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A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a (show ATP7A Proteins), sp1 and sod1 (show SOD1 Proteins) in zebrafish.
zebrafish Sp1-like protein is structurally and functionally comparable to human Sp1
our study demonstrates that Sp1 is a major regulator in SRY (show SRY Proteins) gene transcription, and mutations of the Sp1 binding sites (Sp1-B and Sp1-C) in the 5' flanking region of SRY (show SRY Proteins) induce sex reversal in rabbits
The possible involvement of the GC box 1 at position - 54 in transcriptional regulation of Rbpms (show RBPMS Proteins) was corroborated by EMSA, which showed formation of a DNA-protein complex in the presence of the oligonucleotide corresponding to this Sp1 (show PSG1 Proteins)-binding site.
Our results suggested that BetA was able to enhance radiosensitization at least partially by downregulating Sp1 (show PSG1 Proteins) and upregulating PTEN through inducing Sp1 (show PSG1 Proteins) sumoylation. BetA is suggested to be a promising drug for increasing radiosensitization in oral squamous cell carcinoma radiotherapy.
Mutation of two Sp1 (show PSG1 Proteins) motifs strongly reduced trans-activation of the late UF1 promoter by HPyV9 large T-antigen in HeLa cells.
RhoGDIbeta overexpression led to downregulation of miR (show MLXIP Proteins)-200c, whereas miR (show MLXIP Proteins)-200c was able directly to target 3'-UTR of jnk2mRNA and attenuated JNK2 (show MAPK9 Proteins) protein translation, which resulted in attenuation of Sp1mRNA and protein expression in turn, inhibiting Sp1 (show PSG1 Proteins)-dependent MMP-2 (show MMP2 Proteins) transcription.
Results show that C-terminal domain of SP1 interacts malat1 M5 domain which regulates its expression and stability. In turn, SP1 promotes malat1 transcription, thus forming a positive feedback loop in lung adenocarcinoma cells.
Study demonstrated that Sp1 upregulation is common in castration-resistant prostate cancer (CRPC) tissues. Its knockdown significantly inhibited cell growth, aerobic glycolysis, and hypoxia-induced autophagy, which were accompanied by an increased G1 cell cycle arrest. These results provided evidence that Sp1 is an oncogene and positively regulates PKM2 in CRPC.
The induced expression of RIP3 (show RIPK3 Proteins) by UHRF1 (show UHRF1 Proteins) RNAi depends on the presence of Sp1 (show PSG1 Proteins). Remarkably, the ectopic expression of RIP3 (show RIPK3 Proteins) in RIP3 (show RIPK3 Proteins)-null cancer cells results in a decrease in tumor growth in mice. Therefore, our findings offer insights into RIP3 (show RIPK3 Proteins) expression control in cancer cells and suggest an inhibitory effect of RIP3 (show RIPK3 Proteins) on tumorigenesis.
Licochalcone A showed the anti-proliferative and apoptotic effect in breast cancer cells through regulating Sp1 (show PSG1 Proteins) and apoptosis-related proteins in a dose- and a time-dependent manner.
Results show that SP1 (show PSG1 Proteins) transactivation is prevented by KIBRA (show WWC1 Proteins) promoter methylation in clear cell renal cell carcinoma (show MOK Proteins).
Sp1 (show PSG1 Proteins) induces leptin (show LEP Proteins) expression in cooperation with estradiol action through estrogen receptor alpha (show ESR1 Proteins)
study demonstrates the co-expression of DLX3 (show DLX3 Proteins), PPARG (show PPARG Proteins) and SP1 in trophoblast binucleated cell (BNC)nuclei; this suggests a possible role of these transcription factors through BNC specific genes at the time of pre-placental differentiation
likely involvement of the Sp family in regulating PTH (show PTH Proteins) gene expression through interactions with an Sp1 DNA element in the hormone's promoter.
These results demonstrate that the single nucleotide polymorphism alters the bovine FASN promoter activity in vitro and the Sp1/Sp3 binding ability of the sequence.
The coordinate regulation of the bovine PRNP (show PRNP Proteins) promoter suggests the two Sp1 binding site polymorphisms control Sp1 binding to the PRNP (show PRNP Proteins) promoter and its activity.
an immunoprecipitation assay indicated that hypoxia triggered activation of the binding activity of Sp1 to the promoters of PARP-1 (show PARP1 Proteins) and caspase-3 (show CASP3 Proteins), which is abrogated by miR (show MLXIP Proteins)-7a/b. In summary, these findings identified miR (show MLXIP Proteins)-7a/b as protectors of cardiac remodeling and hypoxia-induced injury in H9c2 cardiomyoblasts involving Sp1 and PARP-1 (show PARP1 Proteins).
Immunoblotting, qPCR, ChIP and siRNA-mediated gene knockdown studies revealed that the activation of phosphatidylinositol 3-kinase/protein kinase C zeta (show PRKCZ Proteins) pathways in poly(I:C)-stimulated cells underlies Sp1 phosphorylation and recruitment to the mCRAMP promoter, leading to enhanced transcription
The Genomic Context and Corecruitment of SP1 Affect ERRalpha Coactivation by PGC-1alpha in Muscle Cells
These results suggest that Sp1 regulates gene expression of AACS (show AACS Proteins) in Neuro-2a cells and ketone body utilization affects the balance of histone acetylation.
the results obtained in this study show that Znf179 (show RNF112 Proteins) autoregulation through Sp1-dependent mechanism plays an important role in neuroprotection, and NGF (show NGFB Proteins)-induced Sp1 signaling may help attenuate more extensive (ROS (show ROS1 Proteins)-induced) damage following brain injury
Using MA, we demonstrated Sp1 as a critical stemness-related transcriptional factor protecting GBM cells against stress- and TMZ-induced death. Thus, Sp1 inhibition may prevent recurrence of malignant cells persisting after primary therapy.
Results suggest that 25-hydroxycholesterol (25-HC) induced the interaction between NFATc1 (show NFATC1 Proteins) and Sp1, reducing the level of free Sp1 to inhibit microRNA miR (show MLXIP Proteins)-139-5p expression and promote osteoclastogenesis.
data indicated that (-)-Epicatechin inhibited AngII-induced cardiac hypertrophy by activating the SP1/SIRT1 (show SIRT1 Proteins) signaling pathway.
This resulted in Sp1 displacement from the promoter and binding of Sp3 to it, leading to p300 recruitment and histone acetylation, activating transcription. This is the first study addressing the mechanisms of physiological TLR5 expression in the intestine. Additionally, a novel insight is gained into Sp1/Sp3-mediated gene regulation that may apply to other genes
adrenergic stimulation induced complex formation between Ifrd1 (show IFRD1 Proteins), Sp1 and mSIN3B, which is a component of the SIN (show POLR3E Proteins) complex containing histone deacetylase (show HDAC1 Proteins), in brown adipocytes. These findings, therefore, suggest that Ifrd1 (show IFRD1 Proteins) could be a pivotal negative regulator of sympathetic regulation of thermogenic and mitochondrial gene expression in brown adipocytes by interacting with Sp1 and the mSIN3 complex.
The protein encoded by this gene is a zinc finger transcription factor that binds to GC-rich motifs of many promoters. The encoded protein is involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Post-translational modifications such as phosphorylation, acetylation, glycosylation, and proteolytic processing significantly affect the activity of this protein, which can be an activator or a repressor. Three transcript variants encoding different isoforms have been found for this gene.
, transcription factor Sp1
, transcription factor
, Sp1 transcription factor
, transcription factor Sp1-like
, specificity protein 1
, specific protein-1
, trans-acting transcription factor 1