Document Detail


Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines.
MedLine Citation:
PMID:  22451656     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The epithelial-to-mesenchymal transition (EMT) plays crucial roles in embryonic development, wound healing, tissue repair, and cancer progression. Results of this study show how transforming growth factor β1 (TGF-β1) down-regulates expression of N-acetylglucosaminyltransferase III (GnT-III) during EMT-like changes. Treatment with TGF-β1 resulted in a decrease in E-cadherin expression and GnT-III expression, as well as its product, the bisected N-glycans, which was confirmed by erythro-agglutinating phytohemagglutinin lectin blot and HPLC analysis in human MCF-10A and mouse GE11 cells. In contrast with GnT-III, the expression of N-acetylglucosaminyltransferase V was slightly enhanced by TGF-β1 treatment. Changes in the N-glycan patterns on α3β1 integrin, one of the target proteins for GnT-III, were also confirmed by lectin blot analysis. To understand the roles of GnT-III expression in EMT-like changes, the MCF-10A cell was stably transfected with GnT-III. It is of particular interest that overexpression of GnT-III influenced EMT-like changes induced by TGF-β1, which was confirmed by cell morphological changes of phase contrast, immunochemical staining patterns of E-cadherin, and actin. In addition, GnT-III modified E-cadherin, which served to prolong E-cadherin turnover on the cell surface examined by biotinylation and pulse-chase experiments. GnT-III expression consistently inhibited β-catenin translocation from cell-cell contact into the cytoplasm and nucleus. Furthermore, the transwell assay showed that GnT-III expression suppressed TGF-β1-induced cell motility. Taken together, these observations are the first to clearly demonstrate that GnT-III affects cell properties, which in turn influence EMT-like changes, and to explain a molecular mechanism for the inhibitory effects of GnT-III on cancer metastasis.
Authors:
Qingsong Xu; Tomoya Isaji; Yingying Lu; Wei Gu; Madoka Kondo; Tomohiko Fukuda; Yuguang Du; Jianguo Gu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-03-26
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  287     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-05-14     Completed Date:  2012-07-13     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  16563-74     Citation Subset:  IM    
Affiliation:
Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai Miyagi, 981-8558, Japan.
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MeSH Terms
Descriptor/Qualifier:
Active Transport, Cell Nucleus / drug effects,  physiology
Animals
Cadherins / genetics,  metabolism
Cell Line, Tumor
Cell Nucleus / genetics,  metabolism*
Cytoplasm / genetics,  metabolism
Down-Regulation / drug effects,  physiology*
Epithelial Cells / cytology,  metabolism*
Epithelial-Mesenchymal Transition / drug effects,  physiology*
Gene Expression Regulation, Enzymologic / drug effects,  physiology*
Humans
Integrin alpha3beta1 / genetics,  metabolism
Mice
Mice, Knockout
N-Acetylglucosaminyltransferases / biosynthesis*,  genetics
Transforming Growth Factor beta1 / metabolism,  pharmacology*
Chemical
Reg. No./Substance:
0/Cadherins; 0/Integrin alpha3beta1; 0/Transforming Growth Factor beta1; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC 2.4.1.144/beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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