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Specific removal of anti-A and anti-B antibodies by using modified dialysis filters
M S Hout1, K E LeJeune, T M Schaack
1Department of Bioengineering, University of Pittsburgh, Pennsylvania, USA.
Removal of anti-A and anti-B blood group antibodies from human blood has been shown to facilitate cross-matched kidney transplantation by preventing hyperacute rejection. Patients in these studies had anti-A and anti-B antibodies removed by using plasmapheresis, followed by immunoadsorption onto packed bead columns. We conducted a study to assess the feasibility of selectively removing anti-A and anti-B antibodies directly from blood by using modified dialysis filters. An anti-A and anti-B specific antigen was covalently attached to the lumenal surfaces of hollow fibers within selected commercial dialysis modules. The filters were able to reduce the anti-A and anti-B titers of 300 ml of blood to 2 or below. A low molecular weight fraction of our antigen system was found to have no antibody binding capacity. The standard antigen was purified by removal of the low molecular weight fraction and a dialysis filter was modified by using the purified antigen. This filter displayed a six-fold higher capacity than a dialysis filter modified with the same mass of standard antigen. We conclude that selective blood group antibody removal by antigen modified dialysis filters is feasible and may be a simpler system than plasmapheresis followed by immunoadsorption.
Removal of anti-A and anti-B blood group antibodies from human blood has been shown to facilitate cross-matched kidney transplantation by preventing hyperacute rejection. Patients in these studies had anti-A and anti-B antibodies removed by using plasmapheresis, followed by immunoadsorption onto packed bead columns. We conducted a study to assess the feasibility of selectively removing anti-A and anti-B antibodies directly from blood by using modified dialysis filters. An anti-A and anti-B specific antigen was covalently attached to the lumenal surfaces of hollow fibers within selected commercial dialysis modules. The filters were able to reduce the anti-A and anti-B titers of 300 ml of blood to 2 or below. A low molecular weight fraction of our antigen system was found to have no antibody binding capacity. The standard antigen was purified by removal of the low molecular weight fraction and a dialysis filter was modified by using the purified antigen. This filter displayed a six-fold higher capacity than a dialysis filter modified with the same mass of standard antigen. We conclude that selective blood group antibody removal by antigen modified dialysis filters is feasible and may be a simpler system than plasmapheresis followed by immunoadsorption.
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