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Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE131402 | GEO | 2020/06/17

REPOSITORIES: GEO

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Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [array]

Project description:Two glioblastoma cell lines (LN18 and HS863) were stable transfected with control empty vector (EV) or RNF123-vector (KPC1). The objective of this experiment was to determine NFKB1-targets regulated by RNF123 overexpression in glioblastoma cell lines. To do that LN18 and HS863 cell lines with RNF123 overexpression were compared to control empty vector. In the present study, we utilized the combination of RPPA and RNA-Sequencing. By comparing both datasets, we identified commonly proteins and genes differentially expressed in control versus RNF123-overexpressing cells.

2020-06-17 | GSE131399 | GEO

Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [RNA-seq]

Project description:We identified RNF123 (KPC1) ubiquitin E3 ligase is involved in glioblastoma progression through NF-kB-target SerpinE1. The goal of the RNA-Seq analysis is to determine the gene expression profile in LN18 cells overexpressing RNF123 compare to control empty vector (EV) cells. By integration of reverse-phase protein array (RPPA) and RNA-Seq data in glioblastoma cells, we determined NF-kB1-target genes that significantly changed by RNF123 overexpression.

2020-06-17 | GSE131400 | GEO

Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1

Project description:Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1

| PRJNA543481 | ENA

Downregulation of the Ubiquitin-E3 Ligase RNF123 Promotes Upregulation of the NF-?B1 Target SerpinE1 in Aggressive Glioblastoma Tumors.

Project description:This study examined the role of the ubiquitin E3-ligase RNF123 in modulating downstream NF-?B1 targets in glioblastoma (GB) tumor progression. Our findings revealed an oncogenic pathway (miR-155-5p-RNF123-NF-?B1-p50-SerpinE1) that may represent a new therapeutic target pathway for GB patients with isocitrate dehydrogenase 1 and 2 (IDH) WT (wild type). Mechanistically, we demonstrated that RNF123 is downregulated in IDH WT GB patients and leads to the reduction of p50 levels. RNA-sequencing, reverse-phase protein arrays, and in vitro functional assays on IDH WT GB cell lines with RNF123 overexpression showed that SerpinE1 was a downstream target that is negatively regulated by RNF123. SERPINE1 knockdown reduced the proliferation and invasion of IDH WT GB cell lines. Both SerpinE1 and miR-155-5p overexpression negatively modulated RNF123 expression. In clinical translational analysis, RNF123, SerpinE1, and miR-155-5p were all associated with poor outcomes in GB patients. Multivariable analysis in IDH WT GB patients showed that concurrent low RNF123 and high SerpinE1 was an independent prognostic factor in predicting poor overall survival (p < 0.001, hazard ratio (HR) = 2.93, 95% confidence interval (CI) 1.7-5.05), and an increased risk of recurrence (p < 0.001, relative risk (RR) = 3.56, 95% CI 1.61-7.83).

| S-EPMC7281601 | biostudies-literature

Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [array]

Project description:Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [array]

| PRJNA543487 | ENA

Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [RNA-seq]

Project description:Downregulation of the Ubiquitin-E3 Ligase KPC1 promotes glioblastoma progression through upregulation of SerpinE1 [RNA-seq]

| PRJNA543485 | ENA

The E3 Ubiquitin Ligase Peli1 Deficiency Promotes Atherosclerosis Progression.

Project description:BackgroundAtherosclerosis is a chronic inflammatory vascular disease and the main cause of death and morbidity. Emerging evidence suggests that ubiquitination plays an important role in the pathogenesis of atherosclerosis including control of vascular inflammation, vascular smooth muscle cell (VSMC) function and atherosclerotic plaque stability. Peli1 a type of E3 ubiquitin ligase has emerged as a critical regulator of innate and adaptive immunity, however, its role in atherosclerosis remains to be elucidated.MethodsApoe-/- mice and Peli1-deficient Apoe-/- Peli1-/- mice were subject to high cholesterol diet. Post sacrifice, serum was collected, and atherosclerotic plaque size and parameters of atherosclerotic plaque stability were evaluated. Immunoprofiling and foam cell quantification were performed.ResultsPeli1 deficiency does not affect atherosclerosis lesion burden and cholesterol levels, but promotes VSMCs foam cells formation, necrotic core expansion, collagen, and fibrous cap reduction. Apoe-/- Peli1-/- mice exhibit a storm of inflammatory cytokines, expansion of Th1, Th1, Th17, and Tfh cells, a decrease in regulatory T and B cells and induction of pro-atherogenic serum level of IgG2a and IgE.ConclusionsIn the present study, we uncover a crucial role for Peli1 in atherosclerosis as an important regulator of inflammation and VSMCs phenotypic modulation and subsequently atherosclerotic plaque destabilization.

| S-EPMC9265341 | biostudies-literature

Ubiquitin E3 ligase MARCH7 promotes ovarian tumor growth.

Project description:Ubiquitin E3 ligase MARCH7 is involved in T cell proliferation and neuronal development. We found that expression of MARCH7 was higher in ovarian cancer tissues than normal ovarian tissues. Silencing MARCH7 decreased cell proliferation, migration, and invasion. Ectopic expression of MARCH7 increased cell proliferation, migration and invasion. Silencing MARCH7 prevented ovarian cancer growth in mice. Silencing MARCH7 inhibited NFkB and Wnt/β-catenin pathway. In agreement, ectopically expressed MARCH7 activated NFkB and Wnt/β-catenin pathways. Finally, MARCH7 was regulated by miR-101. Thus, MARCH7 is oncogenic and a potential target (oncotarget) for ovarian cancer therapy.

| S-EPMC4494930 | biostudies-literature

CRL4Mahj E3 ubiquitin ligase promotes neural stem cell reactivation.

Project description:The ability of neural stem cells (NSCs) to transit between quiescence and proliferation is crucial for brain development and homeostasis. Drosophila Hippo pathway maintains NSC quiescence, but its regulation during brain development remains unknown. Here, we show that CRL4Mahj, an evolutionarily conserved E3 ubiquitin ligase, is essential for NSC reactivation (exit from quiescence). We demonstrate that damaged DNA-binding protein 1 (DDB1) and Cullin4, two core components of Cullin4-RING ligase (CRL4), are intrinsically required for NSC reactivation. We have identified a substrate receptor of CRL4, Mahjong (Mahj), which is necessary and sufficient for NSC reactivation. Moreover, we show that CRL4Mahj forms a protein complex with Warts (Wts/large tumor suppressor [Lats]), a kinase of the Hippo signaling pathway, and Mahj promotes the ubiquitination of Wts. Our genetic analyses further support the conclusion that CRL4Mahj triggers NSC reactivation by inhibition of Wts. Given that Cullin4B mutations cause mental retardation and cerebral malformation, similar regulatory mechanisms may be applied to the human brain.

| S-EPMC6553684 | biostudies-literature

E3 ubiquitin ligase HECTD2 mediates melanoma progression and immune evasion.

Project description:The ubiquitin-proteasome system maintains protein homoeostasis, underpins the cell cycle, and is dysregulated in cancer. However, the role of individual E3 ubiquitin ligases, which mediate the final step in ubiquitin-mediated proteolysis, remains incompletely understood. Identified through screening for cancer-specific endogenous retroviral transcripts, we show that the little-studied E3 ubiquitin ligase HECTD2 exerts dominant control of tumour progression in melanoma. HECTD2 cell autonomously drives the proliferation of human and murine melanoma cells by accelerating the cell cycle. HECTD2 additionally regulates cancer cell production of immune mediators, initiating multiple immune suppressive pathways, which include the cyclooxygenase 2 (COX2) pathway. Accordingly, higher HECTD2 expression is associated with weaker anti-tumour immunity and unfavourable outcome of PD-1 blockade in human melanoma and counteracts immunity against a model tumour antigen in murine melanoma. This central, multifaceted role of HECTD2 in cancer cell-autonomous proliferation and in immune evasion may provide a single target for a multipronged therapy of melanoma.

| S-EPMC8445817 | biostudies-literature

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