Iron release, membrane protein oxidation and erythrocyte ageing

The aerobic incubation of erythrocytes in phosphate buffer for 24–60 h (a model of rapid in vitro ageing) induced progressive iron release and methemoglobin formation. Membrane proteins showed electrophoretic alterations and increase in carbonyl groups (as documented by IR spectroscopy). None of the...

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Bibliographic Details
Published in:FEBS letters 1995-04, Vol.362 (2), p.165-170
Main Authors: Signorini, C., Ferrali, M., Ciccoli, L., Sugherini, L., Magnani, A., Comporti, M.
Format: Article
Language:English
Subjects:
Animals
Buffers
Cattle
Erythrocyte
Erythrocyte Aging
Erythrocytes - drug effects
Erythrocytes - metabolism
Ferrozine - pharmacology
Humans
Immunoglobulin G - blood
Iron - blood
Iron chelation
Iron release
Membrane Proteins - blood
Methemoglobin - metabolism
Oxidation-Reduction
Oxygen - administration & dosage
Phosphates
Protein oxidation
Senescent cell antigen
Spectrophotometry, Infrared
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Summary:The aerobic incubation of erythrocytes in phosphate buffer for 24–60 h (a model of rapid in vitro ageing) induced progressive iron release and methemoglobin formation. Membrane proteins showed electrophoretic alterations and increase in carbonyl groups (as documented by IR spectroscopy). None of these phenomena were seen when the erythrocytes were incubated under anaerobic conditions. The membranes from aerobically incubated cells bound a much higher amount of autologous IgG than those from anaerobically incubated ones, suggesting that the aerobic incubation gives rise to the senescent antigen. The addition of ferrozine during the aerobic incubation prevented both the IgG binding and the protein alterations seen in the IR spectra, suggesting an intracellular chelation of the released iron by ferrozine.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00235-2