Interaction of platelet endothelial cell adhesion molecule (PECAM) with α2,6-sialylated glycan regulates its cell surface residency and anti-apoptotic role
| Autor: | Ayako Kurimoto, Katsunori Tanaka, Rie Imamaki, Yoshiki Yamaguchi, Hiromune Ando, Kazuko Ogawa, Naoyuki Taniguchi, Makoto Kiso, Hideharu Ishida, Nana Kawasaki, Masaki Kato, Noritaka Hashii, Shinobu Kitazume |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Glycan
Angiogenesis Cell Survival Oligosaccharides Glycobiology and Extracellular Matrices Apoptosis Sialic acid binding Glycocalyx Biochemistry chemistry.chemical_compound Mice Polysaccharides Lectins Human Umbilical Vein Endothelial Cells Animals Humans Cell adhesion Molecular Biology Platelet Endothelial Cell Adhesion Molecule biology Chemistry Cell Biology N-Acetylneuraminic Acid Cell biology Endothelial stem cell carbohydrates (lipids) Platelet Endothelial Cell Adhesion Molecule-1 embryonic structures biology.protein cardiovascular system N-Acetylneuraminic acid Protein Binding |
| Zdroj: | The Journal of biological chemistry. 289(40) |
| ISSN: | 1083-351X |
| Popis: | The luminal sides of vascular endothelial cells are heavily covered with a so-called glycocalyx, but the precise role of the endothelial glycocalyx remains unclear. Our previous study showed that N-glycan α2,6-sialylation regulates the cell surface residency of an anti-apoptotic molecule, platelet endothelial cell adhesion molecule (PECAM), as well as the sensitivity of endothelial cells toward apoptotic stimuli. As PECAM itself was shown to be modified with biantennary N-glycans having α2,6-sialic acid, we expected that PECAM would possess lectin-like activity toward α2,6-sialic acid to ensure its homophilic interaction. To verify this, a series of oligosaccharides were initially added to observe their inhibitory effects on the homophilic PECAM interaction in vitro. We found that a longer α2,6-sialylated oligosaccharide exhibited strong inhibitory activity. Furthermore, we found that a cluster-type α2,6-sialyl N-glycan probe specifically bound to PECAM-immobilized beads. Moreover, the addition of the α2,6-sialylated oligosaccharide to endothelial cells enhanced the internalization of PECAM as well as the sensitivity to apoptotic stimuli. Collectively, these findings suggest that PECAM is a sialic acid binding lectin and that this binding property supports endothelial cell survival. Notably, our findings that α2,6-sialylated glycans influenced the susceptibility to endothelial cell apoptosis shed light on the possibility of using a glycan-based method to modulate angiogenesis. |
| Databáze: | OpenAIRE |
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