Sialic acids in T cell development and function |
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Authors: | Shuguang Bi Linda G. Baum |
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Affiliation: | Department of Pathology and Laboratory Medicine, UCLA School of Medicine, 10833 LeConte Ave, Los Angeles, CA 90095, USA |
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Abstract: | Virtually all cell surface proteins and many cell membrane lipids are glycosylated, creating a cell surface glycocalyx. The glycan chains attached to cell surface glycoproteins and glycolipids are complex structures with specific additions that determine functions of the glycans in cell–cell communication and cell sensing of the environment. One type of specific modification of cell surface glycans is decoration of glycan termini by sialic acids. On T cells, these terminal sialic acid residues are involved in almost every aspect of T cell fate and function, from cell maturation, differentiation, and migration to cell survival and cell death. The roles that sialylated glycans play in T cell development and function, including binding to specific sialic acid-binding lectins, are reviewed here. |
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Keywords: | C2GnT, core 2 β1,6-glucosaminyltransferase CD, cluster of differentiation antigen DN, double negative DP, double positive FucT, α1,3-fucosyltransferase Gal, galactose GalNAc, N-acetylgalactosamine Glc, glucose GlcNAc, N-acetylglucosamine GM1, Galβ1,3GalNAcβ1,4(NeuAcα2,3)Galβ1,4Glcβ1-Ceramide IFN, interferon IL, interleukin LacNAc (Galβ1,3GlcNAc, or Galβ1,4GlcNAc), N-acetyllactosamine Neu, neuraminidase Neu5Ac, N-acetylneuraminic acid Neu5Gc, N-glycolylneuraminic acid PNA, peanut agglutinin PSGL-1, P-selectin glycoprotein ligand-1 Sia, sialic acid sLeX, sialyl Lewis X ST3Gal, β-galactoside α2,3 sialyltransferase SNA, Sambucus Nigra agglutinin SP, single positive ST6Gal, β-galactoside α2,6 sialyltransferase ST6GalNAc, GalNAc α2,6 sialyltransferase ST8Sia, α2,8 sialyltransferase Th, T helper Treg, regulatory T cells |
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