Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

FBP1 expression in basal-like breast cancer MDA-MB231 and Hs578T cells

ABSTRACT: FBP1 is a rate limiting enzyme in glucogenogenesis and FBP1 expression changes cells to oxidative phosphorylation. Expressing FBP1 in basal-like breast cancer cells, which lack the expression of this enzyme, will identify the genes involved in glycolysis.

ORGANISM(S): Homo sapiens

PROVIDER: GSE41158 | GEO | 2012/09/27

SECONDARY ACCESSION(S): PRJNA175939

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

FBP1 expression in basal-like breast cancer MDA-MB231 and Hs578T cells

Project description:FBP1 is a rate limiting enzyme in glucogenogenesis and FBP1 expression changes cells to oxidative phosphorylation. Expressing FBP1 in basal-like breast cancer cells, which lack the expression of this enzyme, will identify the genes involved in glycolysis. FBP1 was expressed in MDA-MB231 and Hs578T cells, stable clones were selected, and RNA was prepared for microarray analysis.

2012-09-27 | E-GEOD-41158 | biostudies-arrayexpress

FBP1 expression in basal-like breast cancer MDA-MB231 and Hs578T cells

| S-ECPF-GEOD-41158 | biostudies-other

FBP1 overexpression in MDA-MB-231 breast cancer cells

Project description:Fructose 1,6 bisphosphatase the key enzyme of gluconeogenesis has emerged as a potential metabolic tumor suppressor. In breast cancer distinct FBP1 expression levels are found depending on subtype. In MDA-MB-231 FBP1 expression is suppressed. To get more insight into potential functions of FBP1 we introduced a vector to reintroduce expression of FBP1. These experiments are part of a more comprehensive study on expression of FBP1 in breast cancer cells.

2023-10-02 | GSE244288 | GEO

An EZH2-FBP1 Feedback Circuitry Promotes Tumorigenesis in Gluconeogenic Tissues

Project description:We report that enhancer of zeste homologue 2 (EZH2) represses the expression of a rate-limiting gluconeogenic enzyme fructose-1, 6 -bisphosphatase 1 (FBP1) to promote tumorigenesis. More intriguingly, FBP1 inhibits EZH2 methyltransferase activity by binding EZH2 at targeted loci and dissembles the polycomb complex, which constitutes a negative feedback loop for EZH2-initiated signalings. We performed ChIP-Seq assays using the EZH2 and H3K27me3 antibody in HCC cells with vector control, FBP1 wild-type (WT) or FBP1 S169A re-expression. FBP1 WT severely reduced EZH2 and H3K27me3 signals. Conversely, FBP1 S169A exhibits much less effects on global or target-specific H3K27me3. In addition, ChIP-Seq assays with the FBP1 uncover a significant overlap between EZH2 and FBP1 binding sites, confirming that FBP1 inhibits EZH2 though physical interactions in the vicinity of chromosomes. Collectively, these studies reveal an unexpected crosstalk between metabolic and epigenetic events, and identify a new mechanistic circuitry highlighting EZH2 inhibitors as liver and kidney cancer therapeutics.

2019-03-12 | GSE128137 | GEO

FBP1 associated proteins: FBP1 immunoprecipitants

Project description:To determine whether FBP1 has previously unknown tumor suppressor activity, we immunoprecipitated FBP1 from Huh7 HCC cells and performed mass spectrometry analyses of FBP1 immunoprecipitants.

2024-03-12 | PXD050213 | Pride

FBP1 acts as a protein phosphatase to dephosphorylate histone H3

Project description:We report nuclear FBP1 interacts with PPARa and binds to the promoter regions of PPARa-mediated b-oxidation genes. S170-phosphorylated FBP1 with an altered catalytic domain structure functions as a protein phosphatase that dephosphorylates histone H3 at T11 and suppresses PPARa-mediated gene expression. Chromatin immunoprecipitation DNA-sequencing (ChIP-seq) for FBP1 and PPARa with glucose deprivation in L02 cells.

2022-10-04 | GSE207844 | GEO

Escherichia coli FBP1

Project description:Escherichia coli FBP1 Genome sequencing and assembly

| PRJNA224244 | ENA

FBP1 overexpression in MDA-MB-231 breast cancer cells

Project description:FBP1 overexpression in MDA-MB-231 breast cancer cells

| PRJNA1022090 | ENA

FBP1 loss disrupts liver metabolism and promotes tumourigenesis through a hepatic stellate cell senescence secretome

Project description:Crosstalk between deregulated hepatocyte metabolism and cells within the tumour microenvironment, and consequent effects on liver tumourigenesis, are incompletely understood. We show here that hepatocyte specific loss of the gluconeogenic enzyme fructose 1,6-bisphosphatase 1 (FBP1) disrupts liver metabolic homeostasis and promotes tumour progression. FBP1 is universally silenced in both human and murine liver tumours, and hepatocyte-specific Fbp1 deletion results in steatosis, concomitant with activation and senescence of hepatic stellate cells (HSCs), exhibiting a senescence-associated secretory phenotype (SASP). Depleting senescent HSCs by senolytic treatment with dasatinib/quercetin or ABT-263 inhibits tumour progression. We further demonstrate that FBP1-deficient hepatocytes promote HSC activation by releasing HMGB1; blocking its release with the small molecule inflachromene limits FBP1-dependent HSC activation, subsequent SASP development, and tumour progression. Collectively, these findings provide genetic evidence for FBP1 as a metabolic tumour suppressor in liver cancer and establish a critical link between hepatocyte metabolism and HSC senescence that promotes tumour growth.

2020-03-02 | MSV000085045 | MassIVE

FBP1 loss disrupts liver metabolism and results in distinct transcriptome

Project description:This study set out to globally compare the liver transcriptomes from 24-week old wild type (WT) and FBP1-deficient mice. Total RNA was isolated from 10 snap frozen liver tissue samples using RNeasy Mini Kit (Qiagen). 250~300 bp insert eukaryotic mRNA derived cDNA non-directional libraryRNA libraries were prepared using standard Illumina protocols. The sequencing were performed on Illumina Platform PE150, with 20M raw reads/sample.

2019-08-10 | GSE135616 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data