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Sialic acids in T cell development and function
Authors:Shuguang Bi  Linda G. Baum
Affiliation:Department of Pathology and Laboratory Medicine, UCLA School of Medicine, 10833 LeConte Ave, Los Angeles, CA 90095, USA
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.
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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