Structural alterations of erythrocyte membrane components induced by exhaustive exercise

2008 ◽  
Vol 33 (6) ◽  
pp. 1223-1231 ◽  
Author(s):  
Joanna Brzeszczynska ◽  
Anna Pieniazek ◽  
Lukasz Gwozdzinski ◽  
Krzysztof Gwozdzinski ◽  
Anna Jegier
Keyword(s):  
Lipid Peroxidation ◽  
Membrane Proteins ◽  
Membrane Fluidity ◽  
Erythrocyte Membrane ◽  
Conformational Changes ◽  
Membrane Dynamics ◽  
Resonance Spectroscopy ◽  
Reducing Ability ◽  
Exercise Induced ◽  
Membrane Components

Physical exercise was used as a model of the physiological modulator of free radical production to examine the effects of exercise-induced oxidative modifications on the physico-biochemical properties of erythrocyte membrane. The aim of our work was to investigate conformational changes of erythrocyte membrane proteins, membrane fluidity, and membrane susceptibility to disintegration. Venous blood was taken before, immediately after, and 1 h after an exhaustive incremental cycling test (30 W·min–1ramp), performed by 11 healthy untrained males on balanced diets (mean age, 22 ± 2 years; mean body mass index, 25 ± 4.5 kg·m–2). In response to this exercise, individual maximum heart rate was 195 ± 12 beats·min–1and maximum wattage was 292 ± 27 W. Electron paramagnetic resonance spectroscopy was used to investigate alterations in membrane proteins and membrane dynamics, and to measure production of radical species. The reducing potential of plasma (RPP) was measured using the reduction of 1,1-diphenyl-2-picrylhydrazyl (DPPH) and the ferric-reducing ability of plasma. Exercise induced decreases in erythrocyte membrane fluidity in the polar region (p < 0.0001) and alterations in the conformational state of membrane proteins (p < 0.05). An increase in RPP was observed immediately after exercise (p < 0.001), with a further increase 1 h postexercise (p < 0.0001). Supporting measurements of lipid peroxidation showed an increase in thiobarbituric acid reactive substances immediately after exercise (p < 0.05) and at 1 h of recovery (p < 0.001); however, free radicals were not detected. Results indicate the existence of early postexercise mild oxidative stress after single-exercise performance, which induced structural changes in erythrocyte membrane components (protein aggregation) and in the membrane organization (lipids rigidization) that followed lipid peroxidation but did not lead to cellular hemolysis.

scholarly journals The Effect of Highly Hydroxylated Fullerenol C60(OH)36on Human Erythrocyte Membrane Organization

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Jacek Grebowski ◽  
Anita Krokosz
Keyword(s):  
Membrane Proteins ◽  
Membrane Fluidity ◽  
Erythrocyte Membrane ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Erythrocyte Membranes ◽  
Resonance Spectroscopy ◽  
Protein Protein Interactions ◽  
Hydrophobic Region ◽  
Sh Groups

The mechanism of the interaction of highly hydroxylated fullerenol C60(OH)36with erythrocyte membranes was studied by electron spin resonance spectroscopy (ESR) of stearic acid derivatives labeled with a nitroxyl radical at C-12 or C-16 and with a nitroxyl derivative of maleimide covalently attached to sulfhydryl groups of membrane proteins. A significant increase in membrane fluidity in the hydrophobic region of the lipid bilayer was observed for 12-doxylstearic acid at fullerenol concentrations of 100 mg/L or 150 mg/L, while for 16-doxylstearic acid significant increase in fluidity was only observed at 150 mg/L. Fullerenol at 100 mg/L or 150 mg/L caused conformational changes in membrane proteins, expressed as an increase in thehw/hsparameter, when fullerenol was added before the maleimide spin label (MSL) to the membrane suspension. The increase of thehw/hsparameter may be caused by changes in lipid-protein or protein-protein interactions which increase the mobility of the MSL label and as a result increase the membrane fluidity. Incubation of the membranes with the MSL before the addition of fullerenol blocked the available membrane protein –SH groups and minimized the interaction of fullerenol with them. This confirms that fullerenol interacts with erythrocyte membrane proteins via available protein –SH groups.

A study of Erythrocyte Membrane Proteins and Urinary Polypeptides in Conga Drumming Haemoglobinuria

1985 ◽  
Vol 69 (1) ◽  
pp. 105-108 ◽  
Author(s):  
Richard D. Levy ◽  
Ali A. Khaleeli ◽  
Beatrice L. Griffiths ◽  
Yvonne H. Edwards
Keyword(s):  
Membrane Proteins ◽  
Carbonic Anhydrase ◽  
Erythrocyte Membrane ◽  
Acute Phase ◽  
Protein Staining ◽  
Membrane Components ◽  
Erythrocyte Membrane Proteins ◽  
Erythrocyte Carbonic Anhydrase

1. The erythrocyte membrane proteins and glycoproteins and urinary polypeptides have been examined in a patient exhibiting intermittent pigmenturia associated with conga drumming. 2. Significant excretion of haemoglobin, albumin and probably erythrocyte carbonic anhydrase but not myoglobin occurred during the acute phase of the conga drumming-induced pigmenturia. This usually ceased within 24-48 h. 3. We found no evidence of aberrant erythrocyte membrane components on electrophoresis with either protein staining or a range of 125I-labelled lectins used for detection.

The mobility and reactivity of maleimide-binding proteins in the rat erythrocyte membrane. Effects of dietary zinc deficiency and incubation with zinc in vitro

1988 ◽  
Vol 66 (1) ◽  
pp. 66-71 ◽  
Author(s):  
Stan J. Kubow ◽  
William J. Bettger
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Zinc Deficiency ◽  
Binding Proteins ◽  
Thermal Sensitivity ◽  
Erythrocyte Membranes ◽  
Resonance Spectroscopy ◽  
Dietary Zinc ◽  
Membrane Effects

Erythrocyte ghosts, prepared from rats fed zinc-deficient diets, were analyzed for the mobility of membrane proteins by electron spin resonance spectroscopy of the sulfhydryl-binding spin probe, 4-maleimido-2,2,6,6-tetramethylpiperidine-N-oxyl. Compared with erythrocyte membranes from rats fed zinc-adequate diets ad libitum or pair-fed, erythrocyte membranes from zinc-deficient rats had a significantly increased ratio of weakly immobilized to strongly immobilized probe-binding proteins. This suggests that dietary zinc deficiency causes a conformational change in erythrocyte membrane proteins. Dietary zinc deficiency did not significantly affect N-ethylmaleimide (NEM)-induced thermal sensitivity or NEM-induced mechanical fragility in rat erythrocytes; however, the addition of zinc in vitro to red cells significantly inhibits NEM-induced mechanical fragility.

Comparison of the effect of phenoxyherbicides on human erythrocyte membrane (in vitro)

Biologia ◽  
2011 ◽  
Vol 66 (2) ◽  
Author(s):  
Bożena Bukowska ◽  
Jaromir Michałowicz ◽  
Aneta Wojtaszek ◽  
Agnieszka Marczak
Keyword(s):  
Membrane Proteins ◽  
Membrane Fluidity ◽  
Erythrocyte Membrane ◽  
Molecular Mechanisms ◽  
Acute Poisoning ◽  
Human Organism ◽  
Dichlorophenoxyacetic Acid ◽  
Erythrocyte Membrane Fluidity ◽  
2,4 Dichlorophenoxyacetic Acid

AbstractThe molecular mechanisms of phenoxyherbicides action in animals have been insufficiently studied. Now, we have investigated the interaction of sodium salts of phenoxyherbicides, e.g., 2,4-dichlorophenoxyacetic acid (2,4-D-Na), 2,4,5-trichlorophenoxyacetic acid (2,4,5-T-Na) and 4-chloro-2-methylphenoxyacetic acid (MCPA-Na) with human erythrocytes. In this study, we evaluated the effect of these compounds on erythrocyte membrane fluidity as well as changes in membrane proteins content. It was observed that all of the compounds studied altered membrane fluidity, changed the size and shape of the erythrocytes and provoked echinocytes formation. It was also revealed that 2,4-D-Na and 2,4,5-T-Na changed the content of erythrocyte membrane proteins mainly by a decrease in the level of spectrin and low molecular weight proteins. The comparison of the action of phenoxyherbicides examined showed that 2,4,5-T-Na caused the greatest changes in the erythrocytes membrane, whereas MCPA-Na induced the lowest alterations in the incubated cells. It must be noted that changes of the investigated parameters were observed only at presence of significant concentrations of these compounds that may penetrate human organism only as a result of acute poisoning.

scholarly journals Erythrocyte Membrane Fluidity Alterations in Sudden Sensorineural Hearing Loss Patients: The Role of Oxidative Stress

2017 ◽  
Vol 117 (12) ◽  
pp. 2334-2345 ◽  
Author(s):  
Matteo Becatti ◽  
Rossella Marcucci ◽  
Amanda Mannucci ◽  
Anna Gori ◽  
Betti Giusti ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Hearing Loss ◽  
Sensorineural Hearing Loss ◽  
Membrane Fluidity ◽  
Erythrocyte Membrane ◽  
Blood Viscosity ◽  
Erythrocyte Deformability ◽  
Sudden Sensorineural Hearing Loss ◽  
Erythrocyte Membrane Fluidity

Introduction Sudden sensorineural hearing loss (SSNHL) involves an acute unexplained hearing loss, nearly always unilateral, that occurs over less than a 72-hour period. SSNHL pathogenesis is not yet fully understood. Cochlear vascular occlusion has been proposed as a potential mechanism of hearing damage and cochlear ischaemia has been related to alterations of cochlear microvessels. In addition, some researchers have focused their attention on the rheological alterations and blood hyperviscosity. Erythrocyte deformability plays a key role in determining blood viscosity, and it is critical to cochlear perfusion. It has been shown that oxidative stress-induced erythrocyte membrane fluidity alterations are linked to the progression of cardiovascular diseases. Methods To determine whether erythrocytes from SSNHL patients show signs of oxidative stress, and whether this condition can modify the haemorheologic profile in these patients, we analysed haemorheologic profile and erythrocyte oxidative stress in 35 SSNHL patients and 35 healthy subjects, matched for age and sex. Fluorescence anisotropy was used to evaluate the fluidity of erythrocyte membranes. Results Our results show a significant structural and functional involvement of erythrocyte membrane alterations in SSNHL, as well as elevated levels of membrane lipid peroxidation and intracellular reactive oxygen species (ROS) production. In addition, erythrocyte-derived ROS and erythrocyte lipid peroxidation positively correlated with whole blood viscosity and erythrocyte deformability. Moreover, in vitro experiments demonstrated that ROS display a key role in erythrocyte membrane fluidity. Conclusion These findings indicate that erythrocyte oxidative stress plays a key role in the pathogenesis of SSNHL and pave the way to new therapeutic interventions.

Trans-resveratrol supplement lowers lipid peroxidation responses of exercise in male Wistar rats

2020 ◽  
pp. 1-6 ◽  
Author(s):  
Masoud Nasiri ◽  
Saja Ahmadizad ◽  
Mehdi Hedayati ◽  
Tayebe Zarekar ◽  
Mehdi Seydyousefi ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Antioxidant Capacity ◽  
Total Antioxidant Capacity ◽  
Wistar Rats ◽  
Enzymatic Antioxidants ◽  
Acute Response ◽  
Total Antioxidant ◽  
Male Wistar Rats ◽  
Exercise Induced ◽  
And Control

Abstract. Physical exercise increases free radicals production; antioxidant supplementation may improve the muscle fiber’s ability to scavenge ROS and protect muscles against exercise-induced oxidative damage. This study was designed to examine the effects of all-trans resveratrol supplementation as an antioxidant to mediate anti-oxidation and lipid per-oxidation responses to exercise in male Wistar rats. Sixty-four male Wistar rats were randomly divided into four equal number (n = 16) including training + supplement (TS), training (T), supplement (S) and control (C) group. The rats in TS and S groups received a dose of 10 mg/kg resveratrol per day via gavage. The training groups ran on a rodent treadmill 5 times per week at the speed of 10 m/min for 10 min; the speed gradually increased to 30 m/min for 60 minutes at the end of 12th week. The acute phase of exercise protocol included a speed of 25 m/min set to an inclination of 10° to the exhaustion point. Superoxide dismutase (SOD), glutathione peroxidase (GPx), catalase (CAT) activity, non-enzymatic antioxidants bilirubin, uric acid, lipid peroxidation levels (MDA) and the total antioxidant capacity (TAC) were measured after the exercise termination. The data were analyzed by using one-way ANOVA. The result showed that endurance training caused a significant increase in MDA level [4.5 ± 0.75 (C group) vs. 5.9 ± 0.41 nmol/l (T group)] whereas it decreased the total antioxidant capacity [8.5 ± 1.35 (C group) vs. 7.1 ± 0.55 mmol/l (T group)] (p = 0.001). In addition, GPx and CAT decreased but not significantly (p > 0.05). The training and t-resveratrol supplementation had no significant effect on the acute response of all variables except MDA [4.3 ± 1.4 (C group) vs. 4.0 ± 0.90 nmol/l (TS group)] (p = 0.001) and TAC [8.5 ± 0.90 (C group) vs. 6.6 ± 0.80 mmol/l (TS group)] (p = 0.004). It was concluded that resveratrol supplementation may prevent exercise-induced oxidative stress by preventing lipid peroxidation.

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