2014
DOI: 10.1074/jbc.m114.555888
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NEU1 Sialidase Regulates the Sialylation State of CD31 and Disrupts CD31-driven Capillary-like Tube Formation in Human Lung Microvascular Endothelia

Abstract: Background: Endothelia express NEU1 sialidase and undergo changes in sialylation during angiogenesis. Results: CD31 is a NEU1 substrate, and NEU1 disrupts endothelial cell capillary-like tube formation. Conclusion: NEU1 works through its substrate, CD31, to dysregulate angiogenesis. Significance: Human NEU1 is the first sialidase found to regulate angiogenesis, and the CD31 sialylation state dictates its ability to influence endothelial cell differentiation and tube formation.

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Cited by 67 publications
(66 citation statements)
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“…In contrast, NEU1 involvement in cellular regulatory mechanisms has been demonstrated only recently concomitantly with the discovery of a plasma membrane-associated pool of NEU1 in several cell types. At the cell surface, NEU1 has been shown to regulate sialylation of several receptors and their underlying signaling pathways91012141516171819. However, the mechanisms through which NEU1 might translocate to the plasma membrane, its association with PPCA, its orientation and organization within the membrane are poorly understood and subject to several discrepancies.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…In contrast, NEU1 involvement in cellular regulatory mechanisms has been demonstrated only recently concomitantly with the discovery of a plasma membrane-associated pool of NEU1 in several cell types. At the cell surface, NEU1 has been shown to regulate sialylation of several receptors and their underlying signaling pathways91012141516171819. However, the mechanisms through which NEU1 might translocate to the plasma membrane, its association with PPCA, its orientation and organization within the membrane are poorly understood and subject to several discrepancies.…”
Section: Discussionmentioning
confidence: 99%
“…At the plasma membrane, NEU1 has been shown to be required for signal transduction and elastogenesis through the elastin receptor complex91011 and to be involved in the modulation of insulin receptor signaling1213, regulation of integrin beta 414, TLR415, Trk A16, PDGF-BB and IGF receptors17, EGF and MUC1 receptors18 and more recently CD3119. Consequently, NEU1 now emerges not only as a catabolic enzyme but also as a key actor involved in cell signaling regulation20.…”
mentioning
confidence: 99%
“…Interestingly, homophilic binding ability was linked to the presence of α2,6-sialic acid modified glycan residues, which appeared to be necessary for the ability of PECAM-1 to traffic normally to the cell surface and confer a cell survival advantage to endothelial cells in culture [46]. α2,6-linked sialic acids were also shown to be necessary for endothelial cells to form tube-like structures in vitro [47]. An important caveat of each of these studies is that they were performed using primarily murine cells and murine PECAM-1, More recent studies [48] have identified important species-specific requirements for PECAM-1-mediated homophilic binding, as α2,3- but not α2,6-, sialylated glycans, appear to participate in PECAM-1/PECAM-1 interactions in humans.…”
Section: Lectin-like Properties Of Pecam-1mentioning
confidence: 99%
“…[6][7][8] PECAM-1-mediated homophilic interactions are known to be essential for concentrating PECAM-1 at endothelial cell intercellular junctions, 9,10 where it functions to maintain vascular integrity under conditions of inflammatory or thrombotic stress, [11][12][13][14][15] in survival signaling in endothelial cells subjected to apoptotic stimuli, 16,17 and in mediating leukocyte/endothelial cell interactions during the process of diapedesis. [18][19][20] Mutagenesis studies have implicated amino acids on either side of the face of IgD1 in homophilic binding, 8 however, the spatial orientation of this domain, the role that IgD2 plays in positioning IgD1 to participate in PECAM-1 homophilic interactions, and the contribution of its sialylated glycans to homophilic PECAM-1/ PECAM-1 interactions [21][22][23] remain to be critically explored. Complicating things further, PECAM-1 forms dimers and oligomers within the plane of the plasma membrane.…”
Section: Introductionmentioning
confidence: 99%