Oxidative Stress Induced Carbonyl Group Incorporation to Human RBC Membrane: Role in Vivo Senescence of Erythrocyte
Keywords:
human RBC membrane, protein carbonylation, oxidative membrane damage, senescence of RBC, oxygen free radical, ROS, autoantibody to RBC
Abstract
This study was focused to identify the link between oxidative stress and senescence of erythrocytes in vivo. To elucidate this mechanism, various modification of RBC membrane proteins and lipids were analyzed invitro, exposing them to oxidative stress and the results were compared with the changes observed in erythrocytes undergoing senescence in vivo. The other objective was to confirm the mechanism of autoantibody mediated removal of aged RBCs. Our results established that increased lipid peroxidation products, followed by the enhanced damage of RBC membrane protein caused increased RBC membrane protein carbonylation, to normal red cells exposed to the in vitro Fe2+ & ascorbate induced oxidative stress. It was presumable that these changes were mediated by hydroxyl (ȮH) radicals. Further, similar changes were also seen in percoll gradient age fractionated high density aged RBCs. Both in vitro oxidative stress & in vivo studies with high density red cells showed no changes in membrane protein thiol oxidation and protein cross-linking. It was presumable that the enhanced bound IgGs to the red cells represented auto antibodies directed against carbonylated proteins of RBC membranes playing a central role in the senescence of RBCs followed by in vivo removal of such antibody coated RBCs from the circulation.
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