ArticlePloS one2017
Different behavior of myeloperoxidase in two rodent amoebic liver abscess models.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- GalNAc Carbohydrate Prevents the Formation of Neutrophil Extracellular Traps and Increase Myeloperoxidase Enzyme Activity in Interactions of Neutrophils and Entamoeba histolytica Preincubated With GalNAc.BioMed research international · 2026Article
- Antibiotics accumulate inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Entamoeba histolytica extracellular vesicles drive pro-inflammatory monocyte signaling.PLoS neglected tropical diseases · 2025Article
- Neutrophils versus Protozoan Parasites:Microorganisms · 2024Review
- Apocynin, an NADPH Oxidase Enzyme Inhibitor, Prevents Amebic Liver Abscess in Hamster.Biomedicines · 2023Article
- In Vitro Evaluation of the Antiamoebic Activity of Kaempferol against Trophozoites ofInternational journal of molecular sciences · 2023Article
- CD4Molecular medicine reports · 2022Article
- Ascorbic Acid Ameriolates Liver Damage by Myeloperoxidase Oxidative Products in a Hamster Model of Amoebic Liver Abscess.Frontiers in cellular and infection microbiology · 2022Article
- Mechanisms of natural resistance of Balb/c mice to experimental liver amoebiasis.Bioscience reports · 2019Article
- Complement is a rat natural resistance factor to amoebic liver infection.Bioscience reports · 2018Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protozoan Entamoeba histolytica is the etiological agent of amoebiasis, which can spread to the liver and form amoebic liver abscesses. Histological studies conducted with resistant and susceptible models of amoebic liver abscesses (ALAs) have established that neutrophils are the first cells to contact invasive amoebae at the lesion site. Myeloperoxidase is the most abundant enzyme secreted by neutrophils. It uses hydrogen peroxide secreted by the same cells to oxidize chloride ions and produce hypochlorous acid, which is the most efficient microbicidal system of neutrophils. In a previous report, our group demonstrated that myeloperoxidase presents amoebicidal activity in vitro. The aim of the current contribution was to analyze in vivo the role of myeloperoxidase in a susceptible (hamsters) and resistant (Balb/c mice) animal models of ALAs. In liver samples of hamsters and mice inoculated intraportally with Entamoeba histolytica trophozoites, the number of neutrophils in ALAs was determined by enzymatic activity. The presence of myeloperoxidase was observed by staining, and its expression and activity were quantified in situ. A significant difference existed between the two animal models in the number of neutrophils and the expression and activity of myeloperoxidase, which may explain the distinct evolution of amoebic liver abscesses. Hamsters and mice were treated with an MPO inhibitor (4-aminobenzoic acid hydrazide). Hamsters treated with ABAH showed no significant differences in the percentage of lesions or in the percentage of amoebae damaged compared with the untreated hamsters. ABAH treated mice versus untreated mice showed larger abscesses and a decreased percentage of damaged amoebae in these lesion at all stages of evolution. Further studies are needed to elucidate the host and amoebic mechanisms involved in the adequate or inadequate activation and modulation of myeloperoxidase.
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