RUNX1T1 & HDAC1 Protein Protein Interaction Antibody Pair
- Known as:
- RUNX1T1 & HDAC1 Protein Protein Interaction Antibody Pair
- Catalog number:
- DI0488
- Product Quantity:
- 1 Set
- Category:
- -
- Supplier:
- Abno
- Gene target:
- RUNX1T1 & HDAC1 Protein Interaction Antibody Pair
Related genes to: RUNX1T1 & HDAC1 Protein Protein Interaction Antibody Pair
- Gene:
- HDAC1 NIH gene
- Name:
- histone deacetylase 1
- Previous symbol:
- RPD3L1
- Synonyms:
- HD1, GON-10, KDAC1
- Chromosome:
- 1p35.2-p35.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-15
- Date modifiied:
- 2019-02-19
- Gene:
- RUNX1T1 NIH gene
- Name:
- RUNX1 translocation partner 1
- Previous symbol:
- AML1T1, CBFA2T1
- Synonyms:
- CDR, ETO, MTG8, ZMYND2
- Chromosome:
- 8q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-12-16
- Date modifiied:
- 2016-10-05
Related products to: RUNX1T1 & HDAC1 Protein Protein Interaction Antibody Pair
Related articles to: RUNX1T1 & HDAC1 Protein Protein Interaction Antibody Pair
- Embryo-uterine interaction during embryo implantation depends on the coordinated expression of numerous genes in the receptive endometrium. While DNA methylation is known to play a significant role in controlling gene expression, specific molecular mechanisms underlying this regulatory event remain elusive in early porcine pregnancy. Here, we investigated the genome-wide DNA methylation landscape in the Yorkshire and Meishan pig's endometrium. The results revealed a higher degree of DNA methylation modifications on gene promoter regions on day 32 of pregnancy compared to that on day 18 of pregnancy. By integrating the mRNA and methylation profiles, leukemia inhibitory factor receptor (LIFR) was identified as a differentially methylated and expressed gene, crucial in early pregnancy. LIFR expression is epigenetically silenced via promoter hypermethylation from days 18 to 32 of pregnancy. Moreover, functional assays demonstrated that LIFR knockdown inhibited the proliferation, adhesion, and migration of endometrial epithelial cells (EECs) and downregulated the expression of STAT3 signaling and pregnancy-related genes. In vivo studies further revealed a reduction of implanted mouse embryos upon loss of function of LIFR. Furthermore, RUNX1 up-regulates LIFR expression by binding to the differentially methylated region (DMR) of the LIFR promoter. High levels of RUNX1T1, in turn, recruit RUNX1/HDAC1/DNMTs to assemble a regulatory complex that silences LIFR expression through the same locus. Collectively, our findings shed light on the role of dynamic DNA methylation and the epigenetic regulation of LIFR on embryo implantation in early swine pregnancy. - Source: PubMed
Publication date: 2025/01/04
Zhou ChangfanHuang ShuntaoZheng ShuailongPius LenoxLiu MinXu Dequan - The histone deacetylase (HDAC) family limited accessibility to chromatin containing tumor suppressor genes by removing acetyl groups, which was deemed a path for tumorigenesis. Considering glioma remained one of the most common brain cancers with a dichotomy prognosis and limited therapy responses, HDAC inhibitors were an area of intensive research. However, the expression profiles and prognostic value of the HDACs required more elucidation. Multiple biomedical databases were incorporated, including ONCOMINE, GEPIA, TCGA, CGGA, GEO, TIMER, cBioPortal, and Metascape, to study expression profiles, prognostic value, immune infiltration, mutation status, and enrichment of HDACs in glioma. STRING and GeneMANIA databases were used to identify -related molecules. LASSO regression, Cox regression, Kaplan-Meier plot, and receiver operating characteristic (ROC) analyses were performed for -related signature construction and validation. was significantly overexpressed in glioma, while was downregulated in glioblastoma. Except for , the HDAC family expression was significantly associated with glioma grade. Most of the HDAC family also correlated with glioma genetic mutations. Higher expression level predicted more dismal overall survival (OS) ( < 0.0001) and disease-free survival (DFS) ( < 0.0001), but a higher level of held more favorable OS ( = 2.1e-14) and DFS ( = 4.8e-08). displayed the highest mutation ratio, at 2.6% of the family. The prognostic value of was validated with ROC achieving 0.70, 0.77, 0.75, and 0.80 as separability for 1-, 3-, 5-, and 10-years OS predictions in glioma, respectively. Moreover, expression positively correlated with neutrophil (r = 0.60, = 2.88e-47) and CD4 T cell infiltration (r = 0.52, = 3.96e-35) in lower-grade glioma. The final -related signature comprised of , (Hazard Ratio:1.49, 95%Confidence Interval:1.20-1.86), , , and , and was verified by survival analysis ( < 0.0001) and ROC with 0.80, 0.84, 0.83, and 0.88 as separability for 1-, 3-, 5-, and 10-years OS predictions, respectively. The signature was enriched in chromatin binding. HDAC family was of clinical significance for glioma. Most of the HDAC family significantly correlated with the glioma grade, mutation, and codeletion. was both a prognostic and immune infiltration indicator and a central component of the -related signature for precise prognosis prediction in glioma. - Source: PubMed
Publication date: 2021/09/01
Fan YuxiangPeng XinyuWang YuboLi BaoqinZhao Gang - AML1/ETO fusion gene is one of disease-causing genes of t(8;21)-positive acute myeloid leukemia (AML). Oroxylin A (OA) has showed anticancer effects on other cancer cells. Here, studies were conducted to determine the antileukemia effect of OA on t(8;21)-positive AML cells in vitro and in vivo. - Source: PubMed
Publication date: 2016/04/16
Hui HuiZhang XiaoxiaoLi HuiLiu XiaoShen LeZhu YuXu JingyanGuo QinglongLu Na - We analysed the in vitro effects of a new hydroxamate derivative, ITF2357, on AML cells. ITF2357 potently induced histone acetylation. ITF2357 0.1 microM blocked proliferation and induced apoptosis in AML1/ETO-positive Kasumi-1 cells, while AML1/ETO-negative HL60, THP1 and NB4 cell lines were sensitive only to 1 microM ITF2357. Apoptosis was induced by 0.1 microM ITF2357 in AML1/ETO-positive primary blasts and U937-A/E cells induced to express AML1/ETO, but not in U937-A/E cells non-expressing AML1/ETO. In Kasumi-1 cells 0.1 microM ITF2357 induced AML1/ETO degradation through a caspase-dependent mechanism. ITF2357 0.1 microM also determined DNMT1 efflux from, and p300 influx to, the nucleus. Moreover, 0.1 microM ITF2357 determined local H4 acetylation and release of DNMT1, HDAC1 and AML1/ETO, paralleled by recruitment of p300 to the IL-3 gene promoter. ITF2357 treatment, however, did not induce re-expression of IL-3 gene. Accordingly, the methylation level of IL-3 promoter, as well as of several other genes, was unmodified. In conclusion, ITF2357 emerged as an anti-leukaemic agent very potent on AML cells, and on AML1/ETO-positive cells in particular. More relevantly, clearly emerged from our results that ITF2357 could be an ideal agent to treat AML subtypes presenting AML1/ETO fusion protein which determine HDAC involvement in leukaemogenesis. - Source: PubMed
Publication date: 2007/09/24
Barbetti VGozzini ARovida EMorandi ASpinelli EFossati GMascagni PLübbert MDello Sbarba PSantini V - Gfi-1 and Gfi-1B can repress transcription and play important roles in hematopoietic cell survival and differentiation. Although these proteins are known to bind DNA through a C-terminal zinc-finger domain and may require an N-terminal SNAG domain (SNAIL/Gfi-1) to repress transcription, the mechanism by which Gfi-1 and Gfi-1B act is unknown. A first step towards understanding the mechanism by which these proteins repress transcription is to identify interacting proteins that could contribute to transcriptional repression. ETO (also termed MTG8), was first identified through its involvement in the (8;21) translocation associated with acute myelogenous leukemia. It attaches to the nuclear matrix and associates with histone deacetylases and the co-repressors N-CoR, SMRT, and mSin3A, and may act as a co-repressor for site-specific transcriptions factors. In this report we demonstrate that Gfi-1 interacts with ETO and related proteins both in vitro and in vivo and with histone deacetylase proteins in vivo. We observed that a portion of Gfi-1 and Gfi-1B associated with the nuclear matrix, as is the case with ETO. Moreover, Gfi-1 and ETO co-localize to punctate subnuclear structures. When co-expressed in mammalian cells, Gfi-1 associates with histone deacetylse-1 (HDAC-1), HDAC-2, and HDAC-3. These data identify ETO as a partner for Gfi-1 and Gfi-1B, and suggest that Gfi-1 proteins repress transcription through recruitment of histone deacetylase-containing complexes. - Source: PubMed
McGhee LauraBryan JoshElliott LizaGrimes H LeightonKazanjian AvedisDavis J NathanMeyers Shari