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Expression of α1‐6 fucosyltransferase in rat tissues and human cancer cell lines
Author(s) -
Miyoshi Eiji,
Uozumi Naofumi,
Noda Katsuhisa,
Hayashi Norio,
Hori Masatsugu,
Taniguchi Naoyuki
Publication year - 1997
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19970917)72:6<1117::aid-ijc29>3.0.co;2-#
Subject(s) - fucosyltransferase , cell culture , biology , cancer , human cell , cancer research , gene , genetics
GDP‐L‐Fuc: N ‐acetyl‐β‐d‐glucosaminide α1‐6 fucosyltransferase (α1‐6FucT) catalyzes the transfer of a fucosyl residue from GDP‐fucose to the asparagine‐linked GlcNAc residue of complex N ‐glycans via α1‐6 linkage. These oligosaccharide structures are essential for the attachment of polysialic acid to the neural‐cell‐adhesion molecule, and its levels are useful for the differential diagnosis of hepatocellular carcinomas with respect to the microheterogeneity of α‐fetoprotein. We have been successful in the purification and cDNA cloning of α1‐6FucT from porcine brain and from a human gastric‐cancer cell line. In the present study, mRNA expression of α1‐6FucT in various rat tissues and human cancer cell lines was examined, along with the expression of α1‐6FucT mRNA and the induction by treatment with several cytokines. Northern‐blot analysis indicated high expression levels of α1‐6FucT in brain and gastrointestinal‐tract tissues of normal rats, as well as for a number of lung‐cancer, gastric‐cancer and colon‐cancer cell lines. Although various cytokines did not induce α1‐6FucT mRNA, differentiation of a tumor cell enhanced the mRNA by 2‐ to 3‐fold. These results may provide new insight into studies on α1‐6FucT in terms of carcinogenesis or differentiation. Int. J. Cancer 72:1117–1121, 1997. © 1997 Wiley‐Liss, Inc.