A novel I-branching β-1,6-N-acetylglucosaminyltransferase involved in the human blood group I antigen expression

نویسندگان

  • 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
  • Hisashi Narimatsu
چکیده

National Institute of Advanced Industrial Science and Technology (AIST), Glycogene Function Team, Research Center for Glycoscience (RCG), Tsukuba, Ibaraki, Japan. JGS Japan Genome Solutions, Inc., Hachioji, Tokyo, Japan. Fujirebio Inc., Frontier Research Division, Hachioji, Tokyo, Japan. Jichi Medical School, Division of Stem Cell Regulation, Minamikawachi, Tochigi, Japan. Amersham Biosciences KK, Tokyo, Japan. Gifu Prefecture Blood Center, Gifu, Japan. National Institute of Advanced Industrial Science and Technology (AIST), Cell Regulation Analysis Team, Research Center for Glycoscience (RCG), Tsukuba, Ibaraki, Japan.

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منابع مشابه

Molecular basis of the adult i phenotype and the gene responsible for the expression of the human blood group I antigen.

The human blood group i and I antigens are characterized as linear and branched repeats of N-acetyllactosamine, respectively. Conversion of the i to the I structure requires the activity of I-branching beta-1,6-N-acetylglucosaminyltransferase (IGnT). Thus the blood group I gene is assigned to encode a beta-1,6-N-acetylglucosaminyltransferase; however, its identity has not been confirmed. The nu...

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RED CELLS Molecular basis of the adult i phenotype and the gene responsible for the expression of the human blood group I antigen

The human blood group i and I antigens are characterized as linear and branched repeats of N-acetyllactosamine, respectively. Conversion of the i to the I structure requires the activity of I-branching b-1,6-N-acetylglucosaminyltransferase (IGnT). Thus the blood group I gene is assigned to encode a b-1,6-N-acetylglucosaminyltransferase; however, its identity has not been confirmed. The null phe...

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N-acetylglucosaminyltransferase V negatively regulates integrin α5β1-mediated monocyte adhesion and transmigration through vascular endothelium.

Changes in the expression of glycosyltransferases that branch N-linked glycans are associated with many physiological and pathological events, such as cell adhesion, migration, proliferation and tumor cell malignancy. Here, the altered levels of N-acetylglucosaminyltransferase V (GnT-V) and its product β(1,6)-linked GlcNAc in monocytes were observed during inflammation. The effects of GnT-V and...

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The molecular genetics of the human I locus and molecular background explain the partial association of the adult i phenotype with congenital cataracts.

The human i and I antigens are characterized as linear and branched repeats of N-acetyllactosamine, respectively. Conversion of the i to the I structure requires I-branching beta-1,6-N-acetylglucosaminyltransferase activity. It has been noted that the null phenotype of I, the adult i phenotype, is associated with congenital cataracts in Asians. Previously, the identification of molecular change...

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تاریخ انتشار 2002