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
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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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