Journal
GLYCOCONJUGATE JOURNAL
Volume 26, Issue 5, Pages 511-523Publisher
SPRINGER
DOI: 10.1007/s10719-008-9207-8
Keywords
Sialyl Lewis X; MECA-79; N-glycolylneuraminic acid; HECA-452 antibody; N-acetylneuraminic acid
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Funding
- NIH [CA48737, CA71932, HL85607, GM62116]
- Biotechnology and Biological Sciences Research Council BBSRC
- BBSRC Professor Fellow
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E-, P- and L-selectins critically function in lymphocyte recirculation and recruiting leukocytes to inflammatory sites. MECA-79 antibody inhibits L-selectin-mediated lymphocyte adhesion in several species and does not require sialic acid in its epitope. Many other antibodies, however, recognize human selectin ligands expressing N-acetylneuraminic acid but not mouse selectin ligands expressing N-glycolylneuraminic acid, suggesting that difference in sialic acid in sialyl Lewis X leads to differential reactivity. We found that HECA-452 and FH6 monoclonal antibodies bind Chinese hamster ovary (CHO) cells expressing N-acetylneuraminyl Lewis X oligosaccharide but not its N-glycolyl form. Moreover, synthetic N-acetylneuraminyl Lewis X oligosaccharide but not its N-glycolyl oligosaccharide inhibited HECA-452 and FH6 binding. By contrast, E-, P- and L-selectin bound to CHO cells regardless of whether they express N-acetyl or N-glycolyl form of sialyl Lewis X, showing that selectins have a broader recognition capacity than HECA-452 and FH-6 anti-sialyl Lewis x antibodies.
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