Whole blood storage in CPDA1 blood bags alters erythrocyte membrane proteome

Al-Thani, A. M., Voss, S. C., Al-Menhali, A. S., Barcaru, A., Horvatovich, P., Al Jaber, H., Nikolovski, Z., Latiff, A., Georgakopoulos, C., Merenkov, Z., Segura, J., Alsayrafi, M. & Jaganjac, M., 1-Dec-2018, In : Oxidative Medicine and Cellular Longevity. 2018

Research output: Contribution to journalArticleAcademicpeer-review

  • Amna Mohamed Al-Thani
  • Sven Christian Voss
  • Afnan Saleh Al-Menhali
  • Andrei Barcaru
  • Peter Horvatovich
  • Hind Al Jaber
  • Zoran Nikolovski
  • Aishah Latiff
  • Costas Georgakopoulos
  • Zeyd Merenkov
  • Jordi Segura
  • Mohammed Alsayrafi
  • Morana Jaganjac
Autologous blood transfusion (ABT) has been frequently abused in endurance sport and is prohibited since the mid-1980s by the International Olympic Committee. Apart from any significant performance-enhancing effects, the ABT may pose a serious health issue due to aging erythrocyte-derived "red cell storage lesions." The current study investigated the effect of blood storage in citrate phosphate dextrose adenine (CPDA1) on the red blood cell (RBC) membrane proteome. One unit of blood was collected in CPDA1 blood bags from 6 healthy female volunteers. RBC membrane protein samples were prepared on days 0, 14, and 35 of storage. Proteins were digested in gel and peptides separated by nanoliquid chromatography coupled to tandem mass spectrometry resulting in the confident identification of 33 proteins that quantitatively change during storage. Comparative proteomics suggested storage-induced translocation of cytoplasmic proteins to the membrane while redox proteomics analysis identified 14 proteins prone to storage-induced oxidation. The affected proteins are implicated in the RBC energy metabolism and membrane vesiculation and could contribute to the adverse posttransfusion outcomes. Spectrin alpha chain, band 3 protein, glyceraldehyde-3-phosphate dehydrogenase, and ankyrin-1 were the main proteins affected by storage. Although potential biomarkers of stored RBCs were identified, the stability and lifetime of these markers posttransfusion remain unknown. In summary, the study demonstrated the importance of studying storage-induced alterations in the erythrocyte membrane proteome and the need to understand the clearance kinetics of transfused erythrocytes and identified protein markers.
Original languageEnglish
JournalOxidative Medicine and Cellular Longevity
Publication statusPublished - 1-Dec-2018


  • adult, alpha chain, article, blood autotransfusion, blood bag, cell energy, chromatography, clearance, clinical article, controlled study, energy metabolism, erythrocyte lifespan, erythrocyte membrane, erythrocyte preservation, female, human, human cell, human experiment, kinetics, oxidation reduction reaction, proteomics, tandem mass spectrometry, volunteer, ankyrin, biological marker, cell membrane protein, cytoplasm protein, endogenous compound, erythrocyte band 3 protein, glyceraldehyde 3 phosphate dehydrogenase, proteome, spectrin

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