| Comparative Study of the Asparagine-Linked Sugar Chains of Human Lipocalin-Type Prostaglandin D Synthase Purified from Urine and Amniotic Fluid, and Recombinantly Expressed in Chinese Hamster Ovary Cells (2000) | |||||||||||||
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| Lipocalin-type prostaglandin D synthase (L-PGDS) is a highly glycosylated member of the lipocalin gene family and is secreted into various human body fluids. We comparatively analyzed the structures of asparagine-linked sugar chains of human L-PGDS produced by recombinant Chinese hamster ovary cells and naturally occurring human urine and amniotic fluid. After the sugar chains were liberated by hydrazinolysis followed by N-acetylation, they were derivatized with 2-aminobenzamide. All of the sugar chains of three L-PGDSs occur as biantennary complex-type sugar chains. Most of the sugar chains of three samples were fucosylated on the inner most N-acetylglucosamine residue. Although the sugar chains of the recombinant L-PGDS do not contain any bisecting N-acetylglucosamine residues, 58% and 34% of the fucosylated-sugar chains of amniotic fluid and urine L-PGDSs, respectively, contain bisecting N-acetylglucosamine residues. The sialic acid residues occur solely as Siaα2→3Gal groups of the recombinant L-PGDS; the sialic acid residues of other L-PGDS occur as both Siaα2→3Gal and Siaα2→6Gal groups. Variations in L-PGDS glycosylation may prove useful as markers to further elucidate the role of L-PGDS giycoforms in different tissues. | |||||||||||||
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