Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15‐hydroperoxy‐5,8,11,13‐eicosatetraenoic acid

Walters, Frederick P.; Kennedy, F. G.; Jones, Dean P.

doi:10.1016/0014-5793(83)80838-2

Cited by 46 publications

(11 citation statements)

References 25 publications

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“…As it was expected that the amounts of the radical would be increased with more than 0.3 mM hydrogen peroxide, a high concentration of the radical would make hemoglobin polymerize to become adducts, and the erythrocytes thus would become insoluble in water. The abnormal reaction with hydrogen peroxide caused the shape change of the erythrocytes, which resembled that of cardiac myocytes treated with lipid hydroperoxide (22). Furthermore, aggregation was observed in the system (Fig.…”

Section: Discussionmentioning

confidence: 82%

Characterization of Acatalasemic Erythrocytes Treated with Low and High Dose Hydrogen Peroxide

Masuoka

Sugiyama

Ishibashi

et al. 2006

Journal of Biological Chemistry

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The effects of hydrogen peroxide on normal and acatalasemic erythrocytes were examined. Severe hemolysis of acatalasemic erythrocytes and a small tyrosine radical signal (g ‫؍‬ 2.005) associated with the formation of ferryl hemoglobin were observed upon the addition of less than 0.25 mM hydrogen peroxide. However, when the concentration of hydrogen peroxide was increased to 0.5 mM, acatalasemic erythrocytes became insoluble in water and increased the tyrosine radical signal. Polymerization of hemoglobin and aggregation of the erythrocytes were observed. On the other hand, normal erythrocytes exhibited only mild hemolysis by the addition of hydrogen peroxide under similar conditions. From these results, the scavenging of hydrogen peroxide by hemoglobin generates the ferryl hemoglobin species (H-Hb-Fe(IV)‫؍‬O) plus protein-based radicals ( ⅐ HbFe(IV)‫؍‬O). These species induce hemolysis of erythrocytes, polymerization of hemoglobin, and aggregation of the acatalasemic erythrocytes. A mechanism for the onset of Takarara disease is proposed.In 1952, Takahara reported that Japanese acatalasemia (catalase deficiency) patients suffered from progressive oral gangrene (Takahara disease) as a result of being infected with hydrogen peroxide-generating bacteria (1). Subsequently, Swiss and Hungarian acatalasemia-afflicted people were reported, but they did not evidently suffer from the symptomatic features of the disease (2, 3). The residual catalase (EC 1.11.1.6) activity in Swiss and Hungarian acatalasemic erythrocytes was found to be higher than in the erythrocytes from the Japanese. Ogata et al. (4) suggested the catalase deficiency in the blood to be the etiological cause of the disease. We became interested in the scavenging of hydrogen peroxide in erythrocytes to understand the metabolism of hydrogen peroxide in acatalasemic erythrocytes. The hydrogen peroxide scavenging rates in normal and acatalasemic mouse and human erythrocytes were examined (5-8). It was found that hydrogen peroxide was dominantly scavenged by hemoglobin in hemolysates of acatalasemic erythrocytes. The scavenging rate was enhanced in the presence of reduced pyridine nucleotides (NAD(P)H) or ascorbic acid (AsA).2 A cyclic process has been proposed for the scavenging mechanism; hydrogen peroxide oxidizes hemoglobin, which is then reduced by NAD(P)H or AsA (8).We suspected that during the process, hemoglobin was oxidized to ferryl hemoglobin (H-Hb-Fe(IV)ϭO) with hydrogen peroxide, and then a comproportionation reaction of Hb-Fe(IV)ϭO and ferrous hemoglobin generated methemoglobin (H-Hb-Fe(III) ϩ ) (9). Methemoglobin was then further oxidized to radicals of ferryl hemoglobin ( ⅐ Hb-Fe(IV)ϭO) with hydrogen peroxide (10). In this study, we report that the oxidized hemoglobin species in the scavenging process were identified and that a novel property of acatalasemic erythrocytes was subjected to hydrogen peroxide treatment; erythrocytes aggregated to be insoluble in water at a high concentration (Ն0.5 mM) of hydrogen peroxide, whereas the severe hemol...

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Section: Discussionmentioning

confidence: 82%

Characterization of Acatalasemic Erythrocytes Treated with Low and High Dose Hydrogen Peroxide

Masuoka

Sugiyama

Ishibashi

et al. 2006

Journal of Biological Chemistry

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“…617 nm owing to the addition of sulphur to the haem porphyrin ring, resulting in ferrous sulphMb [28]. The addition of Na # S (1 mM) to an incubated sample of metMb and HPODE showed a similar peak at 617 nm, indicating the formation of sulphMb from ferrylMb ( Figure 3).…”

Section: Detection and Quantification Of Ferryl Myoglobin By Sulphidementioning

confidence: 94%

Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid

Reeder

Wilson

1998

Biochemical Journal

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The reaction between myoglobin and the lipid hydroperoxide 13(S)-hydroperoxy-9,11(cis,trans)-octadecadienoic acid (HPODE) was studied kinetically by spectrophotometric, polarographic and analytical methods. Metmyoglobin catalysed the decomposition of HPODE, resulting in peroxide, oxygen and conjugated diene depletion, together with the transient production of ferryl myoglobin. The reaction stoichiometry was 2:1:1 for peroxide to oxygen to conjugated diene, whereas the myoglobin remained generally intact. This stoichiometry and the rates of change of conjugated diene and ferryl myoglobin concentrations were not completely consistent with previously proposed mechanisms. We propose a novel mechanism in which HPODE reacts with both ferric myoglobin and ferryl myoglobin to form a redox cycle. Both peroxyl and alkoxyl radicals are produced, explaining the observed stoichiometry of peroxide, oxygen and conjugated diene depletion and the transient appearance of ferryl myoglobin. Computer simulation shows that this mechanism is fully capable of reproducing the observed time courses of all components.

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“…Because almost all inflammatory cells in EAM are αβT cells and CD11bc + cells, the NC cells were further separated into αβT cells, CD11bc + cells and NCNI cells such as fibroblasts, smooth muscle cells or endothelial cells with anti-phycoerythrin (PE) micro beads (Miltenyi Biotec, Bergisch Gladbach, Germany) and a MACS magnetic cell sorting system (Miltenyi Biotech) using appropriate monoclonal antibodies, namely PE-conjugated TCRαβ (R73) and CD11bc (OX-42) (Pharmingen, San Diego, CA, USA) [23]. Normal rats were killed and EAM rats were killed on Days 6,9,12,15,18,30 and 60, and their cardiomyocytes were similarly purified for time course analysis of hepcidin, Cox6a2 and hypoxia inducible factor (HIF)-1-α gene expression. For analysis of the relationship between hepcidin/ Cox6a2 and IL-6/γ-actin gene expression or between BNP/Cox6a2 and IL-6/γ-actin gene expression, parts of both ventricles from normal rats and EAM rats killed on Days 6,9,12,15,18,30 and 60 and adjuvant control injected only with adjuvant without cardiac myosin were collected.…”

Section: Induction Of Eam and Purification Of Cellsmentioning

confidence: 99%

“…Normal rats were killed and EAM rats were killed on Days 6,9,12,15,18,30 and 60, and their cardiomyocytes were similarly purified for time course analysis of hepcidin, Cox6a2 and hypoxia inducible factor (HIF)-1-α gene expression. For analysis of the relationship between hepcidin/ Cox6a2 and IL-6/γ-actin gene expression or between BNP/Cox6a2 and IL-6/γ-actin gene expression, parts of both ventricles from normal rats and EAM rats killed on Days 6,9,12,15,18,30 and 60 and adjuvant control injected only with adjuvant without cardiac myosin were collected. To examine hepcidin-expressing organs in EAM, parts of hearts, livers, kidneys and spleens from normal rats and adjuvant control and EAM rats on Day13 were collected.…”

Section: Induction Of Eam and Purification Of Cellsmentioning

confidence: 99%

“…On the other hand, excessive iron is also involved in injury of various tissues and organs due to its ability to catalyze the production of reactive oxygen species [11]. In particular, the cardiomyocyte, which contains myoglobin, is a primary cellular source of large amounts of iron [12,13]. Therefore, destruction of cardiac tissue is thought to release large amounts of iron into the extracellular space.…”

Section: Introductionmentioning

confidence: 99%

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Expression of the peptide hormone hepcidin increases in cardiomyocytes under myocarditis and myocardial infarction

Isoda

Hanawa

Watanabe

et al. 2010

The Journal of Nutritional Biochemistry

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Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15‐hydroperoxy‐5,8,11,13‐eicosatetraenoic acid

Cited by 46 publications

References 25 publications

Characterization of Acatalasemic Erythrocytes Treated with Low and High Dose Hydrogen Peroxide

Characterization of Acatalasemic Erythrocytes Treated with Low and High Dose Hydrogen Peroxide

Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid

Expression of the peptide hormone hepcidin increases in cardiomyocytes under myocarditis and myocardial infarction

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