Journal
CELL ADHESION & MIGRATION
Volume 2, Issue 4, Pages 243-245Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/cam.2.4.6748
Keywords
integrin; E-cadherin; GnT-III; GnT-V; N-glycosylation; 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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Glycosylation is one of the most abundant posttranslational 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 complex carbohydrates such as glycoproteins, glycolipids and proteoglycans. Functional glycomics, which uses sugar remodeling by glycosyltransferases, is a promising tool for the characterization of glycan functions. Here, we will focus on the positive and negative regulation of biological functions of integrins by the remodeling of N-glycans with N-acetylglucosaminyltransferase III (GnT-III) and N-acetylglucosaminyltransferase V (GnT-V), which catalyze branched N-glycan formations, bisecting GlcNAc and beta 1,6 GlcNAc, respectively. Typically, integrins are modified by GnT-III, which inhibits cell migration and cancer metastasis. In contrast, integrins modified by GnT-V promote cell migration and cancer invasion.
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