Metabolism Reactivation in Erythrocytes Cryopreserved with Polyethylene Glycol: Protein State and Reactive Oxygen Species Production
DOI:
https://doi.org/10.15407/cryo32.02.092Keywords:
erythrocyte, membrane, cytoskeleton, protein, reactive oxygen species, cryoprotectant, cryopreservation, polyethylene glycolAbstract
Production of reactive oxygen species (ROS) and protein state of membrane-cytoskeleton complex (MCC) in the erythrocytes, subjected to freeze-thawing with polyethylene glycol (PEG) and subsequently transferred into physiological conditions in vitro after cryoprotective agent removal were examined. Results of SDS-PAGE with β-mercaptoethanol showed a decrease in spectrin content in the MCC profile of cryopreserved erythrocytes. The using of diamide revealed an increase in the accessibility of –SH groups of spectrin for the reagent and an enhanced level of high molecular weight polypeptide complexes relative to the control. A decrease in the content of protein band 8 (peroxiredoxin) in the MCC of cryopreserved erythrocytes revealed by SDS-PAGE with β-mercaptoethanol is apparently associated with a change in its localization caused by an increased ROS production at the previous stages of cryopreservation. At the same time, the absence of significant changes in the ROS production relative to the control upon the metabolism reactivation in erythrocytes indicated the ability of cryopreserved cells to control the oxidative processes during short-term incubation.
Probl Cryobiol Cryomed 2022; 32(2):092–103
References
An X, Gauthier E, Zhang X, et al. Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin. Blood. 2008; 112(13): 5212-8. CrossRef
An X, Guo X, Zhang X, et al. Conformational stabilities of the structural repeats of erythroid spectrin and their functional implications. J Biol Chem. 2006; 281(15): 10527-32. CrossRef
Babijchuk LA, Zemlianskykh NG. Optimization and advantages of washing-out method of erythrocyte cryopreservation with PEO-1500. Problems of Cryobiology. 2001; (1): 35-41.
Bennett V, Baines AJ. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol Rev. 2001; 81(3): 135-92. CrossRef
Fairbanks G, Steck TL, Wallach D. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971; 10(13): 2606-17. CrossRef
Falko OV, Zemlianskykh NG, Lipina OV, Prokopyuk OS. Modification of placental blood serum proteins induced by low temperatures. Biochemistry Suplement Series B: Biomedical Chemistry. 2012; 6(2): 194-202. CrossRef
George A, Pushkaran S, Konstantinidis DG, et al. Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease. Blood. 2013; 121(11): 2099-107. CrossRef
Haest CW, Kamp D, Plasa G, Deuticke B. Intra- and intermolecular cross-linking of membrane proteins in intact erythrocytes and ghosts by −SH-oxidizing agents. Biochim Biophys Acta. 1977; 469(2): 226-30. CrossRef
Henkelman S, Noorman F, Badloe JF, Lagerberg JW. Utilization and quality of cryopreserved red blood cells in transfusion medicine. Vox Sang. 2015; 108(2). 103-12. CrossRef
Kanias T, Acker JP. Biopreservation of red blood cells - the struggle with hemoglobin oxidation. FEBS J. 2010; 277(2): 343-56. CrossRef
Kucherenko YV, Bernhardt I. The study of Ca2+ influx in human erythrocytes in isotonic polyethylene (glycol) 1500 (PEG-1500) and sucrose media. Ukr Biokhim Zh. 2006; 78(6): 46-52. PubMed
Lux IV Samuel E. Anatomy of the red cell membrane skeleton: unanswered questions. Blood. 2016; 127(2): 187-99. CrossRef
Panday A, Sahoo MK, Osorio D, Batra S. NADPH oxidases: an overview from structure to innate immunity-associated pathologies. Cell Mol Immunol. 2015; 12(1): 5-23. CrossRef
Peskin AV, Dickerhof N, Poynton RA, et al. Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine. J Biol Chem. 2013; 288(20): 14170-7. CrossRef
Rhee SG. Overview on peroxiredoxin. Mol Cells. 2016; 39(1): 1-5. CrossRef
Scott KL, Lecak J, Acker JP. Biopreservation of red blood cells: past, present, and future. Transfus Med Rev. 2005; 19(2): 127-42. CrossRef
Sharma S, Punjabi V, Zingde SM, Gokhale SM. A comparative protein profi le of mammalian erythrocyte membranes identified by mass spectrometry. J Membr Biol 2014; 247(11): 1181-9. CrossRef
Sies H. Role of metabolic H2O2 generation: redox signaling and oxidative stress. J Biol Chem 2014; 289(13): 8735-41. CrossRef
Singbartl K, Langer R, Henrich A. Altered membrane skeleton of hydroxyethylstarch-cryopreserved human erythrocytes. Cryobiology. 1998; 36(2): 115-23. CrossRef
Svetina S, Kuzman D, Waugh RE, et al. The cooperative role of membrane skeleton and bilayer in the mechanical behaviour of red blood cells. Bioelectrochemistry. 2004; 62(2): 107-13. CrossRef
Welbourn EM, Wilson MT, Yusof A, et al. The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radic Biol Med. 2017; 103: 95-106. CrossRef
Zemlianskykh NG. Regulation of the asymmetric distribution of lipids in human erythrocyte membrane in the presence of glycerol and polyethylene glycol. Cell Tiss Biol. 2020; 14(4): 286-93. CrossRef
Zemlianskykh NG. [The effect of cryoprotective agents on proteins of the erythrocyte membrane-cytoskeleton complex]. Biomed Khim. 2020; 66(6): 456-63. Russian. CrossRef
Zemlianskykh NG, Babiychuk LA. The changes in erythrocyte Ca2+-ATPase activity induced by PEG-1500 and low temperatures. Cell Tiss Biol. 2017; 11(2): 104-10. CrossRef
Zemlianskykh NG, Babiychuk LA. The production of reactive oxygen species in human erythrocytes during cryopreservation with glycerol and polyethylene glycol. Biophysics. 2019; 64(4): 560-7. CrossRef
Downloads
Published
How to Cite
Issue
Section
License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).