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http://dx.doi.org/10.5483/BMBRep.2011.44.12.772

Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics  

Taniguchi, Naoyuki (Disease Glycomics Team, Systems Glycobiology Research Group, RIKEN Advanced Science Institute)
Korekane, Hiroaki (Disease Glycomics Team, Systems Glycobiology Research Group, RIKEN Advanced Science Institute)
Publication Information
BMB Reports / v.44, no.12, 2011 , pp. 772-781 More about this Journal
Abstract
Branched N-glycans are produced by a series of glycosyltransferases including N-acetylglucosaminyltransferases and fucosyltransferases and their corresponding genes. Glycans on specific glycoproteins, which are attached via the action of glycosyltransferases, play key roles in cell adhesion and signaling. Examples of this are adhesion molecules or signaling molecules such as integrin and E-cadherin, as well as membrane receptors such as the EGF and TGF-${\beta}$ receptors. These molecules also play pivotal roles in the underlying mechanism of a variety of disease such as cancer metastasis, diabetes, and chronic obstructive pulmonary disease (COPD). Alterations in the structures of branched N-glycans are also hall marks and are useful for cancer biomarkers and therapeutics against cancer. This mini-review describes some of our recent studies on a functional glycomics approach to the study of branched N-glycans produced by N-acetylglucosaminyltransferases III, IV, V and IX (Vb) (GnT-III, GnT-IV, V and IX (Vb)) and fucosyltransferase 8 (Fut8) and their pathophysiological significance, with emphasis on the importance of a systems glycobiology approach as a future perspective for glycobiology.
Keywords
Antibody therapy; Branched N-glycans; Cancer biomarker; Growth factor receptors; N-acetylglucosaminyltransferases;
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