Differential Expression of α2,6-Sialyltransferase in Colon Tumors Recognized by a Monoclonal Antibody

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Abstract
It has been reported that α2,6-sialyltransferase (α2,6-ST; E.C. 2.4.99.1) activity is associated with cellular differentiation. To define its role in colon carcinoma differentiation, we have generated murine monoclonal antibodies (MAb) against α2,6-sialyltransferase. The MAb, designated 6B9 of IgM isotype, showed strong reactivity with the purified and crude α2,6-ST by ELISA and dot blot assays. Western blotting with MAb 6B9 identified purified α2,6-ST of MW 47 kDa and the same MW protein from rat and human liver extracts. The MAb also reacted with two other liver proteins of approximate MW 65 and 100 kDa. Immunoperoxidase studies with formalin-fixed paraffin-embedded tissues showed that MAb 6B9 reacts with liver tissues, the staining of hepatocytes was granular and cytoplasmic. There was a distinct pattern of zonal distribution of this enzyme in hepatocytes located particularly in the portal areas of the liver corresponding to zone 1. Normal colon (100%) and hyperplastic polyps (100%) showed very weak to no reactivity. Adenomas (100%) demonstrated moderate reactivity, while the poor (33%), moderate (100%) and well-differentiated (80%) colon adenocarcinomas showed strong reactivity. Results suggest that α2,6-ST is associated with the differentiation state of colon tumors.

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