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Chemical and lectin‐gold electron microscopical studies of the expression of the Galα1‐determinant in the pig aorta
Author(s) -
Hallberg Eva C.,
Strokan Valeri,
Cairns Thomas D.H.,
Breimer Michael E.,
Samuelsson Bo E.
Publication year - 1998
Publication title -
xenotransplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.052
H-Index - 61
eISSN - 1399-3089
pISSN - 0908-665X
DOI - 10.1111/j.1399-3089.1998.tb00035.x
Subject(s) - glycolipid , lectin , xenotransplantation , chemistry , glycoprotein , aorta , griffonia simplicifolia , immunohistochemistry , antigen , microbiology and biotechnology , biochemistry , biology , pathology , immunology , transplantation , medicine
In the xenotransplantation research field, pig aortic endothelial cells are frequently used in different model systems, e.g., for the study of the xenoantibody‐antigen reaction. The Galα1,3Gal determinant is the major target for human xenoreactive antibodies in pig tissue. Characterisation of the Galαl — distribution in pig aortic endothelial cells is thus important for understanding the reaction occurring at the endothelial cells during the xenorejection. We have determined the complete structure of the major Galα1,3Gal terminated glycolipid, Galα1,3nLc 4 Cer. Structural studies were performed on isolated glycosphingolipids by mass spectrometry and NMR spectroscopy. The results show a predominance of the pentasaccharide among the Galα1‐terminated glycolipids but also the presence of several Galα1‐terminated glycolipids with extended carbohydrate core chains. Ultrastructural localisation of the Galαl‐antigen in pig aorta was done by lectin‐gold electron microscopic studies of aortic wall sections using the Griffonia simplicifolia isolectin B 4 . Galα1‐determinants are predominantly localised on the luminal surface of pig aortic endothelial cells and endothelial cells of vasa vasorum and, to a lesser extent, vascular subendothelium.