Discoidin Domain Receptor-1a (DDR1a) Promotes Glioma Cell Invasion and Adhesion in Association with Matrix Metalloproteinase-2

2005 ◽  
Vol 76 (3) ◽  
pp. 239-248 ◽  
Author(s):  
Rosalyn Ram ◽  
Gustavo Lorente ◽  
Karoly Nikolich ◽  
Roman Urfer ◽  
Erik Foehr ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Glioma Cell ◽  
Matrix Metalloproteinase 2 ◽  
Discoidin Domain Receptor

In Silico prediction of the molecular basis of ClTx and AaCTx interaction with matrix metalloproteinase-2 (MMP-2) to inhibit glioma cell invasion

2016 ◽  
Vol 35 (13) ◽  
pp. 2815-2829 ◽  
Author(s):  
Houcemeddine Othman ◽  
Silke Andrea Wieninger ◽  
Mohamed ElAyeb ◽  
Michael Nilges ◽  
Najet Srairi-Abid
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
In Silico ◽  
Molecular Basis ◽  
Glioma Cell ◽  
Matrix Metalloproteinase 2 ◽  
In Silico Prediction

scholarly journals Cannabinoids Inhibit Glioma Cell Invasion by Down-regulating Matrix Metalloproteinase-2 Expression

2008 ◽  
Vol 68 (6) ◽  
pp. 1945-1952 ◽  
Author(s):  
Cristina Blázquez ◽  
María Salazar ◽  
Arkaitz Carracedo ◽  
Mar Lorente ◽  
Ainara Egia ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Glioma Cell ◽  
Matrix Metalloproteinase 2

scholarly journals Chlorotoxin Inhibits Glioma Cell Invasion via Matrix Metalloproteinase-2

2002 ◽  
Vol 278 (6) ◽  
pp. 4135-4144 ◽  
Author(s):  
Jessy Deshane ◽  
Craig C. Garner ◽  
Harald Sontheimer
Keyword(s):  
Matrix Metalloproteinase ◽  
Cell Invasion ◽  
Glioma Cell ◽  
Matrix Metalloproteinase 2

scholarly journals Galectin-9 Promotes Human Trophoblast Cell Invasion through Matrix Metalloproteinase-2 and p38 Signaling Pathway

2018 ◽  
Vol 2 (1) ◽  
pp. 1 ◽  
Author(s):  
Song-Cun Wang ◽  
Mei-Rong Du ◽  
Feng-Run Sun ◽  
Chun-Qing Chen ◽  
Min Yu ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Signaling Pathway ◽  
Cell Invasion ◽  
Trophoblast Cell ◽  
Matrix Metalloproteinase 2 ◽  
Human Trophoblast

Mucin O-glycosylating enzyme GALNT2 facilitates the malignant character of glioma by activating the EGFR/PI3K/Akt/mTOR axis

2019 ◽  
Vol 133 (10) ◽  
pp. 1167-1184 ◽  
Author(s):  
Zhongzheng Sun ◽  
Hao Xue ◽  
Yan Wei ◽  
Chaochao Wang ◽  
Rui Yu ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Glioma Cell ◽  
Proportional Hazards Model ◽  
Cox Proportional Hazards ◽  
Cox Proportional Hazards Model ◽  
The Cancer Genome Atlas ◽  
Matrix Metalloproteinase 2 ◽  
Migration And Invasion ◽  
Expression Levels

AbstractN-Acetylgalactosaminyltransferase 2 (GALNT2), the enzyme that regulates the initial step of mucin O-glycosylation, has been reported to play a role in influencing the malignancy of various cancers. However, the mechanism through which it influences gliomas is still unknown. In the current study, the Cox proportional hazards model was used to select genes. Data obtained from The Cancer Genome Atlas (TCGA) database and immunohistochemistry (IHC) of clinical specimens showed that increased GALNT2 expression levels were associated with an unfavorable prognosis and a higher tumor grade in human gliomas. Then, GALNT2 knockdown and overexpression were performed in glioma cell lines and verified by quantitative real-time PCR (qRT-PCR) and Western blotting. Functional assays demonstrated that GALNT2 was closely related to glioma cell proliferation, cycle transition, migration and invasion. Western blot analysis and lectin pull-down assays indicated that GALNT2 knockdown decreased the level of phosphorylated epidermal growth factor receptor (EGFR) and the expression of the Tn antigen on EGFR and affected the expression levels of p21, cyclin-dependent kinase 4 (CDK4), cyclinD1, matrix metalloproteinase 2 (MMP2) and matrix metalloproteinase 9 (MMP9) through the EGFR/PI3K/Akt/mTOR pathway. GALNT2 overexpression had the opposite effects. In vivo, the growth of orthotopic glioma xenografts in nude mice was distinctly inhibited by the expression of GALNT2 shRNA, and the tumors with GALNT2 shRNA exhibited less aggressiveness and reduced expression of Ki67 and MMP2. Overall, GALNT2 facilitates the malignant characteristics of glioma by influencing the O-glycosylation and phosphorylation of EGFR and the subsequent downstream PI3K/Akt/mTOR axis. Therefore, GALNT2 may serve as a novel biomarker and a potential target for future therapy of glioma.

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