E12

Recent studies have provided important information on the characteristics and porcine targets of PNXAb in humans and nonhuman primates. HAR results from activation of complement initiated by binding of xenoreactive antibodies to carbohydrate antigens on donor endothelium. The presence of anti-gal specific antibodies in certain primates has been linked to their lack of expression of the enzyme (a-galactosyl-transferase) needed to produce nonreducing terminal a-gal sugar residues. In vitro studies suggest that membrane proteins and lipids bearing a-gal structures are widely expressed on porcine cells, and that absorption of antibodies with anti-gal specificity prevents the in vitro lysis of porcine cells. Cooper et al have describes antibodies eluted from porcine organs perfused with human plasma to bind carbohydrates with terminal a-gal residues. Furthermore, in vivo administration of oligosaccharides capable of binding anti-gal antibodies has been shown to reduce antipig PNXAb titres in baboons and result in extended porcine xenograft survival.

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