scholarly journals Regulatory role of peroxinitrite (ONOO-) for oxidative damage to human Red Blood Cells (hRBC)

2015 ◽  
Keyword(s):  
Oxidative Damage ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Regulatory Role ◽  
Human Red Blood Cells

Carboxylated nanodiamonds inhibit γ-irradiation damage of human red blood cells

Nanoscale ◽  
2016 ◽  
Vol 8 (13) ◽  
pp. 7189-7196 ◽  
Author(s):  
K. Santacruz-Gomez ◽  
E. Silva-Campa ◽  
R. Melendrez-Amavizca ◽  
F. Teran Arce ◽  
V. Mata-Haro ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Biological Systems ◽  
Reducing Agents ◽  
Irradiation Damage ◽  
Γ Irradiation ◽  
Human Red Blood Cells

Nanodiamonds when carboxylated (cNDs) act as reducing agents and hence could limit oxidative damage in biological systems.

Honey flavonoids as protection agents against oxidative damage to human red blood cells

2007 ◽  
Vol 104 (4) ◽  
pp. 1635-1640 ◽  
Author(s):  
M BLASA ◽  
M CANDIRACCI ◽  
A ACCORSI ◽  
M PIACENTINI ◽  
E PIATTI
Keyword(s):  
Oxidative Damage ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells

scholarly journals Detection of acyl-CoA-binding protein in human red blood cells and investigation of its role in membrane phospholipid renewal

1995 ◽  
Vol 306 (3) ◽  
pp. 793-799 ◽  
Author(s):  
H Fyrst ◽  
J Knudsen ◽  
M A Schott ◽  
B H Lubin ◽  
F A Kuypers
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Liver ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Human Red Blood Cells ◽  
Low Concentrations ◽  
Membrane Bound ◽  
High Concentrations

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.

scholarly journals Investigations on the role of hemoglobin in sulfide metabolism by intact human red blood cells

2018 ◽  
Vol 149 ◽  
pp. 163-173 ◽  
Author(s):  
Christopher L. Bianco ◽  
Anton Savitsky ◽  
Martin Feelisch ◽  
Miriam M. Cortese-Krott
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells
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