Identification of Guanylate-Binding Protein 1 as a Potential Oral Cancer Marker Involved in Cell Invasion Using Omics-Based Analysis

2011 ◽  
Vol 10 (8) ◽  
pp. 3778-3788 ◽  
Author(s):  
Chia-Jung Yu ◽  
Kai-Ping Chang ◽  
Yin-Ju Chang ◽  
Chia-Wei Hsu ◽  
Ying Liang ◽  
...  
Keyword(s):  
Oral Cancer ◽  
Cell Invasion ◽  
Binding Protein ◽  
Cancer Marker ◽  
Guanylate Binding Protein

scholarly journals Guanylate binding protein 1 is a novel effector of EGFR-driven invasion in glioblastoma

2011 ◽  
Vol 208 (13) ◽  
pp. 2657-2673 ◽  
Author(s):  
Ming Li ◽  
Akitake Mukasa ◽  
Maria del-Mar Inda ◽  
Jianhua Zhang ◽  
Lynda Chin ◽  
...  
Keyword(s):  
Cell Lines ◽  
Cell Invasion ◽  
Glioma Cell ◽  
Binding Protein ◽  
Brain Parenchyma ◽  
Normal Brain ◽  
Matrix Metalloproteinase 1 ◽  
Egfr Expression ◽  
Egfr Activation ◽  
Guanylate Binding Protein

Although GBP1 (guanylate binding protein 1) was among the first interferon-inducible proteins identified, its function is still largely unknown. Epidermal growth factor receptor (EGFR) activation by amplification or mutation is one of the most frequent genetic lesions in a variety of human tumors. These include glioblastoma multiforme (GBM), which is characterized by independent but interrelated features of extensive invasion into normal brain parenchyma, rapid growth, necrosis, and angiogenesis. In this study, we show that EGFR activation promoted GBP1 expression in GBM cell lines through a signaling pathway involving Src and p38 mitogen-activated protein kinase. Moreover, we identified YY1 (Yin Yang 1) as the downstream transcriptional regulator regulating EGFR-driven GBP1 expression. GBP1 was required for EGFR-mediated MMP1 (matrix metalloproteinase 1) expression and glioma cell invasion in vitro. Although deregulation of GBP1 expression did not affect glioma cell proliferation, overexpression of GBP1 enhanced glioma cell invasion through MMP1 induction, which required its C-terminal helical domain and was independent of its GTPase activity. Reducing GBP1 levels by RNA interference in invasive GBM cells also markedly inhibited their ability to infiltrate the brain parenchyma of mice. GBP1 expression was high and positively correlated with EGFR expression in human GBM tumors and cell lines, particularly those of the neural subtype. Together, these findings establish GBP1 as a previously unknown link between EGFR activity and MMP1 expression and nominate it as a novel potential therapeutic target for inhibiting GBM invasion.

scholarly journals Guanylate-binding protein 2 regulates Drp1-mediated mitochondrial fission to suppress breast cancer cell invasion

2017 ◽  
Vol 8 (10) ◽  
pp. e3151-e3151 ◽  
Author(s):  
Juan Zhang ◽  
Yu Zhang ◽  
Wenshuang Wu ◽  
Fang Wang ◽  
Xinyu Liu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Cell Invasion ◽  
Binding Protein ◽  
Mitochondrial Fission ◽  
Regulatory Function ◽  
Cancer Cell Invasion ◽  
Breast Cancer Cell Invasion ◽  
Guanylate Binding Protein

Abstract Guanylate-binding protein 2 (GBP2) is a member of the large GTPase superfamily that is strongly induced by interferon-γ (IFN-γ). Although the biochemical characteristics of GBP2 have been reported in detail, its biological function has not been thoroughly elucidated to date. To the best of our knowledge, this study presents the first demonstration that GBP2 inhibits mitochondrial fission and cell metastasis in breast cancer cells both in vitro and in vivo. Our previous work demonstrated that dynamin-related protein 1 (Drp1)-dependent mitochondrial fission has a key role in breast cancer cell invasion. In this study, we demonstrate that GBP2 binds directly to Drp1. Elimination of Drp1 by shRNA or Mdivi-1 (a Drp1-specific inhibitor) suppressed GBP2’s regulatory function. Furthermore, GBP2 blocks Drp1 translocation from the cytosol to mitochondria, thereby attenuating Drp1-dependent mitochondrial fission and breast cancer cell invasion. In summary, our data provide new insights into the function and molecular mechanisms underlying GBP2’s regulation of breast cancer cell invasion.

Abstract A4: Guanylate binding protein‐1 promotes glioma cell invasion through induction of MMP1 expression

2009 ◽  
Author(s):  
Ming Li ◽  
Frank B. Furnari ◽  
Webster K. Cavenee
Keyword(s):  
Cell Invasion ◽  
Glioma Cell ◽  
Binding Protein ◽  
Guanylate Binding Protein

scholarly journals Correction: Guanylate-binding protein 2 regulates Drp1-mediated mitochondrial fission to suppress breast cancer cell invasion

2018 ◽  
Vol 9 (11) ◽  
Author(s):  
Juan Zhang ◽  
Yu Zhang ◽  
Wenshuang Wu ◽  
Fang Wang ◽  
Xinyu Liu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Cell Invasion ◽  
Binding Protein ◽  
Mitochondrial Fission ◽  
Cancer Cell Invasion ◽  
Breast Cancer Cell Invasion ◽  
Guanylate Binding Protein

Secretome-Based Identification of Mac-2 Binding Protein as a Potential Oral Cancer Marker Involved in Cell Growth and Motility

2008 ◽  
Vol 7 (9) ◽  
pp. 3765-3775 ◽  
Author(s):  
Li-Ping Weng ◽  
Chih-Ching Wu ◽  
Bao-Lian Hsu ◽  
Lang-Ming Chi ◽  
Ying Liang ◽  
...  
Keyword(s):  
Cell Growth ◽  
Oral Cancer ◽  
Binding Protein ◽  
Cancer Marker

Elaeagnus Angustifolia: a Promising Medicinal Plant for Cancer Theraby

2020 ◽  
Author(s):  
Islam Mohamed ◽  
Ahmed Moahmed ◽  
Mennatallah Abdelkader ◽  
Alaaeldin Saleh ◽  
Ala-Eddin Al-Moustafa
Keyword(s):  
Cell Proliferation ◽  
Oral Cancer ◽  
Medicinal Plant ◽  
Cancer Progression ◽  
Plant Extract ◽  
Cell Invasion ◽  
Elaeagnus Angustifolia ◽  
Flower Extract ◽  
Inhibition Of Angiogenesis ◽  
E Cadherin

Introduction: Elaeagnus angustifolia (EA) is a medicinal plant that has been used for centuries in treating many human diseases, in the Middle East, including fever, amoebic dysentery, gastrointestinal problems. However, the effect of EA plant extract on human cancer progression especially oral malignancy has not been investigated yet. Thus, first we examined the effect of EA flower extract on angiogenesis in ovo, and on selected parameters in human oral cancer cells. Materials and methods: Chorioallantoic membranes (CAMs) of chicken embryos at 3-7 days of incubation were used to assess the effect EAflower plant extract on angiogenesis. Meanwhile, cell proliferation, soft agar, cell cycle, cell invasion and cell wounding assays were performed to explore the outcome of EA plant extract on FaDu and SCC25 oral cancer cell lines. On the other hand, western blot analysis was carried out to evaluate E-cadherin and Erk1/Erk2 expression and activation, respectively, in FaDu and SCC25 under the effect of EA extract. Results: Our data show that EA extract inhibits cell proliferation and colony formation, in addition to the initiation of Scell cycle arrest and reductionof G1/G2 phases. In parallel, EA extract provokes differentiation to an epithelial phenotype “mesenchymal-epithelial transition: MET” which is the opposite of “epithelial-mesenchymal transition, EMT”: an important event in cell invasion and metastasis. Thus, EA extract causes a dramatic decrease in cell motility and invasion abilities of FaDu and SCC25 cancer cells in comparison with their controls. These changes are accompanied by an up-regulation of E-cadherin expression. The molecular pathway analysis of the EA flower extract reveals that it can inhibit the phosphorylation of Erk1/Erk2, which could be behind the inhibition of angiogenesis, the initiation of MET event and the overexpression of E-cadherin. Conclusions: Our findings indicate that EA plant extract can downgrade human oral cancer progression by the inhibition of angiogenesis and cell invasion via Erk1/Erk2 signaling pathways.

scholarly journals Healthy and preeclamptic pregnancies show differences in Guanylate-Binding Protein-1 plasma levels

2021 ◽  
Author(s):  
Joost H.N. Schuitemaker ◽  
Rik H.J. Beernink ◽  
Thomas I.F.H. Cremers ◽  
Sicco A. Scherjon ◽  
Maria G. Van Pampus ◽  
...  
Keyword(s):  
Plasma Levels ◽  
Binding Protein ◽  
Guanylate Binding Protein

scholarly journals Transient Kinetic Investigation of GTP Hydrolysis Catalyzed by Interferon-γ-induced hGBP1 (Human Guanylate Binding Protein 1)

2006 ◽  
Vol 281 (39) ◽  
pp. 28627-28635 ◽  
Author(s):  
Simone Kunzelmann ◽  
Gerrit J. K. Praefcke ◽  
Christian Herrmann
Keyword(s):  
Binding Protein ◽  
Interferon Γ ◽  
Kinetic Investigation ◽  
Gtp Hydrolysis ◽  
Guanylate Binding Protein

Nonidentical Induction of the Guanylate Binding Protein and the 56K Protein by Type I and Type II Interferons

1986 ◽  
Vol 6 (4) ◽  
pp. 417-427 ◽  
Author(s):  
YIH-SHYUN E. CHENG ◽  
MARY F. BECKER-MANLEY ◽  
THAI D. NGUYEN ◽  
WILLIAM F. DEGRADO ◽  
GERALD J. JONAK
Keyword(s):  
Binding Protein ◽  
Type I ◽  
Type Ii ◽  
Guanylate Binding Protein

Evolution of the guanylate binding protein (GBP) genes: Emergence of GBP7 genes in primates and further acquisition of a unique GBP3 gene in simians

2021 ◽  
Vol 132 ◽  
pp. 79-81
Author(s):  
João Vasco Côrte-Real ◽  
Hanna-Mari Baldauf ◽  
Joana Abrantes ◽  
Pedro José Esteves
Keyword(s):  
Binding Protein ◽  
Guanylate Binding Protein
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