ArticleMolecular and cellular biochemistry1988
Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants.
Article in Molecular and cellular biochemistry, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 59 citations in OpenAlex.
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- Ordered cleavage of myeloperoxidase ester bonds releases active site heme leading to inactivation of myeloperoxidase by benzoic acid hydrazide analogs.Archives of biochemistry and biophysics · 2014Article
- Mechanisms of neuroprotection by hemopexin: modeling the control of heme and iron homeostasis in brain neurons in inflammatory states.Journal of neurochemistry · 2013Article
- Breathtaking TRP channels: TRPA1 and TRPV1 in airway chemosensation and reflex control.Physiology (Bethesda, Md.) · 2008Review
- Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Effect of arachidonic and eicosapentaenoic acids on acute lung injury induced by hypochlorous acid.Thorax · 2002Article
- Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation.The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability of the polymorphonuclear leukocyte (PMN) oxidants, hypochlorous acid (HOC1) and hydrogen peroxide (H2O2), to oxidize proteins in rat heart and lung tissues was investigated. Cardiac myocytes, heart tissue slices, isolated perfused hearts, and lung tissue slices, were treated with HOC1 and H2O2 and the extent of methionine and cysteine oxidation was determined in the cellular proteins. Cardiac tissues were found to be highly susceptible to oxidation by physiological concentrations of HOC1. For example, in isolated hearts perfused for 60 min with 100 microM HOC1, approximately 18% of the methionine and 28% of the cysteine residues were oxidized. Lung tissues, unlike those of the heart, were resistant to physiological concentrations of HOC1, showing no oxidation of proteins. HOC1 was much more effective than H2O2 in oxidizing proteins, suggesting that HOC1 may be the most reactive oxidant produced by activated PMN. These studies show that PMN oxidants, in particular HOC1, can cause significant oxidation of proteins in target tissues, and may therefore constitute a primary cause of tissue injury at sites of inflammation. In addition, these studies show that different tissues may have varying susceptibilities to PMN oxidants.
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