2010
DOI: 10.1093/glycob/cwq083
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Human L-selectin preferentially binds synthetic glycosulfopeptides modeled after endoglycan and containing tyrosine sulfate residues and sialyl Lewis x in core 2 O-glycans

Abstract: Endoglycan is a mucin-like glycoprotein expressed by endothelial cells and some leukocytes and is recognized by L-selectin, a C-type lectin important in leukocyte trafficking and extravasation during inflammation. Here, we show that recombinant L-selectin and human T lymphocytes expressing L-selectin bind to synthetic glycosulfopeptides (GSPs). These synthetic glycosulfopeptides contain 37 amino acid residues modeled after the N-terminus of human endoglycan and contain one or two tyrosine sulfates (TyrSO(3)) a… Show more

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Cited by 17 publications
(20 citation statements)
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“…31 Moreover, the differences in the interaction between MM cells and normal plasma cells were apparently due to lower expression of PSGL-1 in normal plasma cells or potentially because of different glycosylation patterns of the PSGL-1, which is known to alter binding of selectins to the ligand. 32,33 To confirm the role of PSGL-1 in the interaction of selectins with MM cells, we knocked down PSGL-1 in MM1s cells using siRNA (as verified by flow cytometry; supplemental Figure 2). Knock-down of PSGL-1 decreased the high level of interaction of L-and P-selectins with MM cells (the effect was stronger for interaction of P-selectin on MM cells).…”
Section: Role Of Psgl-1 In the Interaction Of Recombinant Selectins Wmentioning
confidence: 99%
“…31 Moreover, the differences in the interaction between MM cells and normal plasma cells were apparently due to lower expression of PSGL-1 in normal plasma cells or potentially because of different glycosylation patterns of the PSGL-1, which is known to alter binding of selectins to the ligand. 32,33 To confirm the role of PSGL-1 in the interaction of selectins with MM cells, we knocked down PSGL-1 in MM1s cells using siRNA (as verified by flow cytometry; supplemental Figure 2). Knock-down of PSGL-1 decreased the high level of interaction of L-and P-selectins with MM cells (the effect was stronger for interaction of P-selectin on MM cells).…”
Section: Role Of Psgl-1 In the Interaction Of Recombinant Selectins Wmentioning
confidence: 99%
“…Potential ligands include heparan sulfate [30][31][32] and sulfated ligands on TNF-␣-stimulated microvascular and macrovascular endothelial cells, 33,34 P-selectin glycoprotein ligand-1, 35 and endoglycan. 36 L-selectin interaction with P-selectin glycoprotein ligand-1 also facilitates neutrophil-neutrophil interactions or "secondary capture" of cells, resulting in pavementing of neutrophils. 37,38 In 2005, we provided genetic evidence suggesting that endothelial heparan sulfate facilitates neutrophil rolling on different endothelial beds based on inactivation of Ndst1 in the endothelium in Ndst1 f/f Tie2Cre ϩ mice.…”
Section: Discussionmentioning
confidence: 99%
“…There are three groups of L-selectin ligands: the orthodox ligands with 6-sulfo sLe x structure on sialomucins and glycoproteins (i.e. GlyCAM-1 (glycosylation cell adhesion molecule-1), CD34, podocalyxin, and MAdCAM-1 (mucosal vascular addressin)); ligands with clusters of sLe x and Tyr-SO 3 like PSGL-1 (P-selectin-glycoprotein ligand-1) and endoglycan; and proteoglycans with predominantly heparan or chondroitin sulfate modifications (57)(58)(59). However, lubricin is different from those identified L-selectin ligands.…”
Section: Discussionmentioning
confidence: 99%