Influence of Chemical Modification on “In Vivo” and “In Vitro” Mouse Carrier Erythrocyte Survival and Recognition

  • J. A. Jordán
  • F. J. Alvarez
  • J. C. Murciano
  • A. Lotero
  • A. Herráez
  • M. C. Tejedor
  • J. Luque
  • J. R. DeLoach
  • J. C. Díez

Abstract

Several systems have been developed with therapeutical purposes for drug delivery. Among them, red blood cells (RBCs) have been claimed to be a physiological method to convey and deliver active compounds.4,6,8,11 The preparation of erythrocytes as carriers can require encapsulation procedures or/and chemical modification of erythrocyte surface.3,22 In fact, the efficacy of these systems can be dependent of the use of several chemical treatments which can react with cell membrane proteins. Crosslinking reagents can be applied to red blood cell modification. Glutaraldehyde (GA) has been the most extensively used crosslinker.7,21 Also, other crosslinkers can be applied to carrier erythrocytes preparation.12,16 Biotinylation is another alternative method for carrier preparation.15,19 Eventually, chemical modification can promote targeting of carrier erythrocytes to several organs.12,21 We have focused our attention on the action of crosslinking reagents which react with band 3 in mouse erythrocyte membrane. Additionally, biotinylation of mouse erythrocytes has been studied. “In vivo” behaviour of these chemically modified erythrocytes have been studied. These survival results have been compared to recognition by macrophages. Thus, we described conditions for using these chemical treatments for targeting to organs and macrophages.

Keywords

Erythrocyte Membrane Crosslinking Reagent Hypotonic Shock Crosslinker Concentration Mouse Erythrocyte 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    L. Chiarantini, J. Johnson and J. R. DeLoach, Optimized recirculation survival of mouse carrier erythrocytes, Blood Cells 17:607 (1991).PubMedGoogle Scholar
  2. 2.
    L. Chiarantini, L. Rossi, A. Fraternale and M Magnani, Modulated red blood cell survival by membrane protein clustering, Mol. Cell Biochem. 144:53 (1995).PubMedCrossRefGoogle Scholar
  3. 3.
    J.R. DeLoach, Encapsulation of exogenous agents and the circulating survival of carrier erythrocytes, J.Appl. Biochem. 5:149 (1983).PubMedGoogle Scholar
  4. 4.
    J.R. DeLoach, Carrier erythrocytes, Med. Res. Rev. 6:487 (1986).PubMedCrossRefGoogle Scholar
  5. 5.
    J.R. DeLoach and R. Drosleskey, Survival of murine carrier erythrocytes injected via peritoneum, Comp. Biochem. Physiol. 84A:447 (1986).CrossRefGoogle Scholar
  6. 6.
    J.R. DeLoach and U. Sprandel, Eds, Red Blood Cells as Carriers for Drugs, Karger, Basel (1985).Google Scholar
  7. 7.
    J.R. DeLoach, C.H. Tangner and C. Barton, Hepatic pharmacokinetics of glutaraldehyde-treated methrotrexate-loaded carrier erythrocytes in dogs, Res. Exp. Med. 183, 167 (1983).CrossRefGoogle Scholar
  8. 8.
    G.M. Ihler, Erythrocyte Carriers, Pharmac. Ther. 20:151 (1983).CrossRefGoogle Scholar
  9. 9.
    J.A. Jordán, J.R. DeLoach, J. Luque and J.C. Díez, Targeting of mouse erythrocytes by band 3 crosslinkers, Biochim. Biophys. Acta. 1291: 27 (1996).PubMedCrossRefGoogle Scholar
  10. 10.
    U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227:680(1970).PubMedCrossRefGoogle Scholar
  11. 11.
    M. Magnani and J. R. DeLoach,Eds, The Use of Resealed Erythrocytes as Carriers and Bioreactors, Plenum Press, New York (1992)Google Scholar
  12. 12.
    M. Magnani, L. Rossi, G. Brandi, G.F. Schiavano, M. Montroni and G. Piedimonte, Targeting antiretroviral nucleoside analogues in phosphorylated form to macrophages: In vitro and in vivo studies, Proc. Natl. Acad. Sci. USA, 89:6477 (1992).PubMedCrossRefGoogle Scholar
  13. 13.
    M.S. Meltzer, Peritoneal mononuclear phagocytes from small animals in Methods for studying mononuclear phagocytes. D.O. Adams; P.J. Edelson and H. Koren, eds. Academic Press pp. 63-67 (1981).Google Scholar
  14. 14.
    M. Morrison, A.W. Michaels, D.R. Phillips and S. Choi. Life span of erythrocyte membrane protein, Nature 248:763 (1974).PubMedCrossRefGoogle Scholar
  15. 15.
    V. Muzykantov and R. Taylor, Attachment of biotinylated antibody to red blood cells: Antigen binding capacity of immunoerythrocytes and their susceptibility to lysis by complement, Anal. Biochem. 223:142 (1994).PubMedCrossRefGoogle Scholar
  16. 16.
    M. Pinilla, J. Luque, and K. Tipton, Modification in the allosteric properties of phosphofructokinase in rat erythrocyte and reticulocyes cross-linked with dimethylsuberimidate and 3,3′-dithiobispropionimidate, Biochim. Biophys. Acta 702:254 (1982).PubMedCrossRefGoogle Scholar
  17. 17.
    J.V. Staros, N-hydroxysulfosuccinimide active esters: Bis(N-hydroxysulfosuccinimide) esters of dicarboxylic acids are hydrophilic membrane-impermeant, protein cross-linkers, Biochemistry 21:3950 (1982).PubMedCrossRefGoogle Scholar
  18. 18.
    J.V. Staros and B.P. Kakkad, Crosslinking and chymotryptic digestion of the extracytoplasmic domain of the anion exchange channel in intact human erythrocytes, J. Membrane Biol. 74:247 (1983).CrossRefGoogle Scholar
  19. 19.
    T. Suzuki and G.L. Dale, Biotinylated erythrocytes: In vivo survival and in vitro recovery, Blood. 70:791 (1987).PubMedGoogle Scholar
  20. 20.
    J. Vaysse; L. Gattegno; D. Bladier and D. Aminoff, Adhesion and electrophagocytosis of human senescent erythrocytes by autologous monocytes and their inhibition by beta-galactosyl derivatives, Proc. Natl. Acad. Sci. USA 83:1339 (1986).PubMedCrossRefGoogle Scholar
  21. 21.
    E. Zocchi, M. Tonetti, C. Polvani, L. Guida, U. Benatti and A. DeFlora, Encapsulation of doxorubicin in liver-targeted erythrocytes increases the therapeutic index of the drug in a murine metastatic model, Proc. Natl. Acad. Sci. USA, 86:2040 (1989).PubMedCrossRefGoogle Scholar
  22. 22.
    L. Zolla, G. Lupidi, M. Marcheggiani, G. Falcioni and M. Brunori, Encapsulation of proteins into human erythrocytes: a kinetic investigation, Biochim. Biophys. Acta 1024:5 (1990).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • J. A. Jordán
    • 1
  • F. J. Alvarez
    • 1
  • J. C. Murciano
    • 1
  • A. Lotero
    • 1
  • A. Herráez
    • 1
  • M. C. Tejedor
    • 1
  • J. Luque
    • 1
  • J. R. DeLoach
    • 2
  • J. C. Díez
    • 1
  1. 1.Departamento de Bioquímica y Biología MolecularCampus Universitario, Universidad de AlcaláAlcalá de Henares, MadridSpain
  2. 2.USDA.ARS-FAPLCollege StationUSA

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