The proteome of red cell membranes and vesicles during storage in blood bank conditions

• Published in: Transfusion (Philadelphia, Pa.) Pa.), 2008-05, Vol.48 (5), p.827-835
• Main Authors: BOSMAN, Giel J. C. G. M, LASONDER, Edwin, LUTEN, Marleen, ROERDINKHOLDER-STOELWINDER, Bregt, NOVOTNY, Vera M. J, BOS, Harry, DE GRIP, Willem J
• Format: Article
• Language: English
• Subjects: Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy; Anion Exchange Protein 1, Erythrocyte - metabolism; Biological and medical sciences; Blood Banking - methods; Blood Preservation; Blood. Blood and plasma substitutes. Blood products. Blood cells. Blood typing. Plasmapheresis. Apheresis; Bone marrow, stem cells transplantation. Graft versus host reaction; Cell Survival - physiology; Cellular Senescence - physiology; Chromatography, Liquid; Cytoplasmic Vesicles - metabolism; Databases, Protein; Enzymes - metabolism; Erythrocyte Membrane - metabolism; Erythrocytes - cytology; Erythrocytes - metabolism; GTP-Binding Proteins - metabolism; Humans; Mass Spectrometry; Medical sciences; Molecular Chaperones - metabolism; Proteome; Proteomics - methods; Signal Transduction - physiology; Transfusions. Complications. Transfusion reactions. Cell and gene therapy
• ISSN: 0041-1132; 1537-2995
• DOI: 10.1111/j.1537-2995.2007.01630.x

During storage of red cells (RBCs) for transfusion, RBCs undergo a number of biochemical and morphologic changes. To be able to identify the mechanisms underlying these storage lesions, a proteomic analysis of the membranes of RBCs and their vesicles was performed during various periods of storage in blood bank conditions. RBCs and vesicles were isolated from RBCs after various storage periods. The proteins of RBC membranes and vesicles were separated by gel electrophoresis and identified by a semiquantitative proteomic analysis. Our findings confirm previous data, such as a storage-associated increase in hemoglobin binding to the membrane and aggregation and degradation of the integral membrane protein band 3, suggesting a remodeling of the RBC membrane during storage. Our data also show storage-dependent changes in the membrane association of proteasome and chaperone proteins, metabolic enzymes, small G proteins, and signal transduction proteins. Vesicles display similar changes in their protein composition during storage. The results of this analysis indicate that the storage-related changes in the RBC membrane are the results of disturbance and/or acceleration of physiologic processes such as cellular aging, including vesicle formation. The latter may serve to remove damaged membrane patches that would otherwise lead to accelerated RBC removal. These data provide a framework for future studies toward the development of better storage conditions and a reduction of the side effects of RBC transfusion.