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Journal of Histochemistry and Cytochemistry, Vol. 49, 587-596, May 2001, Copyright © 2001, The Histochemical Society, Inc.

ARTICLE

Immunohistochemical Demonstration of {alpha}1,4-N-acetylglucosaminyltransferase that Forms GlcNAc{alpha}1,4Galß Residues in Human Gastrointestinal Mucosa

Mu Xia Zhanga, Jun Nakayamaa,b, Eiko Hidakaa, Seiko Kubotaa, Jing Yana, Hiroyoshi Otaa, and Minoru Fukudac
a Department of Laboratory Medicine, Shinshu University School of Medicine and Central Clinical Laboratories, Shinshu University Hospital, Matsumoto, Japan
b Institute of Organ Transplants, Reconstructive Medicine, and Tissue Engineering, Shinshu University Graduate School of Medicine, Matsumoto, Japan
c Glycobiology Program, the Burnham Institute, La Jolla, California

Correspondence to: Jun Nakayama, Central Clinical Laboratories, Shinshu University Hospital, Asahi 3-1-1, Matsumoto 390-8621, Japan. E-mail: jun@hsp.md.shinshu-u.ac.jp

{alpha}1,4-N-acetylglucosaminyltransferase ({alpha}4GnT) is a glycosyltransferase that mediates transfer of GlcNAc to ßGal residues with {alpha}1,4-linkage, forming GlcNAc{alpha}1-> 4Galß->R structures. In normal human tissues, glycoproteins having GlcNAc{alpha}1->4Galß->R structures at non-reducing terminals are exclusively limited to the mucins secreted from glandular mucous cells of gastric mucosa, Brunner's gland of duodenum, and accessory gland of pancreaticobiliary tract. Recently, we have isolated a cDNA encoding human {alpha}4GnT by expression cloning. Although {alpha}4GnT plays a key role in producing this unique glycan in vitro, the actual localization of {alpha}4GnT was not determined. In this study we examined the localization of {alpha}4GnT in various human tissues, including gastrointestinal mucosa, using a newly developed antibody against human {alpha}4GnT. The specificity of the antibody was confirmed by analyses of human gastric adenocarcinoma AGS cells transfected by {alpha}4GnT cDNA. Expression of {alpha}4GnT was largely associated with the Golgi region of mucous cells that produce the mucous glycoproteins having GlcNAc{alpha}1->4Galß->R, such as the glandular mucous cells of stomach and Brunner's gland. An immunoprecipitation experiment disclosed that two distinct mucin proteins, MUC5AC and MUC6 present in gastric mucin, carried the GlcNAc{alpha}1->4Galß->R structures. These results indicate that {alpha}4GnT is critical to form the mucous glycoproteins having GlcNAc{alpha}1->4Galß->R on MUC6 and MUC5AC in vivo.

(J Histochem Cytochem 49:587–596, 2001)

Key Words: glycosyltransferase, mucin core protein, O-glycan


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