Journal
BIOLOGICAL & PHARMACEUTICAL BULLETIN
Volume 32, Issue 5, Pages 780-785Publisher
PHARMACEUTICAL SOC JAPAN
DOI: 10.1248/bpb.32.780
Keywords
N-glycosylation; integrin; N-acetylglucosaminyltransferase III; N-acetylglucosaminyltransferase V; alpha 2,6 sialyltransferase; glycosyltransferase
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Funding
- Core Research for Evolutional Science and Technology (CREST)
- Japan Science and Technology Agency (JST)
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- JSPS
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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 alpha 2,6 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 alpha 5 subunit.
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