Genome-Wide Transcriptome Analysis of Estrogen Receptor-Positive and Human Epithelial Growth Factor Receptor 2-Positive Breast Cancers by Ribonucleic Acid Sequencing

2017 ◽  
Vol 83 (4) ◽  
pp. 338-348
Author(s):  
Pengtao  Chen ◽  
Wei  Song ◽  
Liangli  Liu
Keyword(s):  
Estrogen Receptor ◽  
Growth Factor ◽  
Transcriptome Analysis ◽  
Ribonucleic Acid ◽  
Growth Factor Receptor ◽  
Breast Cancers ◽  
Epithelial Growth Factor ◽  
Genome Wide ◽  
Estrogen Receptor Positive ◽  
Epithelial Growth

scholarly journals Estrogen Modulation of MgATPase Activity of Nonmuscle Myosin-II-B Filaments

Endocrinology ◽  
2007 ◽  
Vol 148 (1) ◽  
pp. 279-292 ◽  
Author(s):  
George I. Gorodeski
Keyword(s):  
Estrogen Receptor ◽  
Growth Factor ◽  
Myosin Ii ◽  
Growth Factor Receptor ◽  
Estrogen Receptor Α ◽  
Nonmuscle Myosin ◽  
Epithelial Growth Factor ◽  
Nonmuscle Myosin Ii ◽  
Mgatpase Activity ◽  
Epithelial Growth

The study tested the hypothesis that estrogen controls epithelial paracellular resistance through modulation of myosin. The objective was to understand how estrogen modulates nonmuscle myosin-II-B (NMM-II-B), the main component of the cortical actomyosin in human epithelial cervical cells. Experiments used human cervical epithelial cells CaSki as a model, and end points were NMM-II-B phosphorylation, filamentation, and MgATPase activity. The results were as follows: 1) treatment with estrogen increased phosphorylation and MgATPase activity and decreased NMM-II-B filamentation; 2) estrogen effects could be blocked by antisense nucleotides for the estrogen receptor-α and by ICI-182,780, tamoxifen, and the casein kinase-II (CK2) inhibitor, 5,6-dichloro-1-β-(D)-ribofuranosylbenzimidazole and attenuated by AG1478 and PD98059 (inhibitors of epithelial growth factor receptor and ERK/MAPK) but not staurosporine [blocker of protein kinase C (PKC)]; 3) treatments with the PKC activator sn-1,2-dioctanoyl diglyceride induced biphasic effect on NMM-II-B MgATPase activity: an increase at 1 nm to 1 μm and a decrease in activity at more than 1 μm; 4) sn-1,2-dioctanoyl diglyceride also decreased NMM-II-B filamentation in a monophasic and saturable dose dependence (EC50 1–10 μm); 5) when coincubated directly with purified NMM-II-B filaments, both CK2 and PKC decreased filamentation and increased MgATPase activity; 6) assays done on disassembled NMM-II-B filaments showed MgATPase activity in filaments obtained from estrogen-treated cells but not estrogen-depleted cells; and 7) incubations in vitro with CK2, but not PKC, facilitated MgATPase activity, even in disassembled NMM-II-B filaments. The results suggest that estrogen, in an effect mediated by estrogen receptor-α and CK2 and involving the epithelial growth factor receptor and ERK/MAPK cascades, increases NMM-II-B MgATPase activity independent of NMM-II-B filamentation status.

Prostasin Impairs Epithelial Growth Factor Receptor Activation to Suppress Dengue Virus Propagation

2018 ◽  
Vol 219 (9) ◽  
pp. 1377-1388 ◽  
Author(s):  
Chun-Kuang Lin ◽  
Chin-Kai Tseng ◽  
Yu-Hsuan Wu ◽  
Chun-Yu Lin ◽  
Chung-Hao Huang ◽  
...  
Keyword(s):  
Growth Factor ◽  
Dengue Virus ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Epithelial Growth Factor Receptor ◽  
Virus Propagation ◽  
Epithelial Growth Factor ◽  
Epithelial Growth

scholarly journals Increased Eps15 homology domain 1 and RAB11FIP3 expression regulate breast cancer progression via promoting epithelial growth factor receptor recycling

Tumor Biology ◽  
2017 ◽  
Vol 39 (2) ◽  
pp. 101042831769101 ◽  
Author(s):  
Dandan Tong ◽  
Ya-Nan Liang ◽  
AA Stepanova ◽  
Yu Liu ◽  
Xiaobo Li ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Epithelial Growth Factor Receptor ◽  
Epithelial Growth Factor ◽  
Epidermal Growth ◽  
Epithelial Growth ◽  
Eps15 Homology Domain

Recent research indicates that the C-terminal Eps15 homology domain 1 is associated with epithelial growth factor receptor–mediated endocytosis recycling in non-small-cell lung cancer. The aim of this study was to determine the clinical significance of Eps15 homology domain 1 gene expression in relation to phosphorylation of epithelial growth factor receptor expression in patients with breast cancer. Primary breast cancer samples from 306 patients were analyzed for Eps15 homology domain 1, RAB11FIP3, and phosphorylation of epithelial growth factor receptor expression via immunohistochemistry. The clinical significance was assessed via a multivariate Cox regression analysis, Kaplan–Meier curves, and the log-rank test. Eps15 homology domain 1 and phosphorylation of epithelial growth factor receptor were upregulated in 60.46% (185/306) and 53.92% (165/306) of tumor tissues, respectively, as assessed by immunohistochemistry. The statistical correlation analysis indicated that Eps15 homology domain 1 overexpression was positively correlated with the increases in phosphorylation of epithelial growth factor receptor ( r = 0.242, p < 0.001) and RAB11FIP3 ( r = 0.165, p = 0.005) expression. The multivariate Cox proportional hazard model analysis demonstrated that the expression of Eps15 homology domain 1 alone is a significant prognostic marker of breast cancer for the overall survival in the total, chemotherapy, and human epidermal growth factor receptor 2 (−) groups. However, the use of combined expression of Eps15 homology domain 1 and phosphorylation of epithelial growth factor receptor markers is more effective for the disease-free survival in the overall population, chemotherapy, and human epidermal growth factor receptor 2 (−) groups. Moreover, the combined markers are also significant prognostic markers of breast cancer in the human epidermal growth factor receptor 2 (+), estrogen receptor (+), and estrogen receptor (−) groups. Eps15 homology domain 1 has a tumor suppressor function, and the combined marker of Eps15 homology domain 1/phosphorylation of epithelial growth factor receptor expression was identified as a better prognostic marker in breast cancer diagnosis. Furthermore, RAB11FIP3 combines with Eps15 homology domain 1 to promote the endocytosis recycling of phosphorylation of epithelial growth factor receptor.

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