Atherogenesis May Involve the Prooxidant and Proinflammatory Effects of Ferryl Hemoglobin

التفاصيل البيبلوغرافية
العنوان: Atherogenesis May Involve the Prooxidant and Proinflammatory Effects of Ferryl Hemoglobin
المؤلفون: Miguel P. Soares, Gergely Becs, Emese Bányai, Viktória Jeney, József Balla, György Balla, László Potor
المصدر: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Oxidative Medicine and Cellular Longevity
Oxidative Medicine and Cellular Longevity, Vol 2013 (2013)
بيانات النشر: Hindawi Publishing Corporation, 2013.
سنة النشر: 2013
مصطلحات موضوعية: Aging, Cell Membrane Permeability, Article Subject, 030204 cardiovascular system & hematology, Klinikai orvostudományok, Biochemistry, Monocytes, Methemoglobin, 03 medical and health sciences, chemistry.chemical_compound, Hemoglobins, 0302 clinical medicine, Cell Adhesion, Human Umbilical Vein Endothelial Cells, Humans, Globin, lcsh:QH573-671, Cell adhesion, Heme, 030304 developmental biology, Glutathione Peroxidase, 0303 health sciences, Haptoglobins, lcsh:Cytology, Cell adhesion molecule, Hydrogen Peroxide, Orvostudományok, Cell Biology, General Medicine, Glutathione, Oxidants, Atherosclerosis, Lipoproteins, LDL, Cross-Linking Reagents, chemistry, Ferritins, Hemoglobin, Inflammation Mediators, Oxidation-Reduction, Heme Oxygenase-1, Research Article, Lipoprotein
الوصف: Oxidized cell-free hemoglobin (Hb), including covalently cross-linked Hb multimers, is present in advanced atherosclerotic lesions. Oxidation of Hb produces methemoglobin (Fe3+) and ferryl hemoglobin (Fe4+=O2−). Ferryl iron is unstable and can return to theFe3+state by reacting with specific amino acids of the globin chains. In these reactions globin radicals are produced followed by termination reactions yielding covalently cross-linked Hb multimers. Despite the evanescent nature of the ferryl state, herein we refer to this oxidized Hb as “ferryl Hb.” Our aim in this work was to study formation and biological effects of ferrylHb. We demonstrate that ferrylHb, like metHb, can release its heme group, leading to sensitization of endothelial cells (ECs) to oxidant-mediated killing and to oxidation of low-density lipoprotein (LDL). Furthermore, we observed that both oxidized LDL and lipids derived from human atherosclerotic lesions trigger Hb oxidation and subsequent production of covalently cross-linked ferrylHb multimers. Previously we showed that ferrylHb disrupts EC monolayer integrity and induces expression of inflammatory cell adhesion molecules. Here we show that when exposed to ferrylHb, EC monolayers exhibit increased permeability and enhanced monocyte adhesion. Taken together, interactions between cell-free Hb and atheroma lipids engage in a vicious cycle, amplifying oxidation of plaque lipids and Hb. These processes trigger EC activation and cytotoxicity.
وصف الملف: text/xhtml; application/pdf
اللغة: English
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e88edb0f7903bcaf80167240e4e6b14Test
https://hdl.handle.net/10400.7/474Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....8e88edb0f7903bcaf80167240e4e6b14
قاعدة البيانات: OpenAIRE