TY - JOUR
TI - Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells
AU - Kriebardis, A.G.
AU - Antonelou, M.H.
AU - Stamoulis, K.E.
AU - Economou-Petersen, E.
AU - Margaritis, L.H.
AU - Papassideri, I.S.
JO - Journal of Cellular and Molecular Medicine
PY - 2007
VL - 11
TODO - 1
SP - 148-155
PB - 
SN - 1582-1838, 1582-4934
TODO - 10.1111/j.1582-4934.2007.00008.x
TODO - adenine;  citric acid;  CPDA solutions;  cryoprotective agent;  cytoskeleton protein;  glucose;  hemoglobin;  hypotonic solution;  phosphate;  unclassified drug, article;  blood donor;  blood storage;  drug effect;  electrophoresis;  erythrocyte;  erythrocyte membrane;  human;  immunoblotting;  metabolism;  oxidation reduction reaction;  physiology;  protein carbonylation, Adenine;  Blood Donors;  Blood Preservation;  Citrates;  Cryoprotective Agents;  Cytoskeletal Proteins;  Electrophoresis;  Erythrocyte Membrane;  Erythrocytes;  Glucose;  Hemoglobins;  Humans;  Hypotonic Solutions;  Immunoblotting;  Oxidation-Reduction;  Phosphates;  Protein Carbonylation
TODO - Red blood cell (RBC) membrane proteins undergo progressive pathological alterations during storage. In conditions of increased cellular stress, the cytoskeleton also sustains certain modifications. The hemoglobin (Hb) content and oxidative status of the RBC cytoskeletons as a function of the storage period remain unclear. The possible Hb content and oxidative alterations occurring in the cytoskeletons in the course of storage were monitored in six unite, by means of electrophoresis, immunoblotting and protein carbonylation assays. A proportion of the ghost-bound Hb consists of non-reducible crosslinkings of probably oxidized/denatured Hb or hemichromes. The defective Hb-membrane association was strongly affected by the prolonged storage. A progressive accumulation of Hb monomers, multimers and high molecular weight aggregates to the corresponding cytoskeletons were also evident. The oxidative index of the cytoskeletal proteins was found increased, signalizing oxidative modifications in spectrin and possibly other cytoskeletal proteins. The reported data corroborate the evidence for oxidative damage in membrane proteins with emphasis to the eytoskeletal components. They partially address the pathophysiological mechanisms underlying the RBC storage lesion, add some new insight in the field of RBC storage as a hemoglobin- and cytoskeleton-associated pathology and suggest the possible use of antioxidante in the unite intended for transfusion. © 2007 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd.
ER -