DICP OpenIR
Subject Area物理化学
Potential roles of N-glycosylation in cell adhesion
Gu, Jianguo1; Isaji, Tomoya1; Xu, Qingsong1,2; Kariya, Yoshinobu1,3; Gu, Wei1; Fukuda, Tomohiko1; Du, Yuguang2; JianguoGu
KeywordBisected N-glycan Cell Adhesion E-cadherin N-glycosylation Integrin
Source PublicationGLYCOCONJUGATE JOURNAL
2012-12-01
DOI10.1007/s10719-012-9386-1
Volume29Issue:8-9Pages:599-607
Indexed BySCI
SubtypeArticle
Department18
Funding Project1805
Contribution Rank2,3
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemistry & Molecular Biology
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordEPITHELIAL-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
AbstractThe 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.
Language英语
WOS IDWOS:000309868800005
Citation statistics
Cited Times:77[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/118047
Collection中国科学院大连化学物理研究所
Corresponding AuthorJianguoGu
Affiliation1.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
Recommended Citation
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.,...&JianguoGu.(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.
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