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Upregulation of BMI1 correlates with advanced stages of breast neoplasm, poor prognosis and resistance to radiation and chemotherapy. BMI1 seems to be a key player in EMT (Montrer ITK Protéines), chemo-resistance and cancer stemness. Studies showed that reduction of BMI protein level in tumor cells results in inhibition of cell proliferation, induction of apoptosis, and increases susceptibility to cytotoxic agents and radiation therapy. [review]
Down-regulating Bmi-1 may inhibit the biological properties of CD133+ LCSC by blocking NF-kappaB (Montrer NFKB1 Protéines) signaling pathway, which lays a scientific foundation for the clinical treatment of liver cancer.
BMI1 expression is not associated with Colorectal Cancer.
these findings provide further evidence on the tumor-suppression function of miR (Montrer MLXIP Protéines)-630 in breast cancer, and clarify BMI1 as a novel functional target gene of miR (Montrer MLXIP Protéines)-630.
BMI1 is a potential biomarker in epithelial ovarian cancermanagement, especially for tumor progression and chemo-resistance. Molecular traits, including BMI1 and core genes in Focal adhesion and PI3K (Montrer PIK3CA Protéines)/AKT (Montrer AKT1 Protéines) pathways, might be alternatives as therapeutic targets for EOC.
Through radiotherapy and chemotherapy assays, the function of miR (Montrer MLXIP Protéines)-128a on chemoradiotherapy was evaluated. The correlation of miR (Montrer MLXIP Protéines)-128a with BMI1 was identified by performing real-time PCR.
Study demonstrated that BMI-1 was overexpressed in oesophageal squamous cell cancer (ESCC) cells and was related to poor prognosis in ESCC patients. Its knockdown induces radiosensitivity in ESCC and significantly inhibits cell viability, which may contribute to an increased proportion of cells in the G0/G1 phase and cell apoptosis via suppression of the PI3K (Montrer PIK3CA Protéines)/Akt (Montrer AKT1 Protéines) signaling pathway.
Interaction of BMI1 with polyhomeotic protein PHC2 (Montrer PhC2 Protéines) and homo-oligomerization via ubiquitin-like domain are necessary for H2A ubiquitination activity of PRC1 (Montrer PRC1 Protéines) and for clonogenic potential of U2OS cells.
ur results reveal that miR (Montrer MLXIP Protéines)-203a may regulate cholesteatoma growth and proliferation by targeting Bmi1. These findings provide insight for the development of novel nonsurgical options for cholesteatoma.
that the down-regulated Bmi-1 might inhibit the proliferation, invasion, and migration of gastrointestinal stromal tumor cells
Bmi1 is a marker for a distinct population of castration-resistant luminal epithelial cells enriched in the proximal prostate that can serve as a cell of origin for prostate cancer
Findings extend current knowledge of the role of BMI1 and CHD7 in medulloblastoma pathogenesis, and they raise the possibility that pharmacological targeting of BMI1 or ERK may be particularly indicated in a subgroup of MB with low expression levels of CHD7
Many Bmi1-positive cells within the tongue cancer specimens failed to proliferate.
High Expressions of BMI1 is associated with breast cancer.
of Bmi1 in lymphocytes can stimulate osteogenesis in vivo and partially rescue defects in skeletal growth and osteogenesis.
miR (Montrer MLXIP Protéines)-203 is repressed by EZH2 (Montrer EZH2 Protéines) in both embryonic and adult neural stem/progenitor cells (NSPCs). MiR (Montrer MLXIP Protéines)-203 negatively regulates the proliferation of NSPCs. One of PRC1 (Montrer PRC1 Protéines) components, Bmi1, is a downstream target of miR (Montrer MLXIP Protéines)-203 in NSPCs.
Data suggest BMI1 overexpression as a novel mechanism leading to EphA7 (Montrer EPHA7 Protéines) inactivation via H3K27 trimethylation and DNA methylation (Montrer HELLS Protéines) by which BMI-1 controls cell proliferation in the postnatal lateral ventricle wall.
Bmi1 plays an important role in regulating the proliferation of cochlear supporting cells.
Results from this study indicate that estrogen deficiency downregulates BMI-1 and subsequently increases ROS (Montrer ROS1 Protéines), T cell activation, and RANKL (Montrer TNFSF11 Protéines) production in T cells, thus enhancing osteoclastogenesis and accelerating bone loss.
ompounding a previously described Bmi1-transgene and Pten-deficiency prostate cancer mouse model with the Ezh2 (Montrer EZH2 Protéines) transgene did not enhance tumour progression or drive metastasis formation. In conclusion, we here report the generation of a wildtype Ezh2 (Montrer EZH2 Protéines) overexpression mouse model that allows for intravital surveillance of tissues with activated transgene
Bmi1 acts immediately downstream of CCAAT enhancer binding protein-alpha (Montrer CEBPA Protéines) to regulate the survival and self-renewal of hematopoietic stem cells and contribute to the erythropoietic dysplasia.
Pig Bmi1 cDNA is 3,193 bp in length and consists of a 981 bp open reading frame, a 256 bp 5 (Montrer HSPD1 Protéines)' untranslated region (UTR), and a 1,956 bp 3 (Montrer BST1 Protéines)' UTR. The transcript contains no signal peptides and there are no transmembrane regions in the pig Bmi1 coded protein.
Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones\; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity).
B lymphoma Mo-MLV insertion region 1 homolog
, murine leukemia viral (bmi-1) oncogene homolog
, polycomb complex protein BMI-1
, polycomb group RING finger protein 4
, polycomb group protein Bmi1
, ring finger protein 51
, BMI1 polycomb ring finger oncogene
, B lymphoma Mo-MLV insertion region 1
, polycomb group ring finger 4
, polycomb complex protein BMI-1-A
, polycomb group RING finger protein 4-A
, B lymphoma Mo-MLV insertion region
, Polycomb group RING finger protein 4-B
, polycomb complex protein BMI-1-B
, polycomb group RING finger protein 4-B
, oncoprotein BMI-1