Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

BACKGROUND: We have previously demonstrated that porcine livers perfused with human blood remove most of the erythrocytes from three units of human blood over the course of a 72-h extracorporeal perfusion. Red blood cell loss did not appear to involve classical complement pathway-mediated hemolysis, but instead resulted from porcine Kupffer cell phagocytosis. METHODS: We developed a method incorporating collagenase digestion and metrizamide separation to isolate and maintain porcine Kupffer cells in primary culture. An in vitro rosetting assay was used to assess the binding of human and porcine erythrocytes to porcine Kupffer cells. Immunohistochemistry was used to confirm the presence of porcine macrophages. The rosetting assay was quantified using 51Cr-labeling of erythrocytes to assay for both rosette formation and phagocytosis. RESULTS: Porcine Kupffer cells were successfully isolated and maintained in primary culture. The presence of porcine macrophages was confirmed using the monoclonal antibody 74-22-15A. Human, but not porcine, erythrocytes were bound in an in vitro rosetting assay as confirmed by immunohistochemistry, electron microscopy and 51Cr-quantitation. Porcine Kupffer cells bound human erythrocytes regardless of the presence of opsonizing antibody. Approximately 70% of the isolated porcine Kupffer cells demonstrated the capacity to bind non-opsonized human erythrocytes. Phagocytosis was not observed. CONCLUSIONS: Using primary porcine Kupffer cell cultures, we have demonstrated that a subpopulation of porcine macrophages has the ability to recognize specifically xenogeneic human erythrocyte epitopes without the need for prior opsonization. The possibility is discussed that lectin-mediated carbohydrate binding plays a role in the cellular and humoral recognition and rejection of xenografts.

Original publication




Journal article



Publication Date





13 - 19


Animals, Antigens, Heterophile, Epitopes, Erythrocytes, Humans, Kupffer Cells, Lectins, Macrophages, Microscopy, Electron, Scanning, Phagocytosis, Receptors, Cell Surface, Sus scrofa, Transplantation, Heterologous