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- W81689208 endingPage "25" @default.
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- W81689208 abstract "The selectins are type 1 membrane glycoproteins that have an N-terminal C-type lectin domain, followed by an epidermal growth factor (EGF)-like motif, a series of short consensus repeats, a transmembrane domain, and a cytoplasmic tail (see Chapters 2 and 3). Leukocytes express L-selectin, whereas activated platelets express P-selectin and activated endothelial cells express P-selectin and E-selectin. Each selectin mediates leukocyte rolling to vascular surfaces through Ca2+-dependent interactions of the lectin domain with cell-surface glycoconjugates. All selectins bind with low affinity to glycans with terminal components that include α2-3-linked sialic acid and a1-3-linked fucose, typified by the sialyl Lewis x (sLex) determinant (NeuAcα2-3Galβ1-4[Fucα1-3]GlcNAcβ1-R) [1, 2]. Crystal structures of sLex bound to the lectin domains of P- and E-selectin reveal a network of interactions between the fucose, a single Ca2+ ion, and several amino acids, including those that coordinate the Ca2+ [3]. This explains the Ca2+ requirement for binding. Targeted disruption of the α1-3-fucosyltransferases Fuc-TIV and Fuc-TVII in mice eliminates selectin-mediated leukocyte trafficking [4, 5]. This demonstrates that physiologically relevant selectin ligands require al-3-linked fucose. However, there is abundant evidence that selectins bind better to some glycoproteins modified with sLex-capped glycans than to others [1, 2]. This chapter focuses on the most thoroughly characterized of these glycoproteins: P-selectin glycoprotein ligand-1 (PSGL-1), which mediates important biological functions through interactions with each of the selectins." @default.
- W81689208 created "2016-06-24" @default.
- W81689208 creator A5043920114 @default.
- W81689208 date "2007-10-26" @default.
- W81689208 modified "2023-09-25" @default.
- W81689208 title "P-selectin glycoprotein ligand-1 (PSGL-1)" @default.
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