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Iron release, membrane protein oxidation and erythrocyte ageing
Author(s) -
Signorini C.,
Ferrali M.,
Ciccoli L.,
Sugherini L.,
Magnani A.,
Comporti M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00235-2
Subject(s) - incubation , methemoglobin , chemistry , ageing , anaerobic exercise , membrane , intracellular , biochemistry , in vitro , erythrocyte membrane , hemoglobin , biology , physiology , genetics
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.