Glycobiology Advance Access published online on May 25, 2006
Glycobiology, doi:10.1093/glycob/cwl005
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1 Division of Oncological Pathology, Aichi Cancer Center Research Institute
* To whom correspondence should be addressed.
Article
Apical Golgi localization of N,N’-diacetyllactosediamine synthase,
Yuzuru Ikehara 1,
Takashi Sato 2,
Toru Niwa 1,
Sachiko Nakamura 3,
Masanori Gotoh 2,
Sanae Kabata Ikehara 1,
Katsue Kiyohara 2,
Chihiro Aoki 1,
Toshie Iwai 2,
Hayao Nakanishi 1,
Jun Hirabayashi 3,
Masae Tatematsu 1,
and
Hisashi Narimatsu 4 *
4GalNAc-T3, is responsible for LacdiNAc expression on gastric mucosa
2 Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
3 Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology
4 Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8568, Japan
Hisashi Narimatsu, E-mail: h.narimatsu{at}aist.go.jp
Abstract 
1,4-N-acetylgalactosaminyltransferase III (4GalNAc-T3), which was recently cloned and identified, exhibits GalNAc transferase activity toward a GlcNAc residue with 1,4-linkage, forming the N,N’-diacetyllactosediamine, GalNAc1,4GlcNAc (LacdiNAc or LDN).Though LacdiNAc has not been found in the gastric mucosa, a large amount of transcript was detected in our previous study. To increase our knowledge of 4GalNAc-T3 expression and its product LacdiNAc, we examined the exact localization of 4GalNAc-T3 in human gastric mucosa using a newly developed antibody, mAb K1356. This antibody specifically detected the enzyme that trasfected the 4GalNAc-T3 gene into MKN45 cells, and the terminal GalNAc epitope yielded on the cell surface was recognized by a lectin, Wisteria floribunda agglutinin (WFA). 4GalNAc-T3 was localized in the supra-nuclear region of surface mucous cells in gastric mucosa, and WFA positively stained the mucins secreted by the cells. In contrast, in the cells of the glandular compartment in the fundic glands and a few cells in the pyloric glands, 4GalNAc-T3 was observed in the basolateral position of nucleus, where no WFA reactivity was detected. The anti-Tn (GalNAc
-O-Ser/Thr) antibody staining did not overlap with the WFA staining. From measuring the binding activity of WFA using automated frontal affinity chromatography, WFA was found to bind most strongly LacdiNAc among the sugar chains examined. Neither 4GalNAc-T3 nor WFA-positive staining was detected in intestinal metaplastic cells. These results suggest that the supra-nuclear expression of 4GalNAc-T3 is essential for the formation of LacdiNAc on the surface mucous cells, and that LacdiNAc and 4GalNAc-T3 are novel differentiation markers of surface mucous cells in the gastric mucosa.4GalNAc-T3 expression.
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