its glutathione supply. Conclusion Collectively our data provides novel insight into cardiac injury and suggest a potential direct cross-talk between redox signaling and metabolism upon oxidative stress exposure.

FWF - Österr. Wissenschaftsfonds

en

redox-proteomics

thiol metabolome

acute oxidative injury

heart

Alterations of Redox Proteome and Thiol Metabolome in Acute Oxidative Injury

Presentation

Vortrag

Medical University of Graz, Austria

University of Maribor, Slovenia

Institute of Molecular Biotechnology, Austria

Imperial College London, United Kingdom of Great Britain and Northern Ireland (the)

F 7309-B21

Poster Presentation

Lipidhydrolyse im Krebs und in Lipid-assoziierten Krankheiten

Cell Culture Core Facility (CCCF)

X1

Beyond TUW-research focus

100

E164-01-3 - Forschungsgruppe Bioanalytik

E056-12 - Fachbereich ENROL DP

0000-0002-7071-2316

0000-0003-1147-9179

0000-0002-4419-6821

0000-0001-7539-3951

0000-0001-9932-4109

0000-0003-3249-655X

0000-0003-3950-0312

ISHR 2025

11-05-2025

14-05-2025

On Site

Event for scientific audience

Nara

JP

International society for Heart Research

Tomin, Tamara

Chemie

Biologie

Anatomie, Pathologie, Physiologie

1040

1060

3011

50

25

25

en

conference poster not in proceedings

http://purl.org/coar/resource_type/c_18co

none

Publications

no Fulltext

E164-01-3 - Forschungsgruppe Bioanalytik

E164-01-3 - Forschungsgruppe Bioanalytik

Medical University of Graz, Austria

University of Maribor, Slovenia

Institute of Molecular Biotechnology, Austria

Imperial College London, United Kingdom of Great Britain and Northern Ireland (the)

E164-01-3 - Forschungsgruppe Bioanalytik

E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie

0000-0002-7071-2316

0000-0003-1147-9179

0000-0002-4419-6821

0000-0001-7539-3951

0000-0001-9932-4109

0000-0003-3249-655X

0000-0003-3950-0312

E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie

E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie

E164-01 - Forschungsbereich Imaging und Instrumentelle Analytische Chemie

E164 - Institut für Chemische Technologien und Analytik

FWF - Österr. Wissenschaftsfonds

F 7309-B21