Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging

Kanski, Jaroslaw; Behring, Antje; Pelling, Jill; Schöneich, Christian

doi:10.1152/ajpheart.01030.2003

Cited by 217Redox biology and oxidative stressAdvanced Proteomics Techniques and ApplicationsGenetics, Aging, and Longevity in Model Organisms

Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging

Kanski, Jaroslaw, Behring, Antje, Pelling, Jill, Schöneich, Christian·2005·American Journal of Physiology-Heart and Circulatory Physiology

DOI 10.1152/ajpheart.01030.2003

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Abstract

Proteomic techniques were used to identify cardiac proteins from whole heart homogenate and heart mitochondria of Fisher 344/Brown Norway F1 rats, which suffer protein nitration as a consequence of biological aging. Soluble proteins from young (5 mo old) and old (26 mo old) animals were separated by one- and two-dimensional gel electrophoresis. One- and two-dimensional Western blots with an anti-nitrotyrosine antibody show an age-related increase in the immunoresponse of a few specific proteins, which were identified by nanoelectrospray ionization-tandem mass spectrometry (NSI-MS/MS). Complementary proteins were immunoprecipitated with an immobilized anti-nitrotyrosine antibody followed by NSI-MS/MS analysis. A total of 48 proteins were putatively identified. Among the identified proteins were α-enolase, α-aldolase, desmin, aconitate hydratase, methylmalonate semialdehyde dehydrogenase, 3-ketoacyl-CoA thiolase, acetyl-CoA acetyltransferase, GAPDH, malate dehydrogenase, creatine kinase, electron-transfer flavoprotein, manganese-superoxide dismutase, F1-ATPase, and the voltage-dependent anion channel. Some contaminating blood proteins including transferrin and fibrinogen β-chain precursor showed increased levels of nitration as well. MS/MS analysis located nitration at Y105 of the electron-transfer flavoprotein. Among the identified proteins, there are important enzymes responsible for energy production and metabolism as well as proteins involved in the structural integrity of the cells. Our results are consistent with age-dependent increased oxidative stress and with free radical-dependent damage of proteins. Possibly the oxidative modifications of the identified proteins contribute to the age-dependent degeneration and functional decline of heart proteins.

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Multiple studies have shown that nitration is a selective process.
“Although a growing number of proteins have now been shown to be nitrated, multiple studies have shown that nitration is a selective process (47, 484).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [484]

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Authors: Kanski, J., Behring, A., Pelling, J., & Schöneich, C.
ORCID: Schöneich, Christian
Venue: American Journal of Physiology-Heart and Circulatory Physiology
Publisher: American Physiological Society
Published: 2005-01
Volume: 288
Issue: 1
Pages: H371-H381
ISSN: 0363-6135 (ISSN-L)
1522-1539
DOI: 10.1152/ajpheart.01030.2003
OpenAlex: W2170295209
Cited by: 217
References: 74
Citations by year: 2026: 1 · 2025: 4 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 8 · 2015: 6 · 2014: 10 · 2013: 11 · 2012: 13
FWCI: 7.12
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Heart and Circulatory Physiology (publishedVersion)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health
National Institute on Aging (2P01 AG 12993, AG023551, P01AG012993, R01AG023551)
National Cancer Institute (R01CA072987, CA072987)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: nitrotyrosine, protein nitration, cardiac aging, heart mitochondria, oxidative stress, oxidative damage, electron transfer flavoprotein, alpha-enolase, desmin, creatine kinase, manganese superoxide dismutase, voltage-dependent anion channel, myocardial energy metabolism
MeSH terms: Aging, Animals, Myocardium, Proteins, Rats, Inbred BN, Rats, Inbred F344, Tyrosine, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Spectrometry, Mass, Electrospray Ionization, Nanotechnology, Proteomics, Rats

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Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging

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