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Sely, downregulated ENO1 expression in SPCA-1 cells inhibited the expression of these proteins in addition to p21. (B) In A549 cells, overexpressing ENO1 increased the expression of EMT-marker genes including snail, vimentin, and N-cadherin and decreased the expression of E-cadherin. In SPCA-1 cells, suppressing ENO1 expression decreased the expression of these proteins in addition to E-cadherin. (C) In A549 cells, upregulated ENO1 increased levels of -catenin, phos-FAK, PI3K, and AKT, but not their total protein levels; in SPCA-1 cells, reduced ENO1 expression reduced the levels of -catenin, phos-FAK, PI3K, and AKT, but not their total protein levels. (D) ENO1-suppressed SPCA-1 cells were treated with Ang II (1 mol/l) for 12 h to activate the phosphorylation of FAK, then cellular p-FAK, p-AKT, LDHA, cyclin D1, c-Myc, p21, and -catenin were assessed by Western blot. -Actin served as a loading control. All of the experiments were repeated at least three times.the expression of LDHA, c-Myc, cyclin D1, p-Rb, and cyclin E1 while elevating the expression of p21, which promoted cell glycolysis and proliferation of NSCLC. EMT is regarded as a key event in tumor migration and invasion progression. In this study, we further examined the expression of EMT marker genes and found that knocking down ENO1 expression induced the protein levels of E-cadherin while suppressing the expression of snail, vimentin, and N-cadherin in NSCLC cells. These results are consistent with our previous report of ENO1 in glioma [17]. However, ENO1 overexpression did not lead to any changes from epithelial to Chrysin mesenchymal transition in NSCLC cells. PI3K/AKT is a key signal mediator during carcinogenesis [35,36], and its activation induces glycolysis [37-39] and c-Myc-mediated cell cycle PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/10956013 transition [40] and promotes the progression of EMT [37,41]. In addition, c-Myc has also been shown to regulate energy metabolism by regulating LDHA in tumor [42]. We hypothesized thatoncogenic ENO1 functions through the PI3K/AKT pathway in NSCLC. We found that suppressed ENO1 significantly decreased the protein levels of -catenin and phosphorylated PI3K and AKT, but not their total protein levels in SPCA-1 cells, which is similar to our previous report in glioma [17]. Interestingly, we examined the protein levels of FAK, an upstream signal factor of the PI3K/AKT pathway, and found that suppressed ENO1 significantly decreased levels of phosphorylated FAK, but not its total protein levels. We speculated that ENO1 regulates cell glycolysis, proliferation, migration, and invasion through FAK-mediated PI3K/AKT pathway in NSCLC. To further clarify the specific mechanism, Ang II, an activating agent of phosphorylated FAK [19], was used to treat ENO1-suppressed SPCA-1 cells. We observed that not only the production of lactate, cell viability, migration, and invasion was restored but also the expression levels of p-FAK, p-AKT, LDHA, cyclin D1, c-Myc, p21, and -catenin were rescued. TheseFu et al. Journal of Hematology Oncology (2015)8:Page 9 ofFigure 6 ENO1 regulates the expression of cell cycle and EMT-associated genes of NSCLC cells. Immunohistochemical (IHC) staining of ENO1, -catenin, cyclin D1, p21 (A), and EMT-associated genes (B) including E-cadherin, N-cadherin, and vimentin in subcutaneous tumors of mice injected with PLV-Ctr vs A549-ENO1, PLV-shCtr vs shENO1-B SPCA-1 cells.results demonstrated that suppressed ENO1 inhibited cell glycolysis, proliferation, migration, and invasion by in.