Molecular defect in the membrane skeleton of blood bank-stored red cells. Abnormal spectrin-protein 4.1-actin complex formation.

During liquid preservation under blood bank conditions, red cell membranes inexorably undergo damage that decreases erythrocyte survival after transfusion. Accordingly, we have surveyed membrane skeletal protein interactions during storage. We uncovered a decrease in the in vitro formation of spectrin-actin complex in the absence (50%) or presence (60%) of protein 4.1. Actual formation of the spectrin-actin-protein 4.1 complex fell in a linear fashion during the storage period. This fall in spectrin-actin interaction tightly correlated with the decline in total red cell phospholipid (R = 0.9932) measured simultaneously. This decrement of spectrin-actin association could be restored to greater than 70% of normal values by preincubation of stored spectrin with 50 mM dithiothreitol. This storage injury to spectrin-actin interaction might weaken the membrane skeleton and lead to decreased red cell survival. In vitro reversibility of the damage by reducing agents suggests a possible new direction for prolonging the shelf life of stored blood.