The reaction of hydrogen peroxide with hemoglobin induces extensive alpha-globin crosslinking and impairs the interaction of hemoglobin with endogenous scavenger pathways

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Author(s) Vallelian, Florence, Pimenova, Tatiana, Pereira, Claudia P., Abraham, Bindu, Mikolajczyk, Malgorzata G., Schoedon, Gabriele, Zenobi, Renato, Alayash, Abdu I., Buehler, Paul W., Schaer, Dominik J.
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Title The reaction of hydrogen peroxide with hemoglobin induces extensive alpha-globin crosslinking and impairs the interaction of hemoglobin with endogenous scavenger pathways
Author(s) Vallelian, Florence
Pimenova, Tatiana
Pereira, Claudia P.
Abraham, Bindu
Mikolajczyk, Malgorzata G.
Schoedon, Gabriele
Zenobi, Renato
Alayash, Abdu I.
Buehler, Paul W.
Schaer, Dominik J.
Journal or Series Title Free radical biology & medicine
Volume Number 45
Issue Number 8
Start Page 1150
End Page 1158
ISSN 0891-5849
Publisher Elsevier
Publication Place Amsterdam
Publication Date 2008-10-15
Keyword(s) Hemoglobin
Haptoglobin
CD163
Hydrogen peroxide
Oxidative stress
Abstract Cell-free hemoglobin (Hb) enhances the oxidation-related toxicity associated with inflammation, ischemia, and hemolytic disorders. Hb is highly vulnerable to oxidative damage, and irreversible structural changes involving iron/heme oxidation, heme-adduct products, and amino acid oxidation have been reported. Specific structural features of Hb, such as unconstrained a-chains and molecular size, determine the efficiency of interactions between the endogenous Hb scavengers haptoglobin (Hp) and CD163. Using HPLC, mass spectrometry, and Western blotting, we show that H2O2-mediated Hb oxidation results in the formation of covalently stabilized globin multimers, with prominent intramolecular crosslinking between a-globin chains. These structural alterations are associated with reduced Hp binding, reduced CD163 interaction, and severely impaired endocytosis of oxidized Hb by the Hp-CD163 pathway. As a result, when exposed to oxidized Hb, CD163-positive HEK293 cells and human macrophages do not increase hemeoxygenase-1 (HO-1) expression, the physiological anti-oxidative macrophage response to Hb exposure. Failed Hb clearance, inadequate HO-1 expression, and the subsequent accumulation of oxidatively damaged Hb species might thus contribute to pathologies related to oxidative stress.
DOI 10.1016/j.freeradbiomed.2008.07.013
Additional Notes Received 16 May 2008, Received 19 June 2008, Accepted 10 July 2008, Published online 27 July 2008
Document Type Article
Publication Status Published
Language English
NEBIS System Number 000038482
Source Database ID WOS-000260161300012
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@article{Vllln2008,
  author = "Vallelian, Florence and Pimenova, Tatiana and Pereira, Claudia P. and Abraham, Bindu and Mikolajczyk, Malgorzata G. and Schoedon, Gabriele and Zenobi, Renato and Alayash, Abdu I. and Buehler, Paul W. and Schaer, Dominik J.",
  title = "{T}he reaction of hydrogen peroxide with hemoglobin induces extensive alpha-globin crosslinking and impairs the interaction of hemoglobin with endogenous scavenger pathways",
  journal = "Free radical biology \& medicine",
  year = 2008,
  volume = "45",
  number = "8",
  pages = "1150--1158",
  month = oct,
}


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