ArticleThe Biochemical journal2003
Characterization of non-covalent oligomers of proteins treated with hypochlorous acid.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 89 citations in OpenAlex.
- Hypochlorous Acid and Chloramines Induce Specific Fragmentation and Cross-Linking of the G1-IGD-G2 Domains of Recombinant Human Aggrecan, and Inhibit ADAMTS1 Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Impact of Reactive Species on Amino Acids-Biological Relevance in Proteins and Induced Pathologies.International journal of molecular sciences · 2022Review
- Article
- Surviving Reactive Chlorine Stress: Responses of Gram-Negative Bacteria to Hypochlorous Acid.Microorganisms · 2020Review
- Article
- Article
- Nitration and Glycation Turn Mature NGF into a Toxic Factor for Motor Neurons: A Role for p75Antioxidants & redox signaling · 2018Article
- Elucidating the Inhibitory Potential of Designed Peptides Against Amyloid Fibrillation and Amyloid Associated Cytotoxicity.Frontiers in chemistry · 2018Article
- Recent progress in chromogenic and fluorogenic chemosensors for hypochlorous acid.The Analyst · 2016Review
- Protein quality control under oxidative stress conditions.Journal of molecular biology · 2015Review
- Activation of RidA chaperone function by N-chlorination.Nature communications · 2014Article
- Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Polyphosphate is a primordial chaperone.Molecular cell · 2014Article
- Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway.Free radical biology & medicine · 2013Article
- NemR is a bleach-sensing transcription factor.The Journal of biological chemistry · 2013Article
- The myeloperoxidase product hypochlorous acid generates irreversible high-density lipoprotein receptor inhibitors.Arteriosclerosis, thrombosis, and vascular biology · 2013Article
- Bacterial responses to reactive chlorine species.Annual review of microbiology · 2013Review
- Article
- Neutrophils Turn Plasma Proteins into Weapons against HIV-1.PloS one · 2013Article
- Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.Chemical research in toxicology · 2012Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hypochlorous acid (HOCl) is a potent oxidant produced by myeloperoxidase that causes aggregation of many proteins. Treatment of apohaemoglobin and apomyoglobin with HOCl produced a regular series of oligomer bands when the proteins were separated by SDS/PAGE under reducing conditions. Aggregation was detectable at a HOCl/protein molar ratio of 0.5:1 and was maximal at ratios of 10:1-20:1. Dimers formed within 1 min of adding HOCl, and further aggregation occurred over the next 30 min. No convincing evidence for covalent cross-linking was obtained by amino acid analysis, peptide analysis or electrospray ionization-MS of HOCl-modified apomyoglobin. The latter showed an increase in mass consistent with conversion of the two methionine residues into sulphoxides. A 5-fold excess of HOCl generated approximately three chloramines on the apomyoglobin. These underwent slow decay. Protein carbonyls were formed and were almost entirely located only on the polymer bands. Conversion of positively into negatively charged groups on the protein by succinylation caused preformed aggregates to dissociate. Treatment of apomyoglobin with taurine chloramine generated methionine sulphoxides but few protein carbonyls, and did not result in aggregation. We conclude that aggregation was due to strong, non-covalent interactions between protein chains. We propose that formation of protein carbonyls and possibly chloramines, along with methionine oxidation, alters protein folding to expose hydrophobic areas on neighbouring molecules that associate to form dimers and higher-molecular-mass aggregates. This process could lead to the formation of aggregated proteins at sites of myeloperoxidase activity and contribute to inflammatory tissue injury.
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Registered trials
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