Hydroxylamine and phenol-induced formation of methemoglobin and free radical intermediates in erythrocytes

Stolze, Klaus; Dadak, Agnes; Liu, Yang; Nohl, Hans

doi:10.1016/s0006-2952(96)00460-1

Cited by 48 publications

(25 citation statements)

References 30 publications

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“…It has previously been shown that HU reacts with sickle cell hemoglobin to form methemoglobin and hemichromes [11]. The formation of methemoglobin and hemichromes is known to lead to membrane damage in the erythrocyte [3,18]. In vivo, methemoglobin may have beneficial effects on the sickle cell membrane in addition to these deleterious ones.…”

Section: Discussionmentioning

confidence: 99%

“…Because HU reacts with Hb S to form methemoglobin [11], and methemoglobin can adversely effect erythrocyte deformability [18], we hypothesized that HU-incubated cells would have decreased deformability. Methemoglobin can act to decrease deformability though oxidative stress resulting from its formation and from its degradation products [3,18]. In vivo, small amounts of methemoglobin may benefit patients by prolonging the delay time for polymerization and thus reducing sickling.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Untitled

2001

American J Hematol

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Hydroxyurea is a drug that is used to treat some patients with sickle cell disease. We have measured the deformability of sickle erythrocytes incubated in hydroxyurea in vitro and found that hydroxyurea acts to decrease the deformability of these cells. The deformability of normal erythrocytes was not significantly affected by hydroxyurea except at very high concentrations. Hydroxyurea also did not consistently reduce the deformability of sickle erythrocyte ghosts. We propose that the decreased deformability, observed in vitro, is due to the formation of methemoglobin and other oxidative processes resulting from the reaction of hydroxyurea and oxyhemoglobin. Although the reaction with normal hemoglobin is similar to that of sickle hemoglobin, the sickle erythrocytes are affected more. We propose that the sickle erythrocyte membrane is more susceptible to the reaction products of the reaction of hemoglobin and hydroxyurea. An earlier report has shown that hydroxyurea increases the deformability of erythrocytes in patients on hydroxyurea. Taken

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Untitled

2001

American J Hematol

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“…Thus, the nitroxide-type ROS radicals can react with a variety of biological substrates. The same hydronitroxide radical was shown to be generated as an intermediate in the conversion of hemoglobin to methemoglobin following the reaction of HA with intact erythrocytes or with oxyhemoglobin 70 . The formation of ROS from HA can initiate lipid peroxidation that can give rise to general protein damage.…”

Section: B Has and Reactive Oxygen Species (Ros)mentioning

confidence: 95%

Hydroxylamines and Oximes: Biological Properties and Potential Uses as Therapeutic Agents

Ashani¹,

Silman²

2010

Patai's Chemistry of Functional Groups

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“…The sample was spun in a centrifuge at 2000 rpm for 5 min. Repeated above process; removed the plasma, serum, and white blood cell [30]. Then the cellular membrane lysed by sonication for 5 min, diluted to 2 mL with 50 mM PBS (pH 7.4) and stored in refrigerator.…”

Section: Methodsmentioning

confidence: 99%