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6-O-Sulfation of beta-GlcNAc is an initial step in the biosynthesis of N-linked and O-linked sulfated glycans, which are widely distributed in colonic tissues. However, the biochemical mechanism of this sulfation in human colonic carcinogenesis was still unclear. In this study, we found two types of GlcNAc:--&gt;6sulfotransferases (SulT) in human colonic adenocarcinomas and the adjacent normal mucosa, and we determined their enzymatic characteristics. One SulT, named SulT-a, was present in the adjacent normal mucosa and in non-mucinous adenocarcinomas, whereas the other SulT, named SulT-b, was present only in mucinous adenocarcinomas and adenocarcinomas with a mucinous component. SulT-a preferentially acted on Galbeta1--&gt;3(GlcNAcbeta1--&gt;6)GalNAc(alpha1)-p-nitrophenyl (pNP) and GlcNAcbeta1--&gt;2Man, whereas SulT-b could act not only on these two glycans, but also on GlcNAcbeta1--&gt;3GalNAc(alpha1)-pNP and GlcNAcbeta1--&gt;3Galbeta1--&gt;4Glc. The levels of SulT-a activity were significantly lower in non-mucinous adenocarcinomas than in the adjacent mucosa. In contrast, SulT-b was expressed in mucinous adenocarcinomas and in adenocarcinomas with a mucinous component. These results indicate that there are at least two types of GlcNAc:--&gt;6SulT, SulT-a and -b, in colonic mucosa and adenocarcinomas, and that the occurrence of these enzymes is closely correlated with colonic cancer and the presence of areas of mucin accumulation.

glycobiology

Biochemical differences between two types of N-acetylglucosamine:-&gt;6sulfotransferases in human colonic adenocarcinomas and the adjacent normal mucosa: specific expression of a GlcNAc:-&gt;6sulfotransferase in mucinous adenocarcinoma