Oxidants and regulation of K(+)-Cl(-) cotransport in equine red blood cells.
Abstract: The effect of oxidants on K(+)-Cl(-) cotransport (KCC) was investigated in equine red blood cells. Carbon monoxide mimicked O(2). The substituted benzaldehyde, 12C79 (5 mM), markedly increased O(2) affinity. In N(2), however, O(2) saturation was low (<10%) but KCC remained active. Nitrite (NO(2)(-)) oxidized heme to methemoglobin (metHb). High concentrations of NO(2)(-) (1 and 5 mM vs. 0.5 mM) increased KCC activity above control levels; it became O(2) independent but remained sensitive to other stimuli. 1-Chloro-2, 4-dinitrobenzene (1-3 mM) depleted reduced glutathione (GSH). Prolonged exposure (60-120 min, 1 mM) or high concentrations (3 mM) stimulated an O(2)-independent KCC activity; short exposures and low concentrations (30 min, 0.5 or 1 mM) did not. The effect of these manipulations was correlated with changes in GSH and metHb concentrations. An oxy conformation of Hb was necessary for KCC activation. An increase in its activity over the level found in oxygenated control cells required both accumulation of metHb and depletion of GSH. Findings are relevant to understanding the physiology and pathology of regulation of KCC.
Publication Date: 2000-09-26 PubMed ID: 11003578DOI: 10.1152/ajpcell.2000.279.4.C981Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research work explores the impact of oxidants on a certain function, specifically the K(+)-Cl(-) cotransport (KCC), in equine red blood cells. This study aids in enhancing our understanding of the function and regulation of KCC in physiological and pathological scenarios.
Objective and Methodology
The investigators aimed to comprehend the impact of various compounds, recognized as oxidants, on the process of K(+)-Cl(-) cotransport in horse red blood cells. This transport method involves the coordinated movement of potassium (K+) and chloride (Cl-) ions across the cell membrane. Oxidants are substances that can accept electrons and can result in a process known as oxidation, which can affect cell functions.
Findings
- Upon exposure to Carbon Monoxide (CO), the effect was similar to how oxygen (O2) would affect the process. Carbon Monoxide acts like a mimic of oxygen.
- A chemical compound known as 12C79 significantly increased the affinity for oxygen, meaning that cells became more responsive to oxygen.
- In Nitrogen (N2) settings, oxygen saturation was found to be low, less than 10%. Despite this fact, the KCC activity remained active.
- Nitrite (NO2-) oxidized heme into methemoglobin (metHb). When the cells were exposed to higher concentrations of NO2-, it led to an increase in KCC activity higher than the usual levels.
- Upon application of 1-Chloro-2,4-dinitrobenzene, there was depletion of reduced glutathione (GSH), an important antioxidant within the cell. Long exposures or high concentrations of this substance instigated an oxygen-independent KCC activity.
- The manipulation effects observed were correlated with the changes in the concentrations of metHb and GSH.
- For the activation of KCC, an oxy conforming state of hemoglobin was deemed necessary.
- An increase in the KCC activity beyond what was noticed in oxygenated control cells required two conditions: accumulation of methemoglobin and depletion of reduced glutathione.
Relevance of Findings
This piece of research contributes to our understanding of the intricate roles and regulations of the KCC mechanism in red blood cells. This function is particularly important in maintaining the ion balance within the cells. Interruptions in this process may lead to medical conditions such as anemia, dehydration of cells, and other related disorders. By identifying how oxidants can influence KCC, this research forms a building block for further studies into the treatment and prevention of certain disease conditions.
Cite This Article
APA
Muzyamba MC, Speake PF, Gibson JS.
(2000).
Oxidants and regulation of K(+)-Cl(-) cotransport in equine red blood cells.
Am J Physiol Cell Physiol, 279(4), C981-C989.
https://doi.org/10.1152/ajpcell.2000.279.4.C981 Publication
Researcher Affiliations
- Department of Veterinary Preclinical Sciences, University of Liverpool, Liverpool L69 7ZJ, United Kingdom.
MeSH Terms
- Animals
- Benzaldehydes / pharmacology
- Biological Transport, Active / drug effects
- Carbon Monoxide / pharmacokinetics
- Carbon Monoxide / pharmacology
- Carrier Proteins / drug effects
- Carrier Proteins / metabolism
- Cell Size / drug effects
- Dinitrochlorobenzene / pharmacology
- Dose-Response Relationship, Drug
- Enzyme Inhibitors / pharmacology
- Erythrocytes / cytology
- Erythrocytes / drug effects
- Erythrocytes / metabolism
- Glutathione / metabolism
- Horses
- Hypotonic Solutions / pharmacology
- Ion Transport / drug effects
- Methemoglobin / metabolism
- Nitrites / metabolism
- Nitrites / pharmacology
- Nitrogen / pharmacology
- Osmolar Concentration
- Oxidants / metabolism
- Oxidants / pharmacology
- Oxygen / metabolism
- Phosphoprotein Phosphatases / antagonists & inhibitors
- Potassium / metabolism
- Symporters
- Water / metabolism
Citations
This article has been cited 10 times.- Al Balushi H, Hannemann A, Rees D, Brewin J, Gibson JS. The Effect of Antioxidants on the Properties of Red Blood Cells From Patients With Sickle Cell Anemia. Front Physiol 2019;10:976.
- Andreyeva AY, Soldatov AA, Krivchenko AI, Mindukshev IV, Gambaryan S. Hemoglobin deoxygenation and methemoglobinemia prevent regulatory volume decrease in crucian carp (Carassius carassius) red blood cells. Fish Physiol Biochem 2019 Dec;45(6):1933-1940.
- Hannemann A, Rees DC, Brewin JN, Noe A, Low B, Gibson JS. Oxidative stress and phosphatidylserine exposure in red cells from patients with sickle cell anaemia. Br J Haematol 2018 Aug;182(4):567-578.
- Al Balushi HWM, Rees DC, Brewin JN, Hannemann A, Gibson JS. The effect of xanthine oxidase and hypoxanthine on the permeability of red cells from patients with sickle cell anemia. Physiol Rep 2018 Mar;6(5).
- Sega MF, Chu H, Christian J, Low PS. Interaction of deoxyhemoglobin with the cytoplasmic domain of murine erythrocyte band 3. Biochemistry 2012 Apr 17;51(15):3264-72.
- Cheng N, Liu F, Zhang L, Xu XH, Gorthala S, Bai Y. Enrichment of nuclear red blood cells by membrane KCC transporter with urea intervention. J Clin Lab Anal 2011;25(1):1-7.
- Lee YS. Arachidonic Acid Activates K-Cl-cotransport in HepG2 Human Hepatoblastoma Cells. Korean J Physiol Pharmacol 2009 Oct;13(5):401-8.
- Adragna NC, Di Fulvio M, Lauf PK. Regulation of K-Cl cotransport: from function to genes. J Membr Biol 2004 Oct 1;201(3):109-37.
- Muzyamba MC, Gibson JS. Effect of 1-chloro-2,4-dinitrobenzene on K+ transport in normal and sickle human red blood cells. J Physiol 2003 Mar 15;547(Pt 3):903-11.
- Bogdanova AY, Nikinmaa M. Reactive oxygen species regulate oxygen-sensitive potassium flux in rainbow trout erythrocytes. J Gen Physiol 2001 Feb;117(2):181-90.
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