Studies of the antioxidant and antihemolytic activity of quinoline derivatives in a model of oxidative damage to erythrocyte membranes

2009 ◽  
Vol 43 (1) ◽  
pp. 7-10 ◽  
Author(s):  
M. G. Malakyan ◽  
S. A. Badzhinyan ◽  
L. A. Vardevanyan ◽  
D. S. Grigoryan ◽  
D. É. Egiazaryan ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Erythrocyte Membranes ◽  
Quinoline Derivatives ◽  
Antihemolytic Activity

Reduced susceptibility to oxidative damage of erythrocyte membranes from medicated schizophrenic patients

1996 ◽  
Vol 55 (1-2) ◽  
pp. 27-31 ◽  
Author(s):  
C.N. Ramchand ◽  
J.I. Davies ◽  
R.L. Tresman ◽  
I.C.D. Griffiths ◽  
M. Peet
Keyword(s):  
Oxidative Damage ◽  
Erythrocyte Membranes ◽  
Schizophrenic Patients

scholarly journals Impact of membranetropic compounds on the sensitivity of mammalian erythrocytes to the posthypertonic shock action

2020 ◽  
pp. 31-38
Author(s):  
O Chabanenko ◽  
◽  
N Yershova ◽  
N Orlova ◽  
N Shpakova ◽  
...  
Keyword(s):  
Critical Micelle Concentration ◽  
Defect Formation ◽  
Phospholipid Composition ◽  
Erythrocyte Membranes ◽  
Minimum Level ◽  
Rat Erythrocytes ◽  
Amphiphilic Compounds ◽  
Antihemolytic Activity ◽  
Mammalian Erythrocyte ◽  
Shock Action

The effect of cationic trifluoperazine (TFP) and nonionic decyl-β,D-glucopyranoside (DGP) on the sensitivity of human, rabbit and rat erythrocytes to the action of posthypertonic shock (PHS) at 0 °C was studied in this research. Trifluoperazine shows a high antihemolytic activity under conditions of PHS of human and animal erythrocytes at slight differences of values of effective concentrations. The value of antihemolytic activity of TFP for human and rabbit erythrocytes is ~ 60 %, and for rat cells the efficiency of this compound is approximately 1.4 times higher. The values of antihemolytic activity of DGP under PHS conditions of human and rat erythrocytes are comparable and amounts to 62 and 66 %, respectively. Significant differen­ces of this parameter (72 %) were found for rabbit cells compared with human erythrocytes. It was found that the size of plateau (the range of concentrations of amphiphilic compounds within the minimum level of erythrocyte hemolysis was observed) cationic TFP and nonionic DGP are significantly different. Thus, TFP has a narrow plateau (100–200 μmol/L), while DGP has a rather wide one (400–1600 μmol/L). In addition, a shift of the plateau concentrations of DGP to the region of higher values compared with TFP is observed, which is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP. Moreover, a shift of plateau concentrations of DGP to the region of higher values compared with TFP is observed, that is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP one. It was established that under PHS conditions of human erythrocyte, both compounds (TFP and DGP) show a commensurate antihemolytic activity. At the same time, for rabbit cells, DGP is more effective compared with TFP, and for rat erythrocytes, on the contrary, the efficiency of TFP is higher than DGP. This may be due to differences in the phospholipid composition of mammalian erythrocyte membranes. The results suggest that under PHS conditions the efficacy of membrane-tropic compounds is most likely due to their ability to incorporate into membrane to the defect formation areas, and thus significantly increase the critical hemolytic volume of cells, as a result, prevent their destruction.

Phenolics from monofloral honeys protect human erythrocyte membranes against oxidative damage

2012 ◽  
Vol 50 (5) ◽  
pp. 1508-1516 ◽  
Author(s):  
José M. Alvarez-Suarez ◽  
Francesca Giampieri ◽  
Ana M. González-Paramás ◽  
Elisabetta Damiani ◽  
Paola Astolfi ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

The oxidative damage of butenolide to isolated erythrocyte membranes

2007 ◽  
Vol 21 (5) ◽  
pp. 863-869 ◽  
Author(s):  
Yi-Mei Wang ◽  
Shuang-Qing Peng ◽  
Qi Zhou ◽  
Min-Wei Wang ◽  
Chang-Hui Yan ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Erythrocyte Membranes

scholarly journals Interaction of Catechins with Human Erythrocytes

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1456
Author(s):  
Katarzyna Naparlo ◽  
Grzegorz Bartosz ◽  
Ireneusz Stefaniuk ◽  
Bogumil Cieniek ◽  
Miroslaw Soszynski ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Oxidative Damage ◽  
Stearic Acid ◽  
Erythrocyte Membrane ◽  
Membrane Lipid ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Spin Labels ◽  
Protective Effects ◽  
Protein Thiol

The aim of this study was to characterize the interaction of chosen catechins ((+)-catechin, (−)-epigallocatechin (EGC), and (−)-epigallocatechin gallate (EGCG)) with human erythrocytes and their protective effects against oxidative damage of erythrocytes. Uptake of the catechins by erythrocytes was studied by fluorimetry, their interaction with erythrocyte membrane was probed by changes in erythrocyte osmotic fragility and in membrane fluidity evaluated with spin labels, while protection against oxidative damage was assessed by protection against hemolysis induced by permanganate and protection of erythrocyte membranes against lipid peroxidation and protein thiol group oxidation. Catechin uptake was similar for all the compounds studied. Accumulation of catechins in the erythrocyte membrane was demonstrated by the catechin-induced increase in osmotic resistance and rigidification of the erythrocyte membrane detected by spin labels 5-doxyl stearic acid and 16-doxyl stearic acid. (−)-Epigallocatechin and EGCG inhibited erythrocyte acetylcholinesterase (mixed-type inhibition). Catechins protected erythrocytes against permanganate-induced hemolysis, oxidation of erythrocyte protein thiol groups, as well as membrane lipid peroxidation. These results contribute to the knowledge of the beneficial effects of catechins present in plant-derived food and beverages.

Oxidative damage in rat erythrocyte membranes following ethanol intake: Effect of ethyl pyruvate

2007 ◽  
Vol 169 (2) ◽  
pp. 122-131 ◽  
Author(s):  
Rosita Gabbianelli ◽  
Carlo Cifani ◽  
Maurizio Massi ◽  
Carlo Polidori ◽  
Giancarlo Falcioni
Keyword(s):  
Oxidative Damage ◽  
Ethyl Pyruvate ◽  
Ethanol Intake ◽  
Erythrocyte Membranes

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Effect of Integral Proteins on Frozen Membrane Fracture

1980 ◽  
Vol 38 ◽  
pp. 756-759 ◽  
Author(s):  
S. Kirchanski ◽  
D. Branton
Keyword(s):  
Lipid Bilayers ◽  
Freeze Fracture ◽  
Covalent Bond ◽  
Erythrocyte Membranes ◽  
Glycophorin A ◽  
Experimental Protocol ◽  
Transmembrane Glycoprotein ◽  
Bond Breakage ◽  
Human Erythrocyte Membranes ◽  
Integral Proteins

We have investigated the effect of integral membrane proteins upon the fracturing of frozen lipid bilayers. This investigation has been part of an effort to develop freeze fracture labeling techniques and to assess the possible breakage of covalent protein bonds during the freeze fracture process. We have developed an experimental protocol utilizing lectin affinity columns which should detect small amounts of covalent bond breakage during the fracture of liposomes containing purified (1) glycophorin (a transmembrane glycoprotein of human erythrocyte membranes). To fracture liposomes in bulk, frozen liposomes are ground repeatedly under liquid nitrogen. Failure to detect any significant covalent bond breakage (contrary to (2)) led us to question the effectiveness of our grinding procedure in fracturing and splitting lipid bilayers.

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