Abstract
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.
Original language | English |
---|---|
Pages (from-to) | 511-523 |
Number of pages | 13 |
Journal | Glycoconjugate Journal |
Volume | 26 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2009 Jul |
Externally published | Yes |
Keywords
- HECA-452 antibody
- MECA-79
- N-acetylneuraminic acid
- N-glycolylneuraminic acid
- Sialyl Lewis X
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology