Interaction of avidin-carrying red blood cells with nucleated cells.
In vivo application of red blood cells (RBC) modified with avidin-biotin complex has been suggested recently for various purposes. However, avidin attachment to RBC alters their biocompatibility. Thus, it has been described that avidin-carrying biotinylated RBC were lysed by the complement. In the present work interaction between avidin-carrying RBC and nucleated cells has been examined. It was found that attachment of avidin, but not streptavidin, to RBC led to binding of avidin-carrying RBC to nucleated cells. Adhesiveness of nucleated cells for avidin-carrying RBC varied for different types of nucleated cells. The strongest adhesion was observed with human fibroblasts and rat Kupffer cells, while rat liver endothelial cells were practically non-adhesive for avidin-carrying RBC of corresponding species. In contrast with avidin (streptavidin)-induced lysis by the complement, avidin-induced adhesion was independent of temperature, the presence of divalent ions and mode of avidin attachment. Polyanions (dextran sulphate and heparin) efficiently inhibited the adhesion presumably due to interaction with the membrane-bound avidin. Polyanions to a much lesser extent inhibited lysis of avidin-carrying RBC, which might be a result of their interaction with the complement components. Polycations also blocked adhesion of avidin-carrying RBC to nucleated cells, presumably due to interaction with negatively charged cell-surface components. Therefore, attachment of avidin to RBC alters their biocompatibility, due to both high positive charge of avidin and the cross-linking of biotinylated membrane proteins.
Muzykantov
V R
VR
Institute of Experimental Cardiology, Russian Academy of Medical Sciences, Moscow.
Zalzman
A B
AB
Fuki
I V
IV
Smirnov
M D
MD
Samokhin
G P
GP
Romanov
Y A
YA
D000818:Animals; D001360:Avidin / Q000737:chemistry / Q000378:metabolism*; D001710:Biotin; D002448:Cell Adhesion / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D005347:Fibroblasts; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D007728:Kupffer Cells; D008565:Membrane Proteins / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D051381:Rats
D008565:Membrane Proteins; D001360:Avidin; D001710:Biotin; D006493:Heparin