Modifications of proteins of membrane-cytoskeleton complex and production of reactive oxygen species in erythrocytes cryopreserved with polyethylene glycol
N.G. Zemlianskykh, L.O. Babiychuk
Institute for Problems of Cryobiology and Cryomedicine, National Academy of Sciences of Ukraine, Kharkov, Ukraine
DOI: https://doi.org/10.15407/fz67.02.044
Abstract
Protein modifications in the membrane-cytoskeleton complex (MCC) of human erythrocytes, as well as
changes in the intensity of reactive oxygen species (ROS) production upon cell cryopreservation with
polyethylene glycol (PEG) were investigated. The protein profile of ghosts of erythrocytes frozen with PEG
has common features with both the control and cells frozen without cryoprotectant. PEG makes it possible
to restrict the structural rearrangements of the main MCC proteins under the effect of extreme factors and
to restrain the amount of high molecular weight polypeptide complexes induced by the protein-cross-linking
reagent diamide at the control level, in contrast to cells frozen without a cryoprotectant. However, changes
related to the protein peroxiredoxin 2 in ghosts of erythrocytes cryopreserved with PEG are also attributed
to cells frozen without a cryoprotectant that may be associated with the activation of oxidative processes.
This is evidenced by a 10-fold increase in ROS formation in erythrocytes frozen under PEG protection. Thus,
upon cryopreservation of erythrocytes with PEG, certain disorders in MCC proteins may be associated with
increased formation of ROS, which may contribute to the disorganization of the structural components of
MCC and disrupt the stability of cryopreserved cells under physiological conditions.
Keywords:
Erythrocyte; membrane; cytoskeleton; protein; reactive oxygen species; cryopreservation; polyethylene glycol.
References
- Ragoonanan V, Hubel A, Aksan A. Response of the cell membrane - cytoskeleton complex to osmotic and freeze/ thaw stresses. Cryobiology. 2010;61(3):335-44.
CrossRef
PubMed
- Scott KL, Lecak J, Acker JP. Biopreservation of red blood cells: past, present, and future. Transfus Med Rev. 2005;19(2):127-42.
CrossRef
PubMed
- Babijchuk LA, Zemlianskykh NG. Optimization and advantages of washing-out method of erythrocyte cryopreservation with PEO-1500. Probl Cryobiol. 2001;(1):35-41.
- Singbartl K, Langer R, Henrich A. Altered membrane skeleton of hydroxyethylstarch-cryopreserved human erythrocytes. Cryobiology. 1998;36(2),115-23.
CrossRef
PubMed
- Mohandas N, Chasis JA. Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids. Semin Hematol. 1993;30(3):171-92.
- Zemlianskykh NG. Effect of substances with cryoprotective properties on surface marker CD44 in human erythrocytes. Cytol Genet. 2016;50(3):203-13.
CrossRef
- Zemlianskykh NG, Babijchuk LA. Changes in erythrocyte surface marker cd44 during hypothermic and low temperature storage. Fiziol Zh. 2016;62(2):94-102.
CrossRef
PubMed
- Kriebardis AG, Antonelou MH, Stamoulis KE, EconomouPetersen E, Margaritis LH, Papassideri IS. Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells. J Cell Mol Med. 2007;11(1):148-55.
CrossRef
PubMed PubMedCentral
- Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971;10(13),2606-17.
CrossRef
PubMed
- Sharma S, Punjabi V, Zingde SM, Gokhale SM. A comparative protein profile of mammalian erythrocyte membranes identified by mass spectrometry. J Membr Biol. 2014;247(11):1181-1189.
CrossRef
PubMed
- Lux 4th. SE. Anatomy of the red cell membrane skeleton: unanswered questions. Blood. 2016;127(2):187-99.
CrossRef
PubMed
- An X, Gauthier E, Zhang X, Guo X, Anstee DJ, Mohandas N, Chasis JA. Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin. Blood. 2008;112(13):5212-18.
CrossRef
PubMed PubMedCentral
- Peskin AV, Dickerhof N, Poynton RA, Paton LN, Pace PE, Hampton MB, Winterbourn CC. 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):14170-77.
CrossRef
PubMed PubMedCentral
- Kanias T, Acker JP. Biopreservation of red blood cells - the struggle with hemoglobin oxidation. FEBS J. 2010;277(2):343-356.
CrossRef
PubMed
- Pellerin-Mendes C, Million L, Marchand-Arvier M, Labrude P, Vigneron C. In vitro study of the protective effect of trehalose and dextran during freezing of human red blood cells in liquid nitrogen. Cryobiology. 1997;35(2):173-86.
CrossRef
PubMed
- George A, Pushkaran S, Konstantinidis DG, Koochaki S, Malik P, Mohandas N, Zheng Y, Joiner CH, Kalfa TA. 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
PubMed PubMedCentral
- Zemlianskykh NG, Babiychuk LA.. The changes in erythrocyte Ca2+-ATPase activity induced by PEG-1500 and low temperatures. Cell Tissue Biol. 2017;11(2):104-10.
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.
- Osborn KD, Zaidi A, Urbauer RJB, Michaelis ML, Johnsonet CK. Single-molecule characterization of the dynamics of calmodulin bound to oxidatively modified plasma-membrane Ca2+-ATPase. Biochemistry. 2005;44(33):11074-81.
CrossRef
PubMed
- Chen B, Mayer MU, Squier TC. Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase. Biochemistry. 2005;44(12):4737-47.
CrossRef
PubMed
|