Abstract
4-Methylumbelliferyl-beta-D-xyloside (Xyl-MU) was added to the medium of cultured human skin fibroblasts. After incubation, the culture medium was pooled, and the Xyl-MU-induced oligosaccharides in the medium were purified by gel filtration chromatography. A novel Xyl-MU derivative was obtained, in addition to the previously reported Xyl-MU derivatives such as Gal-Gal-Xyl-MU, Gal-Xyl-MU, Sia-Gal-Xyl-MU, GlcA-Xyl-MU, and Xyl-Xyl-MU. The novel Xyl-MU derivative was purified using gel-filtration chromatography and high performance liquid chromatography and then subjected to carbohydrate composition analysis, enzymic digestion, Smith degradation, and ion spray mass spectrometric analysis. The results indicated that it was sulfate-O-3GlcA beta 1-4Xyl beta 1-MU. The structure of the nonreducing terminal of this Xyl-MU-induced oligosaccharide was the same as that of the oligosaccharide chain of a human peripheral nerve-derived glycolipid, reactive with the mouse monoclonal antibody HNK-1, and this Xyl-MU-induced oligosaccharide also reacted with HNK-1. These results suggest that the oligosaccharide, which is structurally identical to that of human peripheral nerve-derived glycolipid synthesized by nervous tissue and related to cell adhesion, is synthesized also by mesenchymal cells.
Highlights
From the +Department of Biochemistry, Hirosaki University School of Medicine, 5 Zaifu-cho, Hirosaki 036, Japan and the §Research Institute for Glycotechnology, 82-4 Zaifu-cho, Hirosaki 036, Japan
The structure of the nonreducing terminal of this Xyl-MU-induced oligosaccharide was the same as that ofthe oligosaccharide chain of a human peripheral nerve-derived glycolipid, reactive with the mouse monoclonal antibody HNK-l, and this Xyl-MUinduced oligosaccharide reacted with HNK-l
The structure of the nonreducing terminal site of the oligosaccharide was the same as that of the oligosaccharide chain of a human peripheral nerve-derived glycolipid, which reacts with a mouse monoclonal antibody, HNK-1 [14,15], and this novel Xyl-MU-induced oligosaccharide was found to be reactive with HNK-l
Summary
The structure of the nonreducing terminal of this Xyl-MU-induced oligosaccharide was the same as that ofthe oligosaccharide chain of a human peripheral nerve-derived glycolipid, reactive with the mouse monoclonal antibody HNK-l, and this Xyl-MUinduced oligosaccharide reacted with HNK-l. These results suggest that the oligosaccharide, which is structurally identical to that of human peripheral nervederived glycolipid synthesized by nervous tissue and related to cell adhesion, is synthesized by mesenchymal cells. The structure of the nonreducing terminal site of the oligosaccharide was the same as that of the oligosaccharide chain of a human peripheral nerve-derived glycolipid, which reacts with a mouse monoclonal antibody, HNK-1 [14,15], and this novel Xyl-MU-induced oligosaccharide was found to be reactive with HNK-l
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