Gal-a-1,3-Gal Epitope: Role in Cell Biology and Transplantation
Keywords:alpha-Gal epitope, transplantation, bioprosthesis, hypothermic storage, cryopreservation
Gal-a-1,3-Gal (a-Gal) epitope is a carbohydrate structure, which is expressed on cell membranes of almost all the mammals except some species of monkeys and human, as well as causes a hyperacute immune response during xenotrans-plantation. This review briefly describes the issues of the evolution of a-Gal epitope, its distribution in the kingdom of animals, biological role and problems of using prostheses of porcine origin in medical practice. For many reasons, this species of animals is the most suitable to obtain the bioprostheses of cardiac valves, vessels and bioscaffolds, however, due to the high a-Gal epitope expression in their body a special treatment to eliminate it is required. This review attempts to summarize the results on studying the a-Gal epitope expression after low-temperature treatment, since it is widely used to store bioprostheses prior to implantation.
Probl Cryobiol Cryomed 2016; 26(1):3-12
Anstee D.J. Blood group-active surface molecules of the human red blood cell. Vox Sang 1990; 58(1): 1â€“20. CrossRef
Artrip J. H., Kwiatkowski P., Michler R. E. et al. Target cell susceptibility to lysis by human natural killer cells is augmented by alpha(1,3)-galactosyltransferase and reduced by alpha(1,2)-fucosyltransferase. J Biol Chem 1999; 274(16): 10717â€“10722. CrossRef PubMed
Azimzadeh A., Meyer C., Watier H. et al. Removal of primate xenoreactive natural antibodies by extracorporeal perfusion of pig kidneys and livers. Transpl Immunol 1998; 6(1): 13â€“22. CrossRef
Bondarenko T.P., Bozhok G.A., Alabedalkarim N.M., Legach E.I. Xenotransplantation: historical aspect and modern state of the problem. Transplantologya 2004; 7(3): 130â€“135.
Brenner P., Hinz M., Huber H. et al. Influence of ischemic time on hyperacute xenograft rejection of pig hearts in a working heart perfusion model with human blood. Transpl Int 2000;13 (Suppl. 1): S494â€“503. CrossRef PubMed
Collins B.H., Cotterell A.H., McCurry K.R. et al. Cardiac xenografts between primate species provide evidence of the a-galactosyl determinant in hyperacute rejection. J Immunol 1994; 154(10): 5500â€“5510.
Etienne-Decerf J., Malaise M., Mahieu P., Winand R. Elevated anti alpha-galactosyl antibody titers. A marker of progression in autoimmune thyroid disorders and endocrine ophthalmo-pathy. Acta Endocrinol 1987; 115: 67â€“74. PubMed
Galili U. Abnormal expression of alpha-galactosyl epitopes in man. A trigger for autoimmune processes. Lancet 1989; 8(8659): 358â€“361. CrossRef
Galili U. Anti-Gal and anti-non Gal antibody barriers in xenotransplantation. Miyagawa S., editor. Xenotransplantation. InTech, 2012. Available from: http://www.intechopen.com/books/xenotransplantation/anti-gal-and-anti-non-gal-antibody-barriers-in-xenotransplantation.
Galili U., Clark M., Mohandas N. et al. The natural anti-c~-galactosyl IgG on red cells in sickle cell disease. Blood Cells 1984; 14(1): 205â€“228.
Galili U., Clark M.R., Shohet S.B. et al. Evolutionary relationship between the natural anti-Gal antibody and the Gal-a-1,3-Gal epitope in primates. Proc Natl Acad Sci USA 1987; 84(5): 1369â€“1373. CrossRef PubMed
Galili U., Clark M.R., Shohet S.B. Excessive binding of natural anti-alpha-galactosyl IgG to sickle erythrocytes may contribute to extravascular cell destruction. J Clin Invest 1986; 77(1): 27â€“33. CrossRef PubMed
Galili U., Korkesh A., Kahane I., Rachmilewitz E.A. Demon-stration of a natural antigalactosyl IgG antibody on thalassemic red blood cells. Blood 1983; 61(6): 1258â€“1264. PubMed
Galili U., Macher B.A., Buehler J., Shohet S.B. Human natural anti-alpha-galactosyl IgG. II. The specific recognition of alpha (1-3)-linked galactose residues. J Exp Med 1985; 162(2): 573â€“582. CrossRef PubMed
Galili U., Mandrell R.E., Hamadeh R.M. et al. Interaction between human natural anti-a-galactosyl immunoglobulin G and bacteria of the human flora. Infect Immun 1988; 56(7): 1730â€“1737. PubMed
Galili U., Shohet S.B., Kobrin E. et al. Man, apes and Old World monkeys differ from other mammals in the expression of a-galactosyl epitopes on nucleated cells. J Biol Chem 1988; 263(33): 17755â€“17762. PubMed
Galili U., Swanson K. Evolution gene sequences suggest inactivation of a-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc Natl Acad Sci USA 1991; 88(16): 7401â€“7404. CrossRef
Galili U., Tibell A., Samuelsson B. et al. Increased anti-Gal activity in diabetic patients transplanted with fetal porcine islet cell clusters. Transplantation 1995; 59(11): 1549â€“1556. CrossRef PubMed
Good A.H., Cooper D.C.K., Malcolm A.J. et al. Identification of carbohydrate structures which bind human anti-porcine antibodies: implication for discordant xenografting in man. Transplant Proc 1992; 24(2): 559â€“562. PubMed
Groth C.G., Korsgren O., Tibell A. et al. Transplantation of fetal porcine pancreas to diabetic patients. Lancet 1994; 344(8934): 1402â€“1404. CrossRef
Hayashi S., Katayama A., Nagasaka T. et al. Tissue distribution of Gal-alpha-1,3-Gal epitope in heart, kidney and liver of pig and mouse. Transplant Proceedings 1996; 28(1): 216. PubMed
Igaz P. Recent strategies to overcome the hyperacute rejection in pig to human xenotransplantation. Yale J Biol Med 2001; 74(5): 329â€“340. PubMed
Joziasse D.H., Oriol R. Xenotransplantation: the importance of the Gal-alpha-1,3-Gal epitope in hyperacute vascular rejec-tion. Biochem Biophys Acta 1999; 1455(2â€“3): 403â€“418. CrossRef
Keller M., Beiras-Fernandez A., Schmoeckel M. et al. Influence of hypothermia and cardioplegic solutions on expression of alpha-Gal epitope on porcine aortic endothelial cells. Exp Clin Transplant 2010; 8(3): 250â€“257. PubMed
Mayo G.L., Posselt A.M., Barker C.F. et al. Prolongation of survival of donor-strain islet xenografts (rat-mouse) by intrathymic inoculation of xenogeneic islet and bone marrow cells. Transplantation 1994; 58(1): 107â€“109. CrossRef PubMed
McKenzie I.F., Xing P.X., Vaughan H.A. et al. Distribution of the major xenoantigen (Gal-alpha-1,3-Gal) for pig to human xenografts. Transplant Immunol 1994; 2(2): 81â€“86. CrossRef
Napier J.R., Napier P. H. The natural history of the primates. Cambridge: MIT Press, 1985.
Oriol R., Ye Y., Koren E., Cooper D.K. Carbohydrate antigenes of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation.Transplantation.1993; 56(6): 1433â€“1442. CrossRef PubMed
Platt J.L. A perspective on xenograft rejection and accommo-dation. Immunol Rev 1994; 141: 127â€“149. CrossRef
Rayat G.R., Rajotte R.V., Hering B.J. et al. In vitro and in vivo expression of Gal-(1,3)-Gal on porcine islet cells is age dependent. J Endocrinology 2003; 177(1): 127â€“135. CrossRef
Saadi S., Ihrcke N.S., Platt J.L. Endothelial cell shape and hyperacute rejection. Transplant Proc 1994; 26(3): 1149. PubMed
Sandrin M., Vaughan H.A., Dabkowski P.L., McKenzie I.F.C. Anti-pig IgM antibodies in human serum react predominantly with Gal-a-1,3-Gal epitopes. Proc Natl Acad Sci USA 1993; 90(23): 11391â€“11395. CrossRef PubMed
Simon P.M., Neethling F.A., Taniguchi S. et al. Intravenous infusion of Gal-alpha-1,3-Gal oligosaccharides in baboons delays hyperacute rejection of porcine hearts xenografts. Transplantation 1998; 65(3): 346â€“353. CrossRef PubMed
Tanemura M., Yin D., DiSesa V. J., Galili U. Preventing anti-Gal response in xenograft recipients by an alpha-Gal toxin. Transplant Proc 2001; 33(1â€“2): 699â€“700. CrossRef
Xu T., Lorf T., Sablinski T. et al. Removal of anti-porcine natural antibodies from human and nonhuman primate plasma in vitro and in vivo by a Gal-a-1,3-Gal-a-1,4-Glc-R immunoaffinity column.Transplantation 1998; 65(2): 172â€“179. CrossRef PubMed
How to Cite
Copyright (c) 2020 Konstantin I. Bohuslavskyi, Galina A. Bozhok, Evgeniy I. Legach, Igor V. Furda, Tatyana P. Bondarenko
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).