中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Potential roles of N-glycosylation in cell adhesion

文献类型:期刊论文

作者Gu, Jianguo1; Isaji, Tomoya1; Xu, Qingsong1,2; Kariya, Yoshinobu1,3; Gu, Wei1; Fukuda, Tomohiko1; Du, Yuguang2
刊名glycoconjugate journal
出版日期2012-12-01
卷号29期号:8-9页码:599-607
关键词Bisected N-glycan Cell adhesion E-cadherin N-glycosylation Integrin
产权排序2,3
通讯作者jianguogu
英文摘要the functional units of cell adhesion are typically multiprotein complexes made up of three general classes of proteins; the adhesion receptors, the cell-extracellular matrix (ecm) proteins, and the cytoplasmic plaque/peripheral membrane proteins. the cell adhesion receptors are usually transmembrane glycoproteins (for example e-cadherin and integrin) that mediate binding at the extracellular surface and determine the specificity of cell-cell and cell-ecm recognition. e-cadherin-mediated cell-cell adhesion can be both temporally and spatially regulated during development, and represents a key step in the acquisition of the invasive phenotype for many tumors. on the other hand, integrin-mediated cell-ecm interactions play important roles in cytoskeleton organization and in the transduction of intracellular signals to regulate various processes such as proliferation, differentiation and cell migration. ecm proteins are typically large glycoproteins, including the collagens, fibronectins, laminins, and proteoglycans that assemble into fibrils or other complex macromolecular arrays. the most of these adhesive proteins are glycosylated. here, we focus mainly on the modification of n-glycans of integrins and laminin-332, and a mutual regulation between cell adhesion and bisected n-glycan expression, to address the important roles of n-glycans in cell adhesion.
WOS标题词science & technology ; life sciences & biomedicine
学科主题物理化学
类目[WOS]biochemistry & molecular biology
研究领域[WOS]biochemistry & molecular biology
关键词[WOS]epithelial-mesenchymal transitions ; asparagine-linked oligosaccharides ; epidermal-growth-factor ; beta-propeller domain ; acetylglucosaminyltransferase-iii ; e-cadherin ; bisecting glcnac ; integrin alpha-v-beta-3 ; aberrant glycosylation ; extracellular segment
收录类别SCI
语种英语
WOS记录号WOS:000309868800005
公开日期2013-10-11
源URL[http://159.226.238.44/handle/321008/118047]  
专题大连化学物理研究所_中国科学院大连化学物理研究所
作者单位1.Tohoku Pharmaceut Univ, Div Regulatory Glycobiol, Aoba Ku, Sendai, Miyagi 9818558, Japan
2.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
3.Fukushima Med Univ, Sch Med, Dept Biochem, Fukushima 9601295, Japan
推荐引用方式
GB/T 7714
Gu, Jianguo,Isaji, Tomoya,Xu, Qingsong,et al. Potential roles of N-glycosylation in cell adhesion[J]. glycoconjugate journal,2012,29(8-9):599-607.
APA Gu, Jianguo.,Isaji, Tomoya.,Xu, Qingsong.,Kariya, Yoshinobu.,Gu, Wei.,...&Du, Yuguang.(2012).Potential roles of N-glycosylation in cell adhesion.glycoconjugate journal,29(8-9),599-607.
MLA Gu, Jianguo,et al."Potential roles of N-glycosylation in cell adhesion".glycoconjugate journal 29.8-9(2012):599-607.

入库方式: OAI收割

来源:大连化学物理研究所

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