Changes in red blood cell membrane structure in patients with chronic renal failure.
The properties of red blood cell membranes in patients with chronic renal failure were investigated using electron paramagnetic resonance spectroscopy. Using spin traps, 5,5-dimethylpirroline-1 oxide and N-tert-butyl-alpha-phenylnitrone, we found generation of hydroxyl radicals in the blood of patients with chronic renal failure after 20 min of regular hemodialysis. The physical state of membrane proteins and membrane osmotic fragility and reductive properties of red blood cells were studied. The increase in the relative correlation time of 4-(2-iodoacetamido)-2,2,6,6-tetramethylpiperidine-1 oxyl indicates the immobilization of membrane protein molecules in erythrocytes of chronic renal failure patients. The decrease in membrane protein mobility was observed in whole blood incubated with tert-butylhydroperoxide, regardless of the presence of iron. We found that the addition of ferrous ions did not aggravate profound changes in membrane proteins induced with tert-butylhydroperoxide. We also demonstrated higher osmotic fragility of erythrocytes in the patients with renal failure as compared to normal subjects. These alterations in membrane structure of red blood cells in hemodialysed patients suggest that hydroxyl radicals generated during hemodialysis can play an important role in the oxidative mechanism of erythrocyte damage.
Gwoździński
K
K
Department of Molecular Biophysics, University of Lódź, Poland. kgwodz@biol.uni.lodz.pl
Janicka
M
M
Brzeszczyńska
J
J
Luciak
M
M
D004578:Electron Spin Resonance Spectroscopy; D004910:Erythrocyte Membrane / Q000737:chemistry* / Q000378:metabolism* / Q000473:pathology; D004912:Erythrocytes / Q000378:metabolism / Q000648:ultrastructure*; D006801:Humans; D007676:Kidney Failure, Chronic / Q000097:blood / Q000473:pathology*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D009994:Osmolar Concentration
D008565:Membrane Proteins