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Reactive oxygen species do not cause arsine-induced hemoglobin damage
1Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, USA.
Journal of Toxicology and Environmental Health
|April 11, 1997
Summary
Arsine (AsH3) causes hemoglobin damage, but reactive oxygen species are not the primary cause. In vitro, hydrogen peroxide is formed, but cellular defenses handle it, suggesting an alternative arsenic-based hemolytic mechanism.
Area of Science:
- Toxicology
- Biochemistry
- Hematology
Background:
- Previous studies linked arsine (AsH3) exposure to hemoglobin (HbO2) damage and hemolysis.
- The role of reactive oxygen species (ROS) in AsH3-induced HbO2 damage remained unclear.
Purpose of the Study:
- To investigate ROS formation by AsH3 in various solutions.
- To determine if ROS mediate AsH3-induced HbO2 damage.
- To explore alternative mechanisms of AsH3 toxicity.
Main Methods:
- Detection of hydrogen peroxide (H2O2) in AsH3 and HbO2 solutions.
- Assessing the protective effects of catalase and glutathione peroxidase.
- Measuring superoxide anion (O2-) using nitro blue tetrazolium (NBT) reduction.
- Evaluating the impact of superoxide dismutase, mannitol, DMSO, ascorbate, and glutathione on HbO2 spectral changes.
Main Results:
- H2O2 was detected in aqueous solutions with AsH3, but not in intact red blood cells or lysates.
- Catalase and glutathione peroxidase offered only minor protection against AsH3-induced damage.
- Superoxide anion and hydroxyl radical were not implicated in the damage.
- Antioxidants like ascorbate and glutathione showed no protective effect.
Conclusions:
- AsH3 can generate H2O2 in vitro, but it is effectively detoxified by cellular defenses.
- Superoxide anion and hydroxyl radical are not the primary mediators of AsH3-induced HbO2 damage.
- An alternative mechanism, possibly involving a direct arsenic species, is proposed for AsH3-induced hemolysis.