Glycobiology, 2002, Vol. 12, No. 1 33-45
© 2002 Oxford University Press
Glycoprotein biosynthesis in porcine aortic endothelial cells and changes in the apoptotic cell population
2Department of Medicine, Division of Rheumatology, and Department of Biochemistry, Queen’s University, Kingston, K7L 3N6, Ontario, Canada; 3Arius Research, 55 York Street, 16th Floor, Toronto, M5J 1R7, Ontario, Canada; 4Hospital for Sick Children, 555 University Avenue, Toronto, M5G 1X8, Ontario, Canada; and 5Institut für Org. Chemie, Martin-Luther-King Platz 6, 20146 Hamburg, Germany
Porcine aortic endothelial cells (PAECs) produce glycoproteins with important biological functions, such as the control of cell adhesion, blood clotting, blood pressure, the immune system, and apoptosis. Cell surface glycoproteins play important roles in these biological activities. To understand the control of cell surface glycosylation, we elucidated biosynthetic pathways leading to N- and O-glycans in PAECs. Based on the enzyme activities, PAECs should be rich in complex biantennary N-glycans. In addition, the enzymes synthesizing complex O-glycans with core 1 and 2 structures are present in PAECs. The first enzyme of the O-glycosylation pathway, polypeptide GalNAc-transferase, was particularly active. Its specificity toward synthetic peptide substrates was found to be similar to that of purified bovine colostrum enzyme T1. A significant fraction of PAECs treated with tumour necrosis factor 
or human serum detached from the culture plate, and most of these cells were apoptotic. The apoptotic cell population exhibited decreased core 2 ß6-GlcNAc-transferase activity. In contrast, the activities of core 1 ß3-Gal-transferase, which synthesizes O-glycan core 1, and of 3-sialyltransferase (O), which sialylates core 1, were increased in apoptotic PAECs. Thus, apoptotic PAECs are predicted to have fewer complex O-glycans and a higher proportion of short, sialylated core 1 chains.
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