scholarly journals Reducing Compounds Roles in Oxidative Stress Relieving of Human Red Blood Cells

2021 ◽  
Author(s):  
Giuseppe Gallo

Oxidative stress is the consequence of an imbalance between pro-oxidant and antioxidant processes. Antioxidants that counteract reactive oxygen species do not all work the same way. Both resveratrol and the more powerful 4-hydroxytyrosol are excellent reducing agents. Polyphenol treatment (red wine polyphenols, resveratrol and catechin) is associated with a significant increase in anion permeability for chloride compared with control and 2.2′-azobis-2 amidinopropan dihydrochloride affected cells. Treatment with polyphenols was associated with a significant reduction in mean ± standard error of the mean membrane lipid peroxidation compared with control and 2.2′-azobis-2 amidinopropan dihydrochloride treatment. Hemolysis data are also obtained in the previously described conditions. 4-hydroxytyrosol is shown to significantly protect red blood cells from oxidative damage by 4-hydroxynonenal. But there are paradoxical effects like uric acid and creatinine. The obtained data evidence that both creatinine and uric acid levels have influence on the ratio of both malondialdehyde/protein and 4-hydroxynonenal/protein content on red blood cell ghosts, demonstrating their possible protective role against oxidative stress at low concentrations in blood and oxidizing power at higher concentrations. Finally, polyunsaturated fatty acids do not have all this reducing power.

2019 ◽  
Vol 32 (6) ◽  
pp. 1096-1102 ◽  
Author(s):  
Daniela Giustarini ◽  
Isabella Dalle-Donne ◽  
Aldo Milzani ◽  
Daniela Braconi ◽  
Annalisa Santucci ◽  
...  

1984 ◽  
Vol 247 (3) ◽  
pp. C143-C149 ◽  
Author(s):  
G. A. Plishker

Cadmium and zinc increased the accumulation of calcium in human red blood cells by increasing passive influx without enhancing the permeability to other ions. The effect of cadmium and zinc appeared specific to these metals, because barium, magnesium, cobalt, strontium, manganese, and nickel had no effect. Changes in calcium uptake by extracellular sodium, potassium, and pH were not altered by zinc and cadmium. Inhibition of calcium uptake by quinine, oligomycin, and iodoacetate was not affected by cadmium or zinc. These results suggest that cadmium and zinc increase calcium movement through normal influx pathways. Cadmium and zinc acted synergistically apparently by different mechanisms. Zinc and cadmium differentially affected calcium uptake in different extracellular calcium concentrations. The cadmium effect was increased by low concentrations of 2-mercaptoethanol and above pH 8.0, while the zinc effect was less sensitive to these factors. These findings suggest that the cadmium effect involves a disulfide bond between cysteinyl residues and the zinc effect involves a different site.


1999 ◽  
Vol 6 (2) ◽  
pp. 103-110 ◽  
Author(s):  
Iwona Cicha ◽  
Yoji Suzuki ◽  
Norihiko Tateishi ◽  
Nobuji Maeda

1995 ◽  
Vol 306 (3) ◽  
pp. 793-799 ◽  
Author(s):  
H Fyrst ◽  
J Knudsen ◽  
M A Schott ◽  
B H Lubin ◽  
F A Kuypers

Acyl-CoA-binding protein (ACBP) has been identified in a number of tissues and shown to affect the intracellular distribution and utilization of acyl-CoA. We have detected ACBP in the cytosol but not the membrane of human red blood cells and, using an e.l.i.s.a. with antibodies prepared against human liver ACBP, found that its concentration was 0.5 microM. To investigate the role of ACBP in human red blood cells, we added purified human liver ACBP and radiolabelled acyl-CoA to isolated membranes from these cells. ACBP prevented high concentrations of acyl-CoA from binding to the membrane but could not keep the acyl-CoA in the aqueous phase at low concentrations. This suggested the presence of a pool in the membrane with a binding affinity for acyl-CoA that was greater than that of ACBP for acyl-CoA. In the presence of lysophospholipid, this membrane-bound pool of acyl-CoA was rapidly used as a substrate by acyl-CoA:lysophospholipid acyltransferase (LAT) to generate phospholipid from lysophospholipid. We also found that ACBP-bound acyl-CoA was preferred over free acyl-CoA as a substrate by LAT. These results are the first documentation that human red blood cells contain ACBP and that this protein can affect the utilization of acyl-CoA in plasma membranes of these cells. The interactions between acyl-CoA, ACBP and the membrane suggest that there are several pools of acyl-CoA in the human red blood cell and that ACBP may have a role in regulating their distribution and fate.


Transfusion ◽  
2018 ◽  
Vol 58 (12) ◽  
pp. 2978-2991 ◽  
Author(s):  
Julie A. Reisz ◽  
Travis Nemkov ◽  
Monika Dzieciatkowska ◽  
Rachel Culp-Hill ◽  
Davide Stefanoni ◽  
...  

RSC Advances ◽  
2016 ◽  
Vol 6 (58) ◽  
pp. 53195-53202 ◽  
Author(s):  
Pawan Kumar Maurya ◽  
Prabhanshu Kumar ◽  
Shirisha Nagotu ◽  
Subhash Chand ◽  
Pranjal Chandra

Quercetin and myricetin help against oxidative stress in human red blood cells during aging, thereby has tremendous scope in medical diagnostics and therapeutics.


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