ArticleMolecular nutrition & food research2011
Mass spectrometry-based quantification of myocardial protein adducts with acrolein in an in vivo model of oxidative stress.
Article in Molecular nutrition & food research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Mitochondrial vulnerability to aldehydic load and the role mitochondrial aldehyde dehydrogenases.Pharmacological research · 2026Review
- A Workflow towards the Reproducible Identification and Quantitation of Protein Carbonylation Sites in Human Plasma.Antioxidants (Basel, Switzerland) · 2021Article
- Complex Coronary Instent Chronic Total Occlusion Lesions: Oxidative Stress, Inflammation, and Coronary Stent Lengths.Oxidative medicine and cellular longevity · 2021Article
- Lipoxidation in cardiovascular diseases.Redox biology · 2019Review
- Cross-talk between lipid and protein carbonylation in a dynamic cardiomyocyte model of mild nitroxidative stress.Redox biology · 2017Article
- Mechanisms Underlying Acrolein-Mediated Inhibition of Chromatin Assembly.Molecular and cellular biology · 2016Article
- Label-Free Proteomics Assisted by Affinity Enrichment for Elucidating the Chemical Reactivity of the Liver Mitochondrial Proteome toward Adduction by the Lipid Electrophile 4-hydroxy-2-nonenal (HNE).Frontiers in chemistry · 2016Article
- Acrolein Exposure in U.S. Tobacco Smokers and Non-Tobacco Users: NHANES 2005-2006.Environmental health perspectives · 2015Article
- Translesion synthesis past acrolein-derived DNA adducts by human mitochondrial DNA polymerase γ.The Journal of biological chemistry · 2013Article
- Protein modifications by electrophilic lipoxidation products: adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification.Mass spectrometry reviewsReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Acrolein (ACR) exposure leads to the formation of protein-ACR adducts. Protein modification by ACR has been associated with various chronic diseases including cardiovascular and neurodegenerative diseases. Here, we report an analytical strategy that enables the quantification of Michael-type protein adducts of ACR in mitochondrial proteome samples using liquid chromatography in combination with tandem mass spectrometry and selected ion monitoring (LC-MS/MS SRM) analysis. Our approach combines site-specific identification and relative quantification at the peptide level of protein-ACR adducts in relation to the unmodified protein thiol pool. Treatment of 3-month-old rats with CCl(4) , an established in vivo model of acute oxidative stress, resulted in significant increases in the ratios of distinct ACR-adducted peptides to the corresponding unmodified thiol-peptides obtained from proteins that were isolated from cardiac mitochondria. The mitochondrial proteins that were found adducted by ACR were malate dehydrogenase, NADH dehydrogenase [ubiquinone] flavoprotein 1, cytochrome c oxidase subunit VIb isoform 1, ATP synthase d chain, and ADP/ATP translocase 1. The findings indicate that protein modification by ACR has potential value as an index of mitochondrial oxidative stress.
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Registered trials
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