Oxidation-induced calcium-dependent dehydration of normal human red blood cells

Shcherbachenko, Irina M.; Lisovskaya, I. L.; Tikhonov, Vladimir P.

doi:10.1080/10715760601161452

Cited by 12 publications

(7 citation statements)

References 48 publications

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“…Oxidative damage of erythrocyte membranes frequently produces a rise in the cell volume, a decrease in osmotic resistance and haemolysis. [23][24][25] The increased corpuscular volume in porphyria patients is accompanied by increased MDA content, which is an index of lipid peroxidation and also indicates greater oxidative damage in the erythrocytes of porphyric women than controls. Variegate porphyria induces slightly higher blood haemoglobin, greater mean corpuscular haemoglobin and a higher hematocrit.…”

Section: Discussionmentioning

confidence: 99%

Enzyme antioxidant defences and oxidative damage in red blood cells of variegate porphyria patients

et al. 2009

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Variegate porphyria is the result of decreased protoporphyrinogen oxidase (PPOX) activity, the penultimate enzyme of haem biosynthesis. Haem precursors can produce free radicals and activate oxygen-inducing oxidative stress. Our aim was to analyse the effects of variegate porphyria on haemoglobin levels, antioxidant enzyme activities and oxidative damage in circulating erythrocytes. Twelve women affected by variegate porphyria and 12 control healthy women participated in the study. Women affected by variegate porphyria presented reduced PPOX content and delta-aminolevulinic acid dehydratase activity in erythrocytes. Haemoglobin content and mean corpuscular volume were higher in the porphyric group. Erythrocyte glutathione reductase and superoxide dismutase activities and catalase content were higher in porphyric women, although MDA levels were also higher in the erythrocytes of the porphyric group. In conclusion, the determination of PPOX could be a useful method to detect variegate porphyria. Despite having higher antioxidant defences, erythrocytes of porphyric women have greater oxidative damage and higher corpuscular volume, which are both indices of a situation of higher oxidative stress.

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Section: Discussionmentioning

confidence: 99%

Enzyme antioxidant defences and oxidative damage in red blood cells of variegate porphyria patients

et al. 2009

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“…According to [25] the percentage of the cells that escaped lysis at specific osmolality of the solution was determined by measuring absorbance at 650 nm in a series of cell suspensions in solutions with different osmolality. The absorbance (light scattering) in this case is determined only by the concentration of undestroyed cells in each of the solutions.…”

Section: Methodsmentioning

confidence: 99%

Rapid Elimination of Blood Alcohol Using Erythrocytes: Mathematical Modeling and In Vitro Study

Alexandrovich

Kosenko

Sinauridze

et al. 2017

BioMed Research International

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Erythrocytes (RBCs) loaded with alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALD) can metabolize plasma ethanol and acetaldehyde but with low efficiency. We investigated the rate-limiting factors in ethanol oxidation by these enzymes loaded into RBCs. Mathematical modeling and in vitro experiments on human RBCs loaded simultaneously with ADH and ALD (by hypoosmotic dialysis) were performed. The simulation showed that the rate of nicotinamide-adenine dinucleotide (NAD+) generation in RBC glycolysis, but not the activities of the loaded enzymes, is the rate-limiting step in external ethanol oxidation. The rate of oxidation could be increased if RBCs are supplemented by NAD+ and pyruvate. Our experimental data verified this theoretical conclusion. RBCs loaded with the complete system of ADH, ALD, NAD+, and pyruvate metabolized ethanol 20–40 times faster than reported in previous studies. The one-step procedure of hypoosmotic dialysis is the optimal method to encapsulate ADH and ALD in RBCs after cell recovery, encapsulation yield, osmotic resistance, and RBC-indexes. Consequently, transfusion of the RBCs loaded with the complete metabolic system, including ADH, ALD, pyruvate, and NAD+ in the patients with alcohol intoxication, may be a promising method for rapid detoxification of blood alcohol based on metabolism.

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“…3b Strongin et al (1993). PMS, a procyanin analog, is a strong oxidant that induces intracellular ROS (Shcherbachenko et al 2007). Direct treatment with extracellular H 2 O 2 could not induce pro-MMP-2 activation, whereas intracellular H 2 O 2 induced by PMS could induce pro-MMP-2 activation (Yoon et al 2002).…”

Section: Erw Inhibits the Invasion Of Ht1080 Cellsmentioning

confidence: 98%

Suppressive effects of electrochemically reduced water on matrix metalloproteinase-2 activities and in vitro invasion of human fibrosarcoma HT1080 cells

Kinjo

Yan

et al. 2012

Cytotechnology

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It has been demonstrated that hydrogen peroxide (H(2)O(2)) is directly associated with elevated matrix metalloproteinase-2 (MMP-2) expression in several cell lines. Electrochemically reduced water (ERW), produced near the cathode during electrolysis, and scavenges intracellular H(2)O(2) in human fibrosarcoma HT1080 cells. RT-PCR and zymography analyses revealed that when HT1080 cells were treated with ERW, the gene expression of MMP-2 and membrane type 1 MMP and activation of MMP-2 was repressed, resulting in decreased invasion of the cells into matrigel. ERW also inhibited H(2)O(2)-induced MMP-2 upregulation. To investigate signal transduction involved in MMP-2 downregulation, mitogen-activated protein kinase (MAPK)-specific inhibitors, SB203580 (p38 MAPK inhibitor), PD98059 (MAPK/extracellular regulated kinase kinase 1 inhibitor) and c-Jun NH(2)-terminal kinase inhibitor II, were used to block the MAPK signal cascade. MMP-2 gene expression was only inhibited by SB203580 treatment, suggesting a pivotal role of p38 MAPK in regulation of MMP-2 gene expression. Western blot analysis showed that ERW downregulated the phosphorylation of p38 both in H(2)O(2)-treated and untreated HT1080 cells. These results indicate that the inhibitory effect of ERW on tumor invasion is due to, at least in part, its antioxidative effect.

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Oxidation-induced calcium-dependent dehydration of normal human red blood cells

Cited by 12 publications

References 48 publications

Enzyme antioxidant defences and oxidative damage in red blood cells of variegate porphyria patients

Enzyme antioxidant defences and oxidative damage in red blood cells of variegate porphyria patients

Rapid Elimination of Blood Alcohol Using Erythrocytes: Mathematical Modeling and In Vitro Study

Suppressive effects of electrochemically reduced water on matrix metalloproteinase-2 activities and in vitro invasion of human fibrosarcoma HT1080 cells

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