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Prepublished online as a Blood First Edition Paper on December 5, 2002; DOI 10.1182/blood-2002-09-2838. This Article Full Text (PDF) All Versions of this Article: 2002-09-2838v1 101/7/2870    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Inaba, N. Articles by Narimatsu, H. Search for Related Content PubMed PubMed Citation Articles by Inaba, N. Articles by Narimatsu, H. Social Bookmarking                   What's this? Submitted September 18, 2002 Accepted November 19, 2002 A novel I-branching -1,6-N-acetylglucosaminyltransferase involved in the human blood group I antigen expression Niro Inaba, Toru Hiruma, Akira Togayachi, Hiroko Iwasaki, Xiao-Hui Wang, Yusuke Furukawa, Ryoichi Sumi, Takashi Kudo, Katsuya Fujimura, Toshie Iwai, Masanori Gotoh, Mitsuru Nakamura, and Hisashi Narimatsu* Glycogene Function Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan; JGS Japan Genome Solutions, Inc., Hachioji, Tokyo, Japan Glycogene Function Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan; Frontier Research Division, Fujirebio Inc., Hachioji, Tokyo, Japan Glycogene Function Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan Glycogene Function Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan; Amersham Biosciences KK, Tokyo, Japan Division of Stem Cell Regulation, Jichi Medical School, Minamikawachi, Tochigi, Japan Gifu Prefecture Blood Center, Gifu, Japan Cell Regulation Analysis Team, Research Center for Glycoscience (RCG), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan; Division of Stem Cell Regulation, Jichi Medical School, Minamikawachi, Tochigi, Japan * Corresponding author; email: h.narimatsu{at}aist.go.jp. The human blood group i and I antigens are determined by linear and branched poly-N-acetyllactosamine structures, respectively. In erythrocytes, the fetal i antigen is converted to the adult I antigen by I-branching -1,6-N-acetylglucosaminyltransferase (IGnT) during development. Dysfunction of the I-branching enzyme may result in the adult i phenotype in erythrocytes. However, the I gene responsible for blood group I antigen has not been fully confirmed. We report here a novel human I-branching enzyme, designated IGnT3. The genes for IGnT1 (reported in 1993), IGnT2 (also presented in this study), and IGnT3, consist of three exons, and share the second and third exons. Bone marrow cells preferentially expressed IGnT3 transcript. During erythroid differentiation using CD34+ cells, IGnT3 was markedly up-regulated with a concomitant decrease in IGnT1/2. Moreover, reticulocytes expressed the IGnT3 transcript, but IGnT1 and IGnT2 were below detectable levels. By molecular genetic analyses of an adult i pedigree, individuals with the adult i phenotype were revealed to have heterozygous alleles with mutations in exon 2 (1006G->A; Gly336Arg) and exon 3 (1049G->A; Gly350Glu), respectively, of the IGnT3 gene. CHO cells transfected with each mutated IGnT3GnT3 cDNA failed to express I antigen. These findings indicate that the expression of the blood group I antigen in erythrocytes is determined by the novel IGnT3 not by IGnT1 nor IGnT2. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: N. G Karlsson and K. A Thomsson Salivary MUC7 is a major carrier of blood group I type O-linked oligosaccharides serving as the scaffold for sialyl Lewis x Glycobiology, March 1, 2009; 19(3): 288 - 300. [Abstract] [Full Text] [PDF] Y.-Y. Fan, S.-Y. Yu, H. Ito, A. Kameyama, T. Sato, C.-H. Lin, L.-C. Yu, H. Narimatsu, and K.-H. 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