title: The proteome of red cell membranes and vesicles during storage in blood bank conditions.
abstract: BACKGROUND
  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.
  
  
  METHODS
  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.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Biochemistry, the Center for Molecular and Biomolecular Informatics, Nijmegen Center of Molecular Life Sciences, Radboud University Nijmegen Medical Center, Nijmegen, The Netherlands. g.bosman@ncmls.ru.nl
authors.forename: Giel J C G M
authors.initials: GJ
authors.lastname: Bosman
authors.forename: Edwin
authors.initials: E
authors.lastname: Lasonder
authors.forename: Marleen
authors.initials: M
authors.lastname: Luten
authors.forename: Bregt
authors.initials: B
authors.lastname: Roerdinkholder-Stoelwinder
authors.forename: Vera M J
authors.initials: VM
authors.lastname: Novotný
authors.forename: Harry
authors.initials: H
authors.lastname: Bos
authors.forename: Willem J
authors.initials: WJ
authors.lastname: De Grip
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D000094902:Blood Banking / Q000379:methods*; D001793:Blood Preservation; D002470:Cell Survival / Q000502:physiology; D016922:Cellular Senescence / Q000502:physiology; D002853:Chromatography, Liquid; D022162:Cytoplasmic Vesicles / Q000378:metabolism*; D030562:Databases, Protein; D004798:Enzymes / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000166:cytology / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry; D018832:Molecular Chaperones / Q000378:metabolism; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D004798:Enzymes; D018832:Molecular Chaperones; D020543:Proteome; D019204:GTP-Binding Proteins