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PU.1 3'UTR attenuates TNFalphainduced proliferation and cytokine release of RAFLS by acting as a ceRNA for FOXO3 (Montrer FOXO3 Protéines) to regulate miR155 activity.
Inhibition of endogenous miR (Montrer MLXIP Protéines)-155 in B cells of rheumatoid arthritis patients restores PU.1 and reduces production of antibodies.
PU.1 binds to OX40L promoter in dendritic cells (Montrer ETS1 Protéines).
These results bring indirect evidence that leukemia develops from cells which have bypassed Spi1-induced senescence. Overall, our results reveal senescence as a Spi1-induced anti-proliferative mechanism that may be a safeguard against the development of acute myeloid leukemia (Montrer BCL11A Protéines).
In contrast, expression of Spi1/PU.1 in a Fli1 (Montrer FLI1 Protéines) producing erythroleukemia cell line in which fli1 (Montrer FLI1 Protéines) is activated, resulted in increased proliferation through activation of growth promoting proteins MAPK (Montrer MAPK1 Protéines), AKT (Montrer AKT1 Protéines), cMYC (Montrer MYC Protéines) and JAK2 (Montrer JAK2 Protéines)
Data show that protein phosphatase-1 (Montrer PPP1CB Protéines) alpha (PP1alpha (Montrer PPP1CA Protéines)) is required to maintain checkpoint kinase 1 (CHK1 (Montrer CHEK1 Protéines)) in a dephosphorylated state and for the accelerated replication fork progression in Spi1/PU.1 transcription factor-overexpressing cells.
PU.1 supports TRAIL-induced cell death by inhibiting RelA (Montrer NFkBP65 Protéines)-mediated cell survival and inducing DR5 (Montrer TNFRSF10B Protéines) expression.
PU.1 and IL-9 (Montrer IL9 Protéines) may play a role in AD pathogenesis and relate to disease severity and clinical eruption types.
PU.1-induced apoptosis in myeloma cells is associated with IRF4 (Montrer IRF4 Protéines) downregulation and subsequent IRF7 (Montrer IRF7 Protéines) upregulation.
Most cases of histiocytic sarcoma expressed histiocytic markers CD68 (Montrer CD68 Protéines) (6 of 7 cases), CD163 (Montrer CD163 Protéines) (5 of 5 cases), and PU.1 (3 of 4 cases).
Mice lacking both PU.1 and SpiB (Montrer SPIB Protéines) in mature B cells do not generate germinal centers and high-affinity antibody after protein immunization. PU.1 and SpiB (Montrer SPIB Protéines) double-deficient B cells have a survival defect after engagement of CD40 (Montrer CD40 Protéines) or Toll (Montrer TLR4 Protéines)-like receptors (TLR), despite paradoxically enhanced plasma cell differentiation.
PU.1 can bind directly to the most-proximal Ets (Montrer ETS1 Protéines) motif, which is essential for the transcriptional function of the mouse OX40L (Montrer TNFSF4 Protéines) promoter in dendritic cells.
PU.1 suppresses Sirt1 (Montrer SIRT1 Protéines) translation via transcriptional promotion of miR (Montrer MLXIP Protéines)-34a/-29c.
The analysis points to a critical role for Hoxa9 (Montrer HOXA9 Protéines) and PU.1 in distal regulation of c-myb (Montrer MYB Protéines) expression in murine myeloid cells during iL-6 (Montrer IL6 Protéines)-induced cell differentiation.
These studies reveal an important role for PU.1 in the regulation of Igkappa transcription and rearrangement and a requirement for PU.1 and Spi-B (Montrer SPIB Protéines) in B cell development.
expression of an essential mediator of neutrophil terminal differentiation, the ets transcription factor PU.1, was significantly decreased in Hbb(th3/+) neutrophils in a model of beta-thalassemia
Moreover, the expression of a cell proliferation marker Ki67 (Montrer MKI67 Protéines) was significantly decreased in tumors from the mice not taking doxycycline, compared with that of tumors from the mice continuously taking doxycycline. The present data strongly suggest that PU.1 functions as a tumor suppressor of myeloma cells in vivo.
the affinities of two sequence-divergent ETS (Montrer ETS1 Protéines) homologs, PU.1 and Ets-1 (Montrer ETS1 Protéines), to DNA sites harboring a hemi- and fully methylated CpG dinucleotide, were measured.
this study shows that PU.1 functions as a positive regulator of CD11c (Montrer ITGAX Protéines) gene expression by directly binding to the Itgax (Montrer ITGAX Protéines) promoter and through transactivation of the Irf4 (Montrer IRF4 Protéines) gene
Here we demonstrate that the transcription factors SPI1 (PU.1) and HOXC13 synergistically regulate Zfp521 expression, and identify the regions of the Zfp521 promoter required for this transcriptional activity. We also show that SPI1 and HOXC13 activate Zfp521 in a dose-dependent manner.
Data show that Spi1 is a downstream target of histone demethylase Jmjd3 (Jmjd3) during myelopoiesis.
The vertical and paralleled Pu.1/Spi-b (Montrer SPIB Protéines) regulatory networks control the development of rostral blood island and ventral wall of dorsal aorta-borne macrophages by regulating Irf8 (Montrer IRF8 Protéines).
eaf1 (Montrer EAF1 Protéines) has a role in suppressing foxo3b expression to modulate transcriptional activity of gata1 (Montrer GATA1 Protéines) and spi1 in primitive hematopoiesis
Our results indicate that Kzp (Montrer ANPEP Protéines) is a critical transcriptional factor for the expression of gata2 and pu.1 to modulate primitive hematopoiesis.
Runx1 (Montrer RUNX1 Protéines) is induced by high Pu.1 level and in turn transrepresses pu.1 expression, thus constituting a negative feedback loop that fashions a favorable Pu.1 level required for balanced fate commitment to neutrophils versus macrophages.
The authors show that tif1gamma (Montrer TRIM33 Protéines) modulates the erythroid versus myeloid fate outcomes from HSCs by differentially controlling the levels of gata1 (Montrer GATA1 Protéines) and pu.1.
found a gene group downregulated on spi1 knockdown,containing all 5 previously identified Spi1-dependent genes as well as a large set of novel immune-related genes
In zebrafish, spi1 marks a rostral population of LPM cells committed to a myeloid fate anatomically separated from and developmentally independent of erythroid commitment in the caudal LPM.
This gene encodes an ETS-domain transcription factor that activates gene expression during myeloid and B-lymphoid cell development. The nuclear protein binds to a purine-rich sequence known as the PU-box found near the promoters of target genes, and regulates their expression in coordination with other transcription factors and cofactors. The protein can also regulate alternative splicing of target genes. Multiple transcript variants encoding different isoforms have been found for this gene.
31 kDa transforming protein
, 31 kDa-transforming protein
, SPI-1 proto-oncogene
, hematopoietic transcription factor PU.1
, spleen focus forming virus (SFFV) proviral integration oncogene spi1
, transcription factor PU.1
, SFFV proviral integration 1 protein
, SFFV proviral integration 1
, spleen focus forming virus proviral integration oncogene spi1
, transcription factor spi1
, Spi-1/PU.1 transcription factor
, LOW QUALITY PROTEIN: transcription factor PU.1
, spleen focus forming virus (SFFV) proviral integration oncogene