Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging
Abstract
Nitration of protein tyrosine residues (nY) is a marker of oxidative stress and may alter the biological activity of the modified proteins. The aim of this study was to develop antibodies toward site-specific nY-modified proteins and to use histochemistry and immunoblotting to demonstrate protein nitration in tissues. Affinity-purified polyclonal antibodies toward peptides with known nY sites in MnSOD nY-34 and of two adjacent nY in the sarcoplasmic endoplasmic reticulum calcium ATPase (SERCA2 di-nY-294,295) were developed. Kidneys from rats infused with ANG II with known MnSOD nY and aorta from atherosclerotic rabbits and aging rat skeletal and cardiac sarcoplasmic reticulum with known SERCA di-nY were used for positive controls. Staining for MnSOD nY-34 was most intense in distal renal tubules and collecting ducts. Staining of atherosclerotic aorta for SERCA2 di-nY was most intense in atherosclerotic plaques. Aging rat skeletal muscle and atherosclerotic aorta and cardiac atrium from human diabetic patients also stained positively. Staining was decreased by sodium dithionite, which chemically reduces nitrotyrosine to aminotyrosine, and the antigenic nY-peptide blocked staining for each respective nY site but not for the other. As previously demonstrated, immunoblotting failed to detect these modified proteins in whole tissue lysates but did when the proteins were concentrated. Immunohistochemical staining for specific nY-modified tyrosine residues offers the ability to assess the effects of oxidant stress associated with pathological conditions on individual proteins whose function may be affected in specific tissue sites.
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The nitroproteome appears to be quite specific.
“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [50]
Pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism.
“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [50]
Peroxynitrite and reactive species derived from it are important in inflammatory responses and can modulate cell signaling, in part by promoting oxidation or nitration of biomolecules.
“Peroxynitrite and reactive species derived from it (e.g., nitrogen dioxide) are important in inflammatory responses [85] and can modulate cell signaling [87-90], in part by promoting the oxidation or nitration of a broad range of biomolecules [62].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [88]
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Self-citation
- Authors
- Xu, S., Ying, J., Jiang, B., Guo, W., Adachi, T., Sharov, V., Lazar, H., Menzoian, J., Knyushko, T. V., Bigelow, D., Schöneich, C., & Cohen, R. A.
- Affiliations
- Boston University (US)
- Venue
- American Journal of Physiology-Heart and Circulatory Physiology
- Publisher
- American Physiological Society
- Published
- 2006-06
- Volume
- 290
- Issue
- 6
- Pages
- H2220-H2227
- ISSN
- 0363-6135 (ISSN-L)
- 1522-1539
- OpenAlex
- W2163726300
- Cited by
- 145
- References
- 12
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 4 · 2019: 3 · 2018: 3 · 2017: 6 · 2016: 5 · 2015: 5 · 2014: 14 · 2013: 5 · 2012: 9
- FWCI
- 9.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Heart and Circulatory Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (n01hv28178-12-0-0)
- National Institute on Aging (2P01 AG 12993, R01 AG 27080-01, R01AG027080, P01AG012993)
- National Heart, Lung, and Blood Institute (R01 HL 31607-21, R01HL055620, N01 HV28178, R01HL031607, R01 HL 55620-08)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- tyrosine nitration, nitrotyrosine, manganese superoxide dismutase, SERCA2, sarcoplasmic reticulum calcium ATPase, site-specific antibodies, oxidative stress, atherosclerosis, aging, diabetic cardiomyopathy, renal tubules, atherosclerotic plaque, dithionite reduction, immunohistochemistry
- MeSH terms
- Calcium-Transporting ATPases, Aging, Animals, Cardiovascular Diseases, Dithionite, Immunohistochemistry, Kidney, Rabbits, Sarcoplasmic Reticulum, Superoxide Dismutase, Tyrosine, Immunoblotting, Oxidative Stress, Peroxynitrous Acid, Sarcoplasmic Reticulum Calcium-Transporting ATPases, In Vitro Techniques
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