ArticleThe Journal of general physiology2001
Reactive oxygen species regulate oxygen-sensitive potassium flux in rainbow trout erythrocytes.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 36 citations in OpenAlex.
- Aptamer-Modified CuJournal of the American Chemical Society · 2021Article
- Hypoxia attenuate ionic transport in the isolated gill epithelium of Carcinus maenas.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2020Article
- Two different oxygen sensors regulate oxygen-sensitive K+ transport in crucian carp red blood cells.The Journal of physiology · 2006Article
- Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter.Molecular and cellular biology · 2006Article
- Regulation of K-Cl cotransport: from function to genes.The Journal of membrane biology · 2004Review
- Pivotal role of reduced glutathione in oxygen-induced regulation of the Na(+)/K(+) pump in mouse erythrocyte membranes.The Journal of membrane biology · 2003Article
- Intracellular pH regulation in rainbow trout (Oncorhynchus mykiss) hepatocytes: the activity of sodium/proton exchange is oxygen-dependent.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the present study, we have investigated if reactive oxygen species are involved in the oxygen-dependent regulation of potassium-chloride cotransport activity in trout erythrocyte membrane. An increase in the oxygen level caused an increase in chloride-sensitive potassium transport (K(+)-Cl(-) cotransport). 5 mM hydrogen peroxide caused an increase in K(+)-Cl(-) cotransport at 5% oxygen. The increase in flux could be inhibited by adding extracellular catalase in the incubation. Pretreatment of the cells with mercaptopropionyl glycine (MPG), a scavenger of reactive oxygen species showing preference for hydroxyl radicals, abolished the activation of the K(+)-Cl(-) cotransporter by increased oxygen levels. The inhibition by MPG was reversible, and MPG could not inhibit the activation of transporter by the sulfhydryl reagent, N-ethylmaleimide, indicating that the effect of MPG was due to the scavenging of reactive oxygen species and not to the reaction of MPG with the cotransporter. Copper ions, which catalyze the production of hydroxyl radicals in the Fenton reaction, activated K(+)-Cl(-) cotransport significantly at hypoxic conditions (1% O(2)). These data suggest that hydroxyl radicals, formed from O(2) in close vicinity to the cell membrane, play an important role in the oxygen-dependent activation of the K(+)-Cl(-) cotransporter.
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