Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Soybean derived phosphatidylserine synthetically targets OTUB2 epigenetic silencing in squamous cell carcinoma

ABSTRACT: Soybean derived phosphatidylserine synthetically targets OTUB2 epigenetic silencing in squamous cell carcinoma

PROVIDER: PRJNA721679 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14229916_1.fastq.gz	Fastqsanger.gz
	SRR14229916_2.fastq.gz	Fastqsanger.gz
	SRR14229917_1.fastq.gz	Fastqsanger.gz
	SRR14229917_2.fastq.gz	Fastqsanger.gz
	SRR14229918_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 40

Similar Datasets

Soybean derived phosphatidylserine synthetically targets OTUB2 epigenetic silencing in squamous cell carcinoma

Project description:Oral and esophageal squamous cell carcinomas (SCCs) are associated with high mortality, yet molecular mechanisms underlying these malignancies are largely unknown. We demonstrate that epigenetic silencing of otubain 2 (OTUB2), a previously recognized oncogene, drives SSCs initiation and drug resistance. Mechanistically, OTUB2 promotes deubiquitination and phosphorylation of signal transducer and activator of transcription 1 (STAT1), then activates transcriptional regulation of calmodulin-like protein 3 (CALML3). Activation of CALML3-mediated mitochondrial calcium signaling promotes oxidative phosphorylation (OXPHOS) and glycerophospholipid synthesis, among which phosphatidylserine (PS) is the most obviously affected. Orally administered soybean-derived PS dramatically inhibits low-OTUB2-expressed SCC initiation and increased sensitivity to chemotherapy in various mouse models. Our study indicates that the OTUB2/STAT1/CALML3/PS axis plays a critical tumor-suppressive role in SCCs, clarifies the low incidence of oral and esophageal SCCs in Western countries with a high-fat diet and demonstrates the potential of food supplementation with PS as a strategy for treatment and prevention of SCCs.

2022-09-19 | GSE172001 | GEO

OTUB2 silencing promotes ovarian cancer via mitochondrial metabolic reprogramming and can be synthetically targeted by CA9 inhibition

Project description:These findings delineate the mechanism of OTUB2 epigenetic silencing in ovarian cancer, demonstrate the critical roles of OTUB2/SNX29P2 in inhibiting glycolysis and eliciting cuproptosis in cancer cells and suggest that CA9 inhibitor treatment is a promising therapeutic option for OTUB2-silenced tumors. To investigate the downstream pathway regulated by OTUB2/SNX29P2, we performed RNA sequencing (RNA-seq) in ES-2 cells expressing EV, OTUB2 or SNX29P2.

2024-04-19 | GSE232772 | GEO

OTUB2 silencing promotes ovarian cancer via mitochondrial metabolic reprogramming and can be synthetically targeted by CA9 inhibition

Project description:OTUB2 silencing promotes ovarian cancer via mitochondrial metabolic reprogramming and can be synthetically targeted by CA9 inhibition

| PRJNA973945 | ENA

Analysis of the differential expression of genes in Otub2- knockout mice

2022-09-19 | GSE171878 | GEO

The Deubiquitinating Enzyme Otub2 Modulates Pancreatic Beta-Cells Function and Survival

Project description:We have previously shown that otubain 2 (OTUB2), a deubiquitinating enzyme, inhibits caspase-3/7 activity in primary human islets; promotes insulin secretion and inhibits cytokine-induced nuclear factor-κB (NFκB) activity. In the present work we show that overexpression of Otub2 in MIN6 cells inhibits NFκB activity and the expression of its target genes MCP-1 and iNOS. Consequently, both the basal and the cytokine-induced apoptosis of cultured MIN6 cells and dispersed human islets were inhibited. Overexpression of Otub2 in MIN6 cells increase the mRNA levels of NKx6.1 and Glut2 and concomitantly increased glucose-stimulated insulin secretion (GSIS) (by 2-3-fold). The beneficial effects of Otub2 on β-cell function was demonstrated by the phenotype of Otub2-/+ and Otub2-/- mice, which manifested impaired glucose tolerance and increased expression of NFkB target genes (e.g. IP-10, MCP-1 and IL-1b). RNAseq analysis of pancreata derived from OTUB2 KO mice revealed reduced expression of genes that down regulate K+ transporters (e.g. Ank2, Cacna1a and Kcnab1) combined with an increase in oxidative phosphorylation related genes. Given that closure of K+ channels is crucial for insulin secretion, these results could account, at least in part, for the impaired GSIS in the OTUB2 KO mice. Indeed, mass-spectrometry analysis of proteins co-immunoprecipitated with Otub2 revealed the voltage-gated potassium channel subunit Kv9.3 as a major Otub2 binding-partner. Additional binding partners included the Peg3 and Camk2d proteins, which promote NFκB signaling and β-cell death. Hence, by deubiquitinating proteins in complexes that contain Peg3 and Camk2d, Otub2 might inhibit propagation of NFκB signaling and β-cell apoptosis. Collectively our findings implicate Otub2 as a key regulator of b cell function, mainly affecting NFkB signaling and the K+ channels that regulate insulin secretion.

2026-03-25 | GSE285973 | GEO

Cellular Validation of Chemically Improved Inhibitor Identifies Monoubiquitination on OTUB2

Project description:Ubiquitin thioesterase OTUB2, a cysteine protease from the ovarian tumor (OTU) deubiquitinase superfamily, is associated with enhanced expression during tumor progression and metastasis. Development of OTUB2 inhibitors is therefore believed to be therapeutically important, yet potent and selective small-molecule inhibitors targeting OTUB2 are scarce. Here, we describe the development of an improved OTUB2 inhibitor, LN5P45, comprising a chloroacethydrazide moiety that covalently reacts to the active-site cysteine residue. When added to cells, LN5P45 shows outstanding target engagement and proteome-wide selectivity. Importantly, we found that LN5P45 and the other OTUB2 inhibitors strongly induce monoubiquitination of OTUB2 via lysine 31. Thus, our findings provide novel insights for the design of future OTUB2-related therapeutics and open new questions regarding the understanding of OTUB2 regulation at the post-translational modification level.

2023-06-27 | PXD041346 | Pride

OTUB2 silencing promotes ovarian cancer via mitochondrial metabolic reprogramming and can be synthetically targeted by CA9 inhibition.

Project description: Not available

| S-EPMC11087800 | biostudies-literature

OTUB2/NR4A1 restrains the development of preeclampsia by suppressing macrophage M1 polarization

Project description:Preeclampsia is one of the most common pregnancy disorders, and characterized by insufficient trophoblast invasion and placental inflammation. RNA sequencing was performed using placental tissues collected from PE patients and control healthy pregnant women. The results showed that OTU deubiquitinase, ubiquitin aldehyde binding 2 (OTUB2) was downregulated in placenta from PE patients.

2025-08-20 | GSE303543 | GEO

Tafazzin Regulates Cell State by Modulating Phosphatidylethanolamine and Phosphatidylserine levels

Project description:Inhibiting tafazzin a cardiolipin remodeling enzyme reduces stemness of AML by modulating the level of phosphatidylserine

2019-03-28 | GSE107045 | GEO

Ptdsr-/- (phosphatidylserine receptor) fibroblasts

Project description:Phagocytosis of apoptotic cells is fundamental to animal development, immune function and cellular homeostasis. The phosphatidylserine receptor (Ptdsr) on phagocytes has been implicated in the recognition and engulfment of apoptotic cells and in anti-inflammatory signaling. Ptdsr is essential for the development and differentiation of multiple organs during embryogenesis. Ptdsr may thus have a novel, unexpected developmental function as an important differentiation-promoting gene. Moreover, Ptdsr is not required for apoptotic cell clearance by macrophages but seems to be necessary for the regulation of macrophage cytokine responses. Keywords: ptdsr, fibroblast, cDNA microarray experiments,

2007-03-01 | GSE6937 | 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