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Quantitative Differences in GlcNAc:ß13 and GlcNAc:ß1-4 Galactosyltransferase Activities between Human Colonic Adenocarcinomas and Normal Colonic Mucosa¹

Department of Biochemistry, Sasaki Institute, 2-2, Kanda-Surugadai, Chiyoda-ku, Tokyo 101 [A. S., T. O., K. Y.], and Second Department of Pathology, Kagoshima University School of Medicine, 8-35-1 Sakuragaoka, Kagoshima City 890 [H. K., S. Y., E. S.], Japan

The activities of GlcNAc:ß13 and GlcNAc:ß14 galactosyltransferases in normal human colonic mucosa and well or moderately differentiated colonic adenocarcinomas and their enzyme-kinetic characteristics were investigated. After UDP-[³H]galactose and N-linked type monoantennary oligosaccharides (GlcNAcß12Man13(6)Manß14GlcNAc) had been incubated with microsome fractions prepared from these tissues, the synthesized [³H]galactose-labeled oligosaccharides were analyzed by Ricinus communis agglutinin-I agarose chromatography, Streptococcus 6646K ß-galactosidase, Galß14-specific diplococcal ß-galactosidase, and Galß13GlcNAc-specific lacto-N-biosidase digestion. The ß-galactosyltransferases from normal mucosa synthesized both type 1 and type 2 chains at comparable levels, whereas those from adenocarcinomas predominantly synthesized type 2 chains. To our knowledge, this is the first quantitative estimation of GlcNAc:ß13 galactosyltransferase activity toward N-linked sugar chains. Furthermore, we compared the two galactosyltransferase activities in 10 normal mucosa and adenocarcinoma samples and found that while there existed similar levels of GlcNAc:ß14 galactosyltransferase activity in normal mucosa and adenocarcinomas, GlcNAc:ß13 galactosyltransferase activity apparently decreased from 0.67 ± 0.26 (normal mucosa) to 0.18 ± 0.11 nmol/min/mg of protein (adenocarcinomas). These results are consistent with those of comparative structural studies on N-linked sugar chains of carcinoembryonic antigen and its normal counterparts and suggest that in the process of differentiated carcinogenesis of human colonic tissues, the expression of GlcNAc:ß13 galactosyltransferase is negatively regulated.

¹ This work was supported by special funds from the Science and Technology Agency of the Japanese government and by funds from the Central Research Institute of Fukuoka University, Japan.

² To whom requests for reprints should be addressed.

Received 3/19/96. Accepted 5/31/96.

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