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Glycobiology, 2000, Vol. 10, No. 7 745-751
© 2000 Oxford University Press

Reduction of the major xenoantigen on glycosphingolipids of swine endothelial cells by various glycosyltransferases

Masaru Koma2,3,4, Shuji Miyagawa1,3, Koichi Honke2, Yoshitaka Ikeda2, Souichi Koyota2, Shinichiro Miyoshi4, Hikaru Matsuda4, Shuichi Tsuji5, Ryota Shirakura3 and Naoyuki Taniguchi2

2Department of Biochemistry, 3Division of Organ Transplantation, Biomedical Research Center, 4Department of Surgery for Functional Regulation, Osaka University Graduate School of Medicine, 2–2 Yamadaoka, Suita, Osaka 565–0871, Japan, 5Molecular Glycobiology, Frontier Research Program, Inst. of Physical and Chemical Res. (RIKEN), Wako, Saitama 351–0100, Japan

The effect of the various glycosyltransferases on glycosphingolipids was examined, using transfected swine endothelial cell (SEC) lines. The reactivity of parental SEC to normal human serum (NHS) and Griffonia simplicifolia IB4 (GSIB4) lectin, which binds to the Gal {alpha}1–3 Gal ß 1–4 GlcNAc-R ({alpha}-galactosyl epitope), was reduced by ~20% by the treatment with D-PDMP (D-threo-1-phenyl-2-decan- oylamino-3-morpholino-1-propanol), suggesting that glycosphingolipids contained by SEC have a considerable amount of the {alpha}-galactosyl epitope. The overexpression of two different types of glycosyltransferase, N-acetylglucosaminyl transferase III (GnT-III), as well as {alpha}2,6-sialyltransferase (ST6Gal I), {alpha}2,3-sialyltransferase (ST3Gal III), and {alpha}1,2-fucosyltransferase ({alpha}1,2FT), suppresses the total antigenicity of SEC significantly. However, the reduction in reactivities toward NHS and GSIB4 lectin in the case of GnT-III transfectants was milder than those in other transfectants. Western blot analysis indicated that the glycoproteins in all transfectants had diminished reactivity to NHS and GSIB4 lectin to approximately the same extent. Therefore, the neutral glycosphingolipids of these transfectants were separated by thin layer chromatography, followed by immunostaining with NHS and GSIB4 lectin. The levels of the {alpha}-galactosyl epitope in glycosphingolipids were not decreased in the GnT-III transfectants but were in the ST6Gal I, ST3Gal III, and {alpha}1,2FT transfectants. These data indicate that ST6Gal I, ST3Gal III, and {alpha}1,2FT reduced the {alpha}-galactosyl epitope in both glycoproteins and glycosphingolipids, while GnT-III reduced them only in glycoproteins.

1 To whom correspondence should be addressed


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