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Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells.

Galili, U, Shohet, S B, Kobrin, E, Stults, C L, Macher, B A·1988·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)77900-9
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Abstract

The study of the expression of alpha-galactosyl epitopes on various mammalian cells is of particular interest, since as much as 1% of circulating IgG antibodies in humans interact with this carbohydrate residue. This natural antibody, designated "anti-Gal," was previously found to bind to terminal Gal alpha 1----3Gal beta 1----4GlcNAc-R on biochemically defined glycolipids (Galili, U., Macher, B. A., Buehler, J., and Shohet, S. B. (1985) J. Exp. Med. 162, 573-582; Galili, U., Buehler, J., Shohet, S. B., and Macher, B. A. (1987) J. Exp. Med. 165, 693-704). The expression of anti-Gal binding epitopes on nucleated cells from various mammalian species was studied by immunostaining with this antibody. The binding of anti-Gal to various cells was correlated with the binding of the lectin Bandeiraea (Griffonia) simplicifolia IB4 (BS lectin). The BS lectin also interacts with alpha-galactosyl residues and particularly with high affinity with Gal alpha 1----3Gal beta 1----4GlcNAc residues. We observed a striking evolutionary pattern in the expression of these epitopes on mammalian nucleated cells. Fibroblasts, epithelial cells, endothelial cells, smooth muscle cells, and lymphoid cells of nonprimate mammals, prosimians, and New World monkeys readily bound both anti-Gal and BS lectin. However, no such binding was detectable on cells of Old World monkeys, apes, and humans. Measurment of the binding of radiolabeled BS lectin to the various nucleated cells suggests that cells binding anti…

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  • Porcine cells display three major glycan antigens on their cell surface - α-Gal, Neu5Gc and Sd(a) - which are the products of GGTA1, CMAH and B4GALNT2/B4GALNT2L.

    “Porcine cells display three major glycan antigens on their cell surface — α-Gal15, Neu5Gc16 and Sd(a)17 (Fig. 1a) — which are the products of the corresponding glycan synthesis genes, glycoprotein α-galactosyltransferase 1 (GGTA1), cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) and β-1,4-N-acetyl-galactosaminyltransferase 2 (B4GALNT2)/B4GALNT2-like (B4GALNT2L).”

    From Design and testing of a humanized porcine donor for xenotransplantation (2023) · cites this paper as [15]

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Metadata

Authors
Galili, U., Shohet, S. B., Kobrin, E., Stults, C. L., & Macher, B. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1988-11
Volume
263
Issue
33
Pages
17755-17762
ISSN
0021-9258
DOI
10.1016/s0021-9258(19)77900-9
Cited by
817
References
0
Language
en
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