2008
DOI: 10.1007/s10719-008-9122-z
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Anti-oligosaccharide antibodies as tools for studying sulfated sialoglycoconjugate ligands for siglecs and selectins

Abstract: Several sulfated sialoglycoconjugates have recently been shown to serve as ligands for selectins and siglecs. For instance, alpha2-->3 sialylated 6-sulfo-Lewis x was found to serve as a ligand for selectins on skin-homing helper memory T cells, and alpha2-->6 sialylated 6-sulfo-LacNAc to be a preferred ligand for CD22/siglec-2 on human naïve B cells. Monoclonal antibodies specific to sulfated sialoglycoconjugates are effective tools to dissect these ligands on minor subsets of human leukocytes.

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Cited by 17 publications
(15 citation statements)
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References 23 publications
(20 reference statements)
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“…A complete list of glycans is described in Fig. 5 using the appropriate markers to distinguish GC B-cells (28). In humans, loss of the high affinity human CD22 ligand occurs through loss of ␣2-6-linked sialosides bearing a 6-O-sulfate modification on GlcNAc residues.…”
Section: Discussionmentioning
confidence: 99%
“…A complete list of glycans is described in Fig. 5 using the appropriate markers to distinguish GC B-cells (28). In humans, loss of the high affinity human CD22 ligand occurs through loss of ␣2-6-linked sialosides bearing a 6-O-sulfate modification on GlcNAc residues.…”
Section: Discussionmentioning
confidence: 99%
“…It is also known that P-selectin is expressed on activated platelets. However, none of the conventional anti-sLe x monoclonal antibodies (mAbs), except for one mAb, react with the high endothelial venules (HEVs) in mouse or rat peripheral lymph nodes (PLNs), where L-selectin ligands are expressed (4,5). This situation is probably due to the fact that a large proportion of the terminal sialic acid in WT mice is in the form of N-glycolylneuraminic acid (Neu5Gc), whereas most existing mAbs react with glycans modified with N-acetylneuraminic acid (Neu5Ac) (4).…”
mentioning
confidence: 99%
“…Indeed, 6S-Gal has been found in O-linked glycans in both the L-selectin receptor glycoprotein GlyCAM-1 and MUC1 secreted from breast cancer cells (6,7). To date, facile detection of this glycoepitope has been greatly hampered as no specific monoclonal antibodies have been available (8,9). Although several endogenous lectins, including Langerin, Siglec-8, and Siglec-F, have been shown to recognize 6S-Gal-containing glycans (10 -12), precise distribution of their ligand glycans in vivo and identification of their carrier proteins remain to be determined.…”
mentioning
confidence: 99%