1992
DOI: 10.1016/0006-291x(92)90697-j
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Comparison of L-selectin and E-selectin ligand specificities: The L-selectin can bind the E-selectin ligands Sialyl Lex and Sialyl Lea

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Cited by 173 publications
(84 citation statements)
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“…sialyl-Lewis x (sLe X )] on discrete macromolecules [2]. CLA + T cells are detected most notably by the mAb HECA-452, which binds glycans such as sLe X [3][4][5]. CLA + T cells can be stained by soluble recombinant E-selectin-immunoglobulin chimeric proteins, which are comprised of the extracellular region of E-selectin and the Fc region of an immunoglobulin (E-selectin/Fc)] [6][7][8][9].…”
Section: Introductionmentioning
confidence: 99%
“…sialyl-Lewis x (sLe X )] on discrete macromolecules [2]. CLA + T cells are detected most notably by the mAb HECA-452, which binds glycans such as sLe X [3][4][5]. CLA + T cells can be stained by soluble recombinant E-selectin-immunoglobulin chimeric proteins, which are comprised of the extracellular region of E-selectin and the Fc region of an immunoglobulin (E-selectin/Fc)] [6][7][8][9].…”
Section: Introductionmentioning
confidence: 99%
“…The former mediates binding to thrombin activated platelets (23) while the latter permits attachment to E-selectin transfectants and cytokine-treated HUVE (24). These ligands have not been characterized but are presumably related to the sialylated, fucosylated binding sites identified on neutrophils and cell lines (25)(26)(27)(28)(29)(30)(31). The j31 integrin VLA-4 (CD49d) is constitutively expressed, enabling monocytes to interact with a second, cytokine-induced endothelial adhesion molecule termed VCAM-1 (24).…”
Section: Introductionmentioning
confidence: 99%
“…FucT-III, FucT-IV, FucT-V, FucT-VI, and FucT-IX can synthesize the Le x structure, while FucT-VII cannot. FucT-III, FucT-IV, FucT-V, FucT-VI, and FucT-VII can synthesize the sialyl Le x structure, which is the minimal ligand for all three selectins known as cell adhesion molecules for leukocyte-endothelium interaction (5,13,31). Detailed analysis of the substrate specificity of the polylactosamine acceptor has revealed Fuc-TIX to have more-efficient activity for synthesis of the Le x carbohydrate epitope than other ␣1,3FUTs (34) and to fucosylate the remote internal N-acetyllactosamine units of ␣2,3-sialylated polylactosamine (47).…”
mentioning
confidence: 99%