Importance of N-Glycosylation on α5β1 Integrin for Its Biological Functions
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概要
- 論文の詳細を見る
N-Glycosylation of proteins is conserved in eukaryotes, which is one of the most abundant post-translational modification reactions, and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structure (glycan) are associated with many physiological and pathological events, including cell adhesion, migration, cell growth, cell differentiation and tumor invasion. Glycosylation reactions are catalyzed by the action of glycosyltransferases, which add sugar chains to various glycans on glycoproteins, glycolipids and proteoglycans. Here, we focus mainly on the modification of N-glycans with N-acetylglucosaminyltransferase III (GnT-III), N-acetylglucosaminyltransferase V (GnT-V) and α2,6 sialyltransferase (ST6GalI) to address the important roles of N-glycans in integrin-meditaed cell adhesion and migration. In addition, we also discuss the potential roles of N-glycosylation sites on integrin α5 subunit.
- 公益社団法人 日本薬学会の論文
著者
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Gu Jianguo
Division Of Regulatory Glycobiology Institute Of Molecular Biomembrane And Glycobiology Tohoku Pharm
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SATO YUYA
Division of Hematology, Department of Pediatrics, Dokkyo University School of Medicine
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FUKUDA Tomohiko
Division of Regulatory Glycobiology, Tohoku Pharmaceutical University
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Fukuda Tomohiko
Division Of Chemistry Faculty Of Science Hokkaido University
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Isaji Tomoya
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pha
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Kariya Yoshinobu
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pha
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Gu Jianguo
Division Of Neuroscience Univ. Of Florida
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GU Jianguo
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University
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Kariya Yoshinobu
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University
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Isaji Tomoya
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University
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Kariya Yoshinobu
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University
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Sato Yuya
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University
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Fukuda Tomohiko
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University
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