Scope includes mutations and abnormal protein expression. Note: list is not exhaustive. Number of papers are based on searches of Pub. Med (click on topic title for arbitrary criteria used). Useful Links. BIRC5. OMIM, Johns Hopkin University. Angiogenesis in the New Zealand obese mouse. Lipids in Health and Disease. Genes encoding matrix protein such as. Characterization of synergistic anti-cancer effects of docosahexaenoic acid and curcumin on DMBA-induced mammary tumorigenesis in mice. Tuesday, August 2, 2016 Poster Session. We also found that BIRC5 mRNA and protein expression was. Referenced article focusing on the relationship between phenotype and genotype. BIRC5. International Cancer Genome Consortium. Summary of gene and mutations by cancer type from ICGCBIRC5. Cancer Genome Anatomy Project, NCIGene Summary. ![]() ![]() BIRC5. COSMIC, Sanger Institute. Somatic mutation information and related details BIRC5. Epigenomics, NCBISearch the Epigenomics database and view relevant gene tracks of samples. Latest Publications: BIRC5 (cancer- related)Ling X, Xu C, Fan C, et al. FL1. 18 induces p. Mdm. X. Cancer Res. Although FL1. 18 is a camptothecin analogue, its antitumor potency is much superior to other FDA- approved camptothecin analogues (irinotecan and topotecan). The mechanism of action (MOA) underlying the antitumor effects of FL1. Here, we report that FL1. MOA in p. 53 wild- type cancer cells. Our studies show that this MOA involves an induction of proteasomal degradation of Mdm. X, a critical negative regulator of p. ATM- dependent DNA damage signaling pathway but dependent on E3- competent Mdm. FL1. 18 inhibits p. Mdm. 2- Mdm. X E3 complex in cells and in cell- free systems. ![]() While on a high-fat diet. Birc5 (F), 5. ![]()
In contrast, FL1. Mdm. 2- mediated Mdm. X ubiquitination. Coimmunoprecipitation revealed that FL1. Mdm. 2- p. 53 interactions and moderately increases Mdm. Mdm. X interactions, suggesting a change of targeting specificity of Mdm. Mdm. X E3 complex from p. Mdm. X, resulting in accelerated Mdm. X degradation. As a result, p. Mdm. 2- Mdm. X E3 complex is reduced, which in turn activates p. Activation of the p. FL1. 18 induces p. However, in the absence of p. Mdm. X overexpression, FL1. These two distinct cellular consequences collectively contribute to the potent effects of FL1. This study identifies a potential application of FL1. Mdm. X inhibitor for targeted therapies. However, PTX- induced apoptosis might be inhibited by DEX. This study was undertaken to investigate the effects of DEX on the apoptosis induced by PTX. METHODS: Both of SKOV- 3 and HO- 8. Con); (2) treated with DEX (0. Cell proliferation was determined by the 3- (4,5)- dimethylthiahiazo (- z- y. MTT) dye uptake method, while cell apoptosis was analyzed by propidium iodide (PI) staining and flow cytometry. Then, reverse transcription polymerase chain reactions (RT- PCRs) were applied to semi- quantitative analysis, followed by western blot analysis. Statistical analysis was performed, with Fisher's least significant difference test. RESULTS: Our results demonstrated that DEX can differentially inhibit SKOV- 3 and HO- 8. PTX and decrease the apoptosis rates in cancer cells. Pre- treatment with DEX could up- regulate the expressions of members of anti- apoptotic Bcl- 2 family (Bcl- 2 and Bcl- XL) and members of IAP family (survivin). The expression of cleaved caspase- 3 was down- regulated by DEX, shown by semi- quantitative RT- PCRs and western blot analysis. CONCLUSIONS: Our data gained invaluable insights of the antagonistic mechanisms of DEX on PTX- induced cancer cell death and may provide new methods of using DEX as antineoplastic drugs or agents in the clinical treatment for ovarian cancer patients. RES treatment reduced cell proliferation and colony formation and increased senescence and apoptosis in both parental and resistant cells. Importantly, RES augmented the effects of paclitaxel in both cell lines. Up- regulation of the MDR1 and CYP2. C8 genes were shown to be potential mechanisms of paclitaxel resistance in the resistant cells. CONCLUSION: RES, both alone and in combination with paclitaxel, may be useful in the treatment of paclitaxel- sensitive and paclitaxel- resistant triple- negative breast cancer cells. Jul- Sep; 1. 9(3): 7. The cells were then divided into the blank control, plasmid control, Livin, Survivin, and co- transfected groups. Real- time quantitative PCR (q. RT- PCR) and Western blot assay were used to determine the m. RNA and protein expression levels of Livin and Survivin. The MTT assay was used to evaluate the changes in cell proliferation. The TUNEL assay was used to evaluate the apoptotic rate. RESULTS: The sh. RNA eukaryotic expression vectors of Livin and Survivin were successfully constructed. The m. RNA and protein expression of Livin and Survivin were significantly lower in the co- transfected group than in the control groups (p< 0. At 4. 8, 6. 0, and 7. At 4. 8 hrs after transfection, the apoptotic rate significantly increased (p< 0. CONCLUSION: Co- silencing of Livin and Survivin can effectively inhibit the cell proliferation and apoptosis of lung cancer cells. We evaluated for Proliferation Axis Score differences, as determined by Oncotype Dx, in Hispanic and non- Hispanic white women with newly diagnosed breast cancer. We matched 2. 19 women, based upon age, stage, and nodal status. Compared to non- Hispanic whites, Hispanic women with hormone- sensitive, HER2- negative early- stage breast cancer had a higher Proliferation Axis Score. No differences were seen in Recurrence Score, ER, PR, or HER2 by Oncotype DX. CCNB1 and AURKA were significantly higher in Hispanic women. These tumor differences may help explain breast cancer outcome differences between the two ethnicities. PL selectively kills both solid and hematologic cancer cells, but not normal counterparts. Here we evaluated the effect of PL on the proliferation and survival of B- cell acute lymphoblastic leukemia (B- ALL), including glucocorticoid (GC)- resistant B- ALL. Regardless of GC- resistance, PL inhibited the proliferation of all B- ALL cell lines, but not normal B cells, in a dose- and time- dependent manner and induced apoptosis via elevation of ROS. Interestingly, PL did not sensitize most of B- ALL cell lines to dexamethasone (DEX). Only Uo. C- B1 exhibited a weak synergistic effect between PL and DEX. All B- ALL cell lines tested exhibited constitutive activation of multiple transcription factors (TFs), including AP- 1, MYC, NF- . Treatment of the B- ALL cells with PL significantly downregulated these TFs and modulated their target genes. While activation of AURKB, BIRC5, E2. F1, and MYB m. RNA levels were significantly downregulated by PL, but SOX4 and XBP levels were increased by PL. Intriguingly, PL also increased the expression of p. B- ALL cells through a p. Given that these TFs and their target genes play critical roles in a variety of hematological malignancies, our findings provide a strong preclinical rationale for considering PL as a new therapeutic agent for the treatment of B- cell malignancies, including B- ALL and GC- resistant B- ALL. The stress response gene activating transcription factor 4 (ATF4) is involved in homeostasis and cellular protection. However, relatively little is known about the expression and function of ATF4 in esophageal squamous cell carcinoma (ESCC) MDR. In this study, we investigate the potential role and mechanisms of ATF4 in ESCC MDR. We demonstrated that overexpression of ATF4 promotes the MDR phenotype in ESCC cells, while depletion of ATF4 in the MDR ESCC cell line induces drug re- sensitization. We also demonstrated that ATF4 transactivates STAT3 expression by directly binding to the signal transducers and activators of transcription 3 (STAT3) promoter, resulting in MDR in ESCC cells. Significantly, inhibition of STAT3 by small interfering RNA (si. RNA) or a selective inhibitor (JSI- 1. In addition, increased Bcl- 2, survivin, and MRP1 expression levels were observed in ATF4- overexpressing cells. In conclusion, ATF4 may promote MDR in ESCC cells through the up- regulation of STAT3 expression, and thus is an attractive therapeutic target to combat therapeutic resistance in ESCC. We propose an additional generalized hallmark of malignant transformation corresponding to the differential expression of a family of mitochondrial nc. RNAs (ncmt. RNAs) that comprises sense and antisense members, all of which contain stem- loop structures. Normal proliferating cells express sense (Sncmt. RNA) and antisense (ASncmt. RNA) transcripts. In contrast, the ASncmt. RNAs are down- regulated in tumor cells regardless of tissue of origin. Here we show that knockdown of the low copy number of the ASncmt. RNAs in several tumor cell lines induces cell death by apoptosis without affecting the viability of normal cells. In addition, knockdown of ASncmt. RNAs potentiates apoptotic cell death by inhibiting survivin expression, a member of the inhibitor of apoptosis (IAP) family. Down- regulation of survivin is at the translational level and is probably mediated by micro. RNAs generated by dicing of the double- stranded stem of the ASncmt. RNAs, as suggested by evidence presented here, in which the ASncmt. RNAs are bound to Dicer and knockdown of the ASncmt. RNAs reduces reporter luciferase activity in a vector carrying the 3'- UTR of survivin m. RNA. Taken together, down- regulation of the ASncmt. RNAs constitutes a vulnerability or Achilles' heel of cancer cells, suggesting that the ASncmt. RNAs are promising targets for cancer therapy. Apr- Jun; 1. 0(2): 3. It was detected in 8. Also, the expression of survivin 2. According to the results, it can be concluded that survivin 2. The link between aberrant autophagy and cancer has been increasingly recognized. Survivin, an anti- apoptotic molecule, and the autophagy pathway are correlated with therapeutic responses to cancer. However, the role of autophagy in cancer progression remains unclear. Here, we generated survivin knockdown cells (survivin- KD) by introducing a short interfering RNA (si. RNA) into hepatocellular carcinoma (HCC) cells, and we observed a 2. KD cells, as determined by MTT assay. In addition, an increased number of stress granules, increased positive staining by acridine orange and a shift in the high side scatter (SSC) cell population in flow cytometry analysis were observed in survivin- KD cells.
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