Storage conditions determine the characteristics of red blood cell derived extracellular vesicles

February 1, 2022

Title

Storage conditions determine the characteristics of red blood cell derived extracellular vesicles

Author

Tímea Bebesi, Diána Kitka, Anikó Gaál, Imola Csilla Szigyártó, Róbert Deák, Tamás Beke-Somfai, Kitti Koprivanacz, Tünde Juhász, Attila Bóta, Zoltán Varga & Judith Mihály

Year

2022

Journal

Scientific Reports

Abstract

Extracellular vesicles (EVs) are released during the storage of red blood cell (RBC) concentrates and might play adverse or beneficial roles throughout the utilization of blood products (transfusion). Knowledge of EV release associated factors and mechanism amends blood product management. In the present work the impact of storage time and medium (blood preserving additive vs isotonic phosphate buffer) on the composition, size, and concentration of EVs was studied using attenuated total reflection infrared (ATR-IR) spectroscopy, microfluidic resistive pulse sensing (MRPS) and freeze-fraction combined transmission electron micrography (FF-TEM). The spectroscopic protein-to-lipid ratio based on amide and the C–H stretching band intensity ratio indicated the formation of various vesicle subpopulations depending on storage conditions. After short storage, nanoparticles with high relative protein content were detected. Spectral analysis also suggested differences in lipid and protein composition, too. The fingerprint region (from 1300 to 1000 cm−1) of the IR spectra furnishes additional information about the biomolecular composition of RBC-derived EVs (REVs) such as adenosine triphosphate (ATP), lactose, glucose, and oxidized hemoglobin. The difference between the vesicle subpopulations reveals the complexity of the REV formation mechanism. IR spectroscopy, as a quick, cost-effective, and label-free technique provides valuable novel biochemical insight and might be used complementary to traditional omics approaches on EVs.

Instrument

LC-2000

Keywords

Evs, blood cell, lipid, proteins