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NADPH oxidase-dependent free radical generation and protein adduct formation in neutrophils

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F24%3A73626490" target="_blank" >RIV/61989592:15110/24:73626490 - isvavai.cz</a>

  • Alternative codes found

    RIV/61989592:15310/24:73626490

  • Result on the web

    <a href="https://pubs.rsc.org/en/content/articlepdf/2024/ra/d4ra02739f" target="_blank" >https://pubs.rsc.org/en/content/articlepdf/2024/ra/d4ra02739f</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/d4ra02739f" target="_blank" >10.1039/d4ra02739f</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    NADPH oxidase-dependent free radical generation and protein adduct formation in neutrophils

  • Original language description

    Neutrophils mediate the early innate immune response through extracellular traps comprising intracellular protein and DNA. These traps play a pivotal role in both immunity against invading pathogens and the development of immunopathological reactions through the production of reactive oxygen species (ROS). Proteins serve as the main target for ROS, resulting in the formation of protein adducts. Herein, we report that the superoxide anion radical (O2(center dot)-) plays a vital role in neutrophil function through sequential events involving 5-lipoxygenase (5-LOX) and NADPH oxidase (NOX). More specifically, differences in NOX homologs expression were observed post-stimulation with PMA and LPS. Differentiation conditions and O2(center dot)- generation were confirmed using flow cytometry. Immunoblotting analysis confirmed the time-dependent expression of NOX underlying its requirement and 5-LOX-mediated lipid peroxidation events in neutrophil function. Protein-malondialdehyde (MDA) adducts formed were detected using immunoblotting, and quercetin was evaluated for its ability to scavenge free radicals through electron paramagnetic resonance (EPR) spin-trapping spectroscopy and results were confirmed with blotting analysis. Free radical-mediated protein oxidation events influence neutrophil function and protein adducts formed serve as markers of neutrophil activation upon infection and inflammation. The study warrants further corroboration and the study of specific proteins involved in neutrophil activation and their role in inflammation.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Plants as a tool for sustainable global development</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    RSC Advances

  • ISSN

    2046-2069

  • e-ISSN

  • Volume of the periodical

    14

  • Issue of the periodical within the volume

    34

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    16

  • Pages from-to

    24765-24780

  • UT code for WoS article

    001285891100001

  • EID of the result in the Scopus database

    2-s2.0-85200946122