CHANGES IN ERYTHROCYTE SURFACE MARKER CD44 DURING HYPOTHERMIC AND LOW TEMPERATURE STORAGE
N.G. Zemlianskykh, L.A. Babijchuk
Institute for Problems of Cryobiology and Cryomedicine,
Kharkіv.
DOI: https://doi.org/10.15407/fz62.02.094
![](/images/cite.png)
Abstract
We studied the changes in surface marker CD44 in erythrocytes,
cryopreserved under the protection of glycerol and PEG–1500,
or stored in hypothermic conditions. It was shown that during
hypothermic storage the CD44 characteristics in erythrocyte
suspension were unchanged within 10 days. In cryopreserved
erythrocytes a reduction in CD44–positive cells and in the
level of expression of the surface marker were marked. Using
PEG–1500 resulted in more pronounced change in erythrocyte
CD44 characteristics after freeze–thawing in comparison with
glycerol. Removal of cryoprotectants and the loss of a part of
cells during the washing process led to the restoration of the
CD44 characteristics in freeze–thawed erythrocytes suspension
which successfully survived after the stresses. The results
indicate that revealed changes in cryopreserved erythrocytes
cover only a part of the cells, and they are associated with
the instability of the population of erythrocytes with altered
CD44 characteristics wherethrough after the removal of
cryoprotectants with concomitant hemolysis of unstable cells
the CD44 parameters in erythrocyte suspensions recovered.
The mechanisms underlying the changes in the parameters of
the surface marker CD44 in freeze–thawed erythrocyte may
be related to the disruption of intermolecular interactions in
the membrane under the influence of physical and chemical
environmental factors, followed by the membrane vesiculation
with the inclusion of the CD44 into the vesicles.
Keywords:
erythrocyte; membrane; CD44; freezing; cryoprotectant; hypothermia.
References
- Gottlieb Y, Topaz O, Cohen LA, Yakov LD, Haber T, Morgenstern A, Weiss A, Berman KC, Fibach E, Meyron–Holtz EerG. Physiologically aged red blood cells undergo erythrophagocytosis in vivo but not in vitro. Haematologica. 2012;97(7):994–1002.
CrossRef
PubMed PubMedCentral
- Dinkla S, Novotný VM, Joosten I, Bosman GJ. Storage– induced changes in erythrocyte membrane proteins promote recognition by autoantibodies. PLoS One. 2012;7(8):1-9.
CrossRef
PubMed PubMedCentral
- Borland G, Ross JA, Guy K. Forms and functions of CD44 Immunology. 1998;93(2):139–148.
- Rudzki Z, Jothy S. CD44 and the adhesion of neoplastic cells. Mol Pathol. 1997; 5(2): 57–71.
CrossRef
- Telen MJ, Udani M, Washington MK, Levesque MC, Lloyd E, Rao N. A blood group–related polymorphism of CD44 abolishes a hyaluronan–binding consensus sequence without preventing hyaluronan binding. J Biol Chem. 1996;271(12):7147–53.
CrossRef
PubMed
- Xu Z, Duffett L, Tokessy M, Cote J, Goldman M, Saidenberg E. Anti– AnWj causing acute hemolytic transfusion reactions in a patient with aplastic anemia. Transfusion. 2012; 2(7):1476–81.
CrossRef
PubMed
- Telen MJ. Red blood cell surface adhesion molecules: their possible roles in normal human physiology and disease. Semin Hematol. 2000;37(2):130–142.
CrossRef
- Hale LP, Singer KH, Haynes BF. CD44 antibody against In(Lu)–related p80, lymphocyte–homing receptor molecule inhibits the binding of human erythrocytes to T cells. J Immunol. 1989 143(12):3944–48.
PubMed
- Funaro A, Spagnoli GC, Momo M, Knapp W, Malavasi F. Stimulation of T cells via CD44 requires leukocyte– function– associated antigen interactions and interleukin–2 production. Hum Immunol. 1994;40(4):267–78.
CrossRef
- van den Akker E, Satchwell TJ, Pellegrin S, Flatt JF, Maigre M, Daniels G, Delaunay J, Bruce LJ, Toye AM. Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2(–) cells (mutations Chartres 1 and 2). Haematologica. 2010;95(8):1278–86.
CrossRef
PubMed PubMedCentral
- Lelkens CC, Noorman F, Koning JG, Truijens–de Lange R, Stekkinger PS, Bakker JC, Lagerberg JW, Brand A, Verhoeven AJ. Stability after thawing of RBCs frozen with the high– and low–glycerol method. Transfusion. 2003;43(2):157–64.
CrossRef
PubMed
- Stoll C, Holovati JL, Acker JP, Wolkers WF. Synergistic effects of liposomes, trehalose, and hydroxyethyl starch for cryopreservation of human erythrocytes. Biotechnol Prog. 2012;28(2):364–71.
CrossRef
PubMed
- Feuerecker M, Kaufmann I, Salam AP, Choukèr A. Effects of cryopreservation with polyethylene glycol on the expression of CD11b and CD62L on the surface of polymorphonuclear leukocytes. Cryo Letters. 2012;33(2):151–60.
- Gabellieri E, Strambini GB. ANS fluorescence detects widespread perturbations of protein tertiary structure in ice. Biophys J. 2006;90(9):3239–45.
CrossRef
PubMed PubMedCentral
- Wolkers WF, Balasubramanian SK, Ongstad EL, Zec HC, Bischof JC. Effects of freezing on membranes and proteins in LNCaP prostate tumor cells. Biochim Biophys Acta. 2007;1768(3):728–36.
CrossRef
PubMed PubMedCentral
- Celedón G, González G, Barrientos D, Pino J, Venegas F, Lissi EA, Soto C, Martinez D, Alvarez C, Lanio ME. Stycholysin II, a cytolysin from the sea anemone Stichodactyla helianthus promotes higher hemolysis in aged red blood cells. Toxicon. 2008;51(8):1383–90.
CrossRef
PubMed
- Iglic A, Veranic P, Jezernik K, Fosnaric M, Kamin B, Hägerstrand H, Kralj–Iglic V. Spherocyte shape transformation and release of tubular nanovesicles in human erythrocytes Bioelectrochemistry. 2004;62(2):159–61.
CrossRef
PubMed
- Holovati JL, Wong KA, Webster JM, Acker JP. The effects of cryopreservation on red blood cell microvesiculation, phosphatidylserine externalization, and CD47 expression. Transfusion. 2008;48(8):1658–68.
CrossRef
PubMed
- Bosman GJ, Lasonder E, Groenen–Döpp YA, Willekens FL, Werre JM. The proteome of erythrocyte– derived microparticles from plasma: new clues for erythrocyte aging and vesiculation. J Proteomics. 2012;76(Spec.):203–10.
CrossRef
PubMed
- Nunomura W, Takakuwa Y, Tokimitsu R, Krauss SW, Kawashima M, Mohandas N. Regulation of CD44 – protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44–ankyrin interaction. J Biol Chem. 1997;272(48):30322–8.
CrossRef
PubMed
- Jeremy KP, Plummer ZE, Head DJ, Madgett TE, Sanders KL, Wallington A, Storry JR, Gilsanz F, Delaunay J, Avent N.D. 4.1R– deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins. Haematologica. 2009;94(10):1354–61.
CrossRef
PubMed PubMedCentral
- Kofanova OA, Zemlyanskikh NG, Ivanova L, Bernhardt I. Changes in the intracellular Ca2+ content in human red blood cells in the presence of glycerol. Bioelectrochemistry. 2008;73(2):151–4.
CrossRef
PubMed
- 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. [Russian].
- Zemlyanskikh NG, Kofanova OA. Modulation of human erythrocyte Ca2+–ATPase activity by glycerol: the role of calmodulin. Biochemistry (Moscow). 2006;71(8):900–05.
CrossRef
- Zemlianskykh NG, Khomenko MV. Human erythrocyte Ca2+–ATPase activity in a hypertonic media at
low and physiological temperature. Biol Membrane. 2006;23(№5):375–83. [Russian].
|