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• W1993194541 abstract "Hemoglobin is considered a potentially toxic molecule when released from erythrocytes during hemolysis, inflammation, or tissue injury. The mechanisms of toxicity involve reduced nitric oxide bioavailability and oxidative processes both occurring at the heme prosthetic groups. When the endogenous oxidant H2O2 reacts with Hb, transient radicals are generated during the peroxidative consumption of H2O2. If not neutralized, these radicals can lead to tissue toxicity. The net biologic effect of extracellular Hb in an H2O2-rich environment will therefore be determined by the balance of H2O2 decomposition (potential protective effect) and radical generation (potential damaging effect). Here we show that Hb can protect different cell types from H2O2-mediated cell death and the associated depletion of intracellular glutathione and ATP. Importantly, Hb blunts the transcriptional oxidative-stress response induced by H2O2 in human vascular smooth muscle cells (VSMCs). Based on spectrophotometric and quantitative mass spectrometry analysis, we suggested a novel mechanism in which Hb redox-cycles H2O2 and simultaneously internalizes the radical burden, with irreversible structural globin changes starting with specific amino acid oxidation involving the heme proximate βCys93 and ultimately ending with protein precipitation. Our results suggest that complex interactions determine whether extracellular Hb, under certain circumstances, acts a protective or a damaging factor during peroxidative stress conditions. Antioxid. Redox Signal. 12, 185–198." @default.
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• W1993194541 date "2010-01-15" @default.
• W1993194541 modified "2023-10-18" @default.
• W1993194541 title "Hemoglobin Can Attenuate Hydrogen Peroxide–Induced Oxidative Stress by Acting as an Antioxidative Peroxidase" @default.
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• W1993194541 doi "https://doi.org/10.1089/ars.2009.2826" @default.
• W1993194541 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19702440" @default.
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