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Prepublished online as a Blood First Edition Paper on April 24, 2003; DOI 10.1182/blood-2003-03-0836. This Article Full Text (PDF) All Versions of this Article: 2003-03-0836v1 102/5/1678    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 Asano, M. Articles by Iwakura, Y. Search for Related Content PubMed PubMed Citation Articles by Asano, M. Articles by Iwakura, Y. Social Bookmarking                   What's this? Submitted March 19, 2003 Accepted April 19, 2003 Impaired selectin ligand biosynthesis and reduced inflammatory responses in -1,4-galactosyltransferase-I-deficient mice Masahide Asano*, Susumu Nakae, Norihiro Kotani, Naoki Shirafuji, Aya Nambu, Noriyoshi Hashimoto, Hiroto Kawashima, Mayumi Hirose, Masayuki Miyasaka, Seiichi Takasaki, and Yoichiro Iwakura Department of Transgenic Animal Science, Kanazawa University Graduate School of Medical Science, Ishikawa, Japan; Center for Experimental Medicine, Institute of Medical Science, Tokyo University, Tokyo, Japan Department of Biochemistry, Institute of Medical Science, Tokyo University, Tokyo, Japan Department of Advanced Medical Science, Institute of Medical Science, Tokyo University, Tokyo, Japan Laboratory of Molecular and Cellular Recognition, Osaka University Graduate School of Medical Science, Osaka, Japan * Corresponding author; email: asano{at}kiea.m.kanazawa-u.ac.jp. Selectins recognize ligands containing carbohydrate chains such as sialyl Lewis x (sLex) that are mainly presented at the terminus of N-acetyllactosamine repeats on core 2 O-glycans. Several glycosyltransferases act successively to extend the N-acetyllactosamine repeats and to synthesize sLex, and -1,4-galactosyltransferase (4GalT) plays a key role in these processes. Recently isolated six 4GalT genes are candidates, but their individual roles, including those in selectin ligand biosynthesis, remain to be elucidated. More than 80% of the core 2 O-glycans on the leukocyte membrane glycoproteins of 4GalT-I-deficient mice lacked galactose residues in -1,4 linkage, and soluble P-selectin binding to neutrophils and monocytes of these mice was significantly reduced, indicating an impairment of selectin ligand biosynthesis. 4GalT-I-deficient mice exhibited blood leukocytosis, but normal lymphocyte homing to peripheral lymph nodes. Acute and chronic inflammatory responses including the contact hypersensitivity (CHS) and delayed-type hypersensitivity (DTH) responses were suppressed, and neutrophil infiltration into inflammatory sites was largely reduced in these mice. Our results demonstrate that 4GalT-I is a major galactosyltransferase responsible for selectin ligand biosynthesis and that inflammatory responses of 4GalT-I-deficient mice are impaired due to the defect in selectin ligand biosynthesis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Zarbock, H. Muller, Y. Kuwano, and K. Ley PSGL-1-dependent myeloid leukocyte activation J. Leukoc. Biol., November 1, 2009; 86(5): 1119 - 1124. [Abstract] [Full Text] [PDF] T. Yoshihara, K. Sugihara, Y. Kizuka, S. Oka, and M. Asano Learning/Memory Impairment and Reduced Expression of the HNK-1 Carbohydrate in {beta}4-Galactosyltransferase-II-deficient Mice J. Biol. 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