ArticlePloS one2011
Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
The trial behind it
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
19 citing papers in PubMed, 41 citations in OpenAlex.
- Electrolyzed Water as a Biocide in Premise Water Networks: A Narrative Review and a Conceptual Framework.Pathogens (Basel, Switzerland) · 2026Review
- Serum melatonin as a potential biomarker for COVID-19 severity.Scientific reports · 2025Article
- Real-timeBiomedical optics express · 2023Article
- Melatonin interferes with COVID-19 at several distinct ROS-related steps.Journal of inorganic biochemistry · 2021Review
- Development of an ultrafast fluorescent probe for specific recognition of hypochlorous acid and its application in live cells.RSC advances · 2021Article
- Methoxyphenol derivatives as reversible inhibitors of myeloperoxidase as potential antiatherosclerotic agents.Future medicinal chemistry · 2020Article
- A fluorescent hydrazone exchange probe of pyridoxal phosphate for the assessment of vitamin B6 status.Chemical communications (Cambridge, England) · 2019Article
- Melatonin prevents hypochlorous acid-mediated cyanocobalamin destruction and cyanogen chloride generation.Journal of pineal research · 2018Article
- Antiinflammatory and Antimicrobial Effects of Thiocyanate in a Cystic Fibrosis Mouse Model.American journal of respiratory cell and molecular biology · 2015Article
- Hypochlorous acid via peroxynitrite activates protein kinase Cθ and insulin resistance in adipocytes.Journal of molecular endocrinology · 2015Article
- Melatonin prevents myeloperoxidase heme destruction and the generation of free iron mediated by self-generated hypochlorous acid.PloS one · 2015Article
- Diffused Intra-Oocyte Hydrogen Peroxide Activates Myeloperoxidase and Deteriorates Oocyte Quality.PloS one · 2015Article
- Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid.Journal of inorganic biochemistry · 2014Article
- Article
- Mode of action of lactoperoxidase as related to its antimicrobial activity: a review.Enzyme research · 2014Review
- Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway.Free radical biology & medicine · 2013Article
- Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense.The Journal of biological chemistry · 2013Article
- Impact of hydrogen peroxide-driven Fenton reaction on mouse oocyte quality.Free radical biology & medicine · 2013Article
- Identification of a hypochlorite-specific transcription factor from Escherichia coli.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent. In nasal inflammatory diseases, such as cystic fibrosis, both LPO and myeloperoxidase (MPO), another mammalian peroxidase secreted by neutrophils, are known to co-localize. The aim of this study was to assess the interaction of LPO and hypochlorous acid (HOCl), the final product of MPO. Our rapid kinetic measurements revealed that HOCl binds rapidly and reversibly to LPO-Fe(III) to form the LPO-Fe(III)-OCl complex, which in turn decayed irreversibly to LPO Compound II through the formation of Compound I. The decay rate constant of Compound II decreased with increasing HOCl concentration with an inflection point at 100 µM HOCl, after which the decay rate increased. This point of inflection is the critical concentration of HOCl beyond which HOCl switches its role, from mediating destabilization of LPO Compound II to LPO heme destruction. Lactoperoxidase heme destruction was associated with protein aggregation, free iron release, and formation of a number of fluorescent heme degradation products. Similar results were obtained when LPO-Fe(II)-O(2), Compound III, was exposed to HOCl. Heme destruction can be partially or completely prevented in the presence of SCN(-). On the basis of the present results we concluded that a complex bi-directional relationship exists between LPO activity and HOCl levels at sites of inflammation; LPO serve as a catalytic sink for HOCl, while HOCl serves to modulate LPO catalytic activity, bioavailability, and function.
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Registered trials
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