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Glycobiology, Vol 9, 915-925, Copyright © 1999 by Oxford University Press

Characterization of human vascular endothelial cadherin glycans [In Process Citation]

H Geyer, R Geyer, M Odenthal-Schnittler and HJ Schnittler
Institute of Biochemistry, Justus-Liebig-Universitat Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany and Institute of Physiology, Westfalische Wilhelms-Universitat Munster, Robert-Koch- Strasse 27a, D-48149 Munster, Ger.

The glycosylation pattern of human vascular endothelial cadherin (VE- cadherin), purified from cultured human umbilical cord vein endothelial cells, was analyzed. VE-cadherin was metabolically radiolabeled with d- [6-(3)H]glucosamine, isolated by immunoprecipitation, purified by SDS- PAGE and in-gel digested with endoproteinase Asp N. Oligosaccharides were sequentially released from resulting glycopeptides and analyzed by chromatographic profiling. The results revealed that VE-cadherin carries predominantly sialylated diantennary and hybrid-type glycans in addition to some triantennary and high mannose-type species. Highly branched, tetraantennary oligosaccharides were found in trace amounts only. Immunohistochemical labeling of VE-cadherin and sialic acids displayed a codistribution along the intercellular junctions in endothelial cells of human umbilical arteries, veins, and cultured endothelial monolayers. Ca(2+)-depletion, performed on cultured endothelial cells, resulted in a reversible complete disappearance of VE-cadherin and of almost all sialic acid staining from the junctions. Sialidase treatment of whole cells caused a change of VE-cadherin immunofluorescence from a continuous and netlike superstructural organization to a scattered inconsistent one. Hence, cell surface sialic acids might play a role in VE-cadherin organization.
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