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  4. β1,4-N-acetylgalactosaminyltransferase III enhances malignant phenotypes of colon cancer cells
 
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β1,4-N-acetylgalactosaminyltransferase III enhances malignant phenotypes of colon cancer cells

Journal
Molecular Cancer Research
Journal Volume
5
Journal Issue
6
Pages
543-552
Date Issued
2007
Author(s)
JOHN HUANG  
JIN-TUNG LIANG  
Hsiu-Chin Huang
Shen, Tang-Long  
Hsiao-Yu Chen
NENG-YU LIN  
Mei-Ieng Che
WEI-CHOU LIN  
MIN-CHUAN HUANG  
DOI
10.1158/1541-7786.MCR-06-0431
URI
https://www.scopus.com/inward/record.uri?eid=2-s2.0-34250892600&doi=10.1158%2f1541-7786.MCR-06-0431&partnerID=40&md5=ae92f93dc08f2a08a1c913ad813e3d93
https://scholars.lib.ntu.edu.tw/handle/123456789/596193
Abstract
The enzyme β1,4-N-acetylgalactosaminyltransferase III (β4GalNAc-T3) exhibits in vitro activity of synthesizing N,N′-diacetyllactosediamine, GalNAcβ1,4GlcNAc. Here, we investigate the expression of β4GalNAc-T3 in primary colon tumors and the effects of its overexpression on HCT116 colon cancer cells. Real-time reverse transcription-PCR showed that the expression of β4GalNAc-T3 was up-regulated in 72.5% (n = 40) of primary colon tumors compared with their normal counterparts. β4GalNAc-T3 overexpression resulted in enhanced cell-extracellular matrix adhesion, migration, anchorage-independent cell growth, and invasion of colon cancer cells. Moreover, β4GalNAc-T3 overexpression increased tumor growth and metastasis and decreased survival of tumor-bearing nude mice. β4GalNAc-T3 overexpression showed increased tyrosine phosphorylation of focal adhesion kinase and paxillin Y118 as well as increased extracellular signal-regulated kinase phosphorylation. These results suggest that up-regulation of β4GalNAc-T3 may play a critical role in promoting tumor malignancy and that integrin and mitogen-activated protein kinase signaling pathways could be involved in the underlying mechanism. Copyright ? 2007 American Association for Cancer Research.
SDGs

[SDGs]SDG3

Other Subjects
beta1,4 n acetylgalactosaminyltransferase III; focal adhesion kinase; mitogen activated protein kinase; paxillin; transferase; unclassified drug; antineoplastic agent; beta 1,4 N acetylgalactosaminyltransferase III, human; beta-1,4-N-acetylgalactosaminyltransferase III, human; n acetylgalactosaminyltransferase; paxillin; anchorage independent growth; animal experiment; animal model; animal tissue; article; cancer cell culture; cancer invasion; cancer survival; cell adhesion; cell invasion; cell migration; colon cancer; controlled study; enzyme phosphorylation; extracellular matrix; female; gene overexpression; human; human cell; malignant neoplastic disease; metastasis; mouse; nonhuman; phenotype; priority journal; protein function; real time polymerase chain reaction; reverse transcription polymerase chain reaction; tumor promotion; upregulation; animal; cell proliferation; colon tumor; gene expression regulation; metabolism; nude mouse; pathology; phenotype; physiology; tumor cell line; Mus musculus; Animals; Antineoplastic Agents; Cell Line, Tumor; Cell Proliferation; Colonic Neoplasms; Focal Adhesion Protein-Tyrosine Kinases; Gene Expression Regulation, Neoplastic; Humans; Mice; Mice, Nude; N-Acetylgalactosaminyltransferases; Neoplasm Invasiveness; Neoplasm Metastasis; Paxillin; Phenotype
Type
journal article

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