Title : Polyamine-Conjugated Nitroxides Are Efficacious Inhibitors of Oxidative Reactions Catalyzed by Endothelial-Localized Myeloperoxidase.

Pub. Date : 2021 Jun 21

PMID : 34085520






5 Functional Relationships(s)
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1 At this site, MPO mediates endothelial dysfunction by catalytically consuming nitric oxide (NO) and producing reactive oxidants, hypochlorous acid (HOCl) and the nitrogen dioxide radical ( NO2). Hypochlorous Acid myeloperoxidase Homo sapiens
2 At this site, MPO mediates endothelial dysfunction by catalytically consuming nitric oxide (NO) and producing reactive oxidants, hypochlorous acid (HOCl) and the nitrogen dioxide radical ( NO2). Hypochlorous Acid myeloperoxidase Homo sapiens
3 Nitroxides effectively inhibited the consumption of MPO"s substrate hydrogen peroxide (H2O2) and formation of HOCl catalyzed by endothelial-localized MPO, with their efficacy dependent on both nitroxide and conjugated-polyamine structure. Hypochlorous Acid myeloperoxidase Homo sapiens
4 Nitroxides effectively inhibited the consumption of MPO"s substrate hydrogen peroxide (H2O2) and formation of HOCl catalyzed by endothelial-localized MPO, with their efficacy dependent on both nitroxide and conjugated-polyamine structure. Hypochlorous Acid myeloperoxidase Homo sapiens
5 Novel polyamine-conjugated nitroxides, ethylenediamine-TEMPO and putrescine-TEMPO, emerged as efficacious nitroxides uniquely exhibiting high endothelial cell uptake and efficient inhibition of MPO-catalyzed HOCl production, protein nitration, and NO oxidation. Hypochlorous Acid myeloperoxidase Homo sapiens