ArticleThe Journal of biological chemistry2014
Interaction of platelet endothelial cell adhesion molecule (PECAM) with α2,6-sialylated glycan regulates its cell surface residency and anti-apoptotic role.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Anti-PECAM-1 antibodies: another tool for visualization of Reissner´s fiber and the subcommissural organ in rat central nervous system.Brain structure & function · 2026Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Review
- Gemcitabine alters sialic acid binding of the glycocalyx and induces inflammatory cytokine production in cultured endothelial cells.Medical molecular morphology · 2023Article
- ST6Gal1: Oncogenic signaling pathways and targets.Frontiers in molecular biosciences · 2022Review
- Review
- The manifold roles of sialic acid for the biological functions of endothelial glycoproteins.Glycobiology · 2020Review
- Glycosylation in the Tumor Microenvironment: Implications for Tumor Angiogenesis and Metastasis.Cells · 2019Review
- Glycosylation controls cooperative PECAM-VEGFR2-β3 integrin functions at the endothelial surface for tumor angiogenesis.Oncogene · 2018Article
- The Deletion of Endothelial Sodium Channel α (αENaC) Impairs Endothelium-Dependent Vasodilation and Endothelial Barrier Integrity in EndotoxemiaFrontiers in pharmacology · 2018Article
- Contribution of vascular endothelial growth factor receptor-2 sialylation to the process of angiogenesis.Oncogene · 2017Article
- In Situ Ligation of High- and Low-Affinity Ligands to Cell Surface Receptors Enables Highly Selective Recognition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017Article
- Platelet Endothelial Cell Adhesion Molecule-1 and Oligodendrogenesis: Significance in Alcohol Use Disorders.Brain sciences · 2017Review
- Biological roles of glycans.Glycobiology · 2017Review
- The Role of Sialylated Glycans in Human Platelet Endothelial Cell Adhesion Molecule 1 (PECAM-1)-mediated Trans Homophilic Interactions and Endothelial Cell Barrier Function.The Journal of biological chemistry · 2016Article
- Endothelial functions of platelet/endothelial cell adhesion molecule-1 (CD31).Current opinion in hematology · 2016Review
- Structural basis for PECAM-1 homophilic binding.Blood · 2016Article
- Cell surface and in vivo interaction of dendrimeric N-glycoclusters.Glycoconjugate journal · 2015Review
- N-glycosylation controls the function of junctional adhesion molecule-A.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.