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Expression data of the human multiple myeloma cell line LME-1 after AKT inhibition in a FOXO1 deficient background

ABSTRACT: Expression data of the human multiple myeloma cell line LME-1 after AKT inhibition in a FOXO1 deficient background

PROVIDER: PRJNA495067 | ENA |

REPOSITORIES: ENA

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Expression data of the human multiple myeloma cell line LME-1 after AKT inhibition in a FOXO1 deficient background

Project description:Forkhead box O transcription factors are important downstream targets of AKT signalling. In the human Multiple Myeloma celline LME-1 AKT inhibtion leads to cell death in a FOXO1 dependent fashion. We used microarrays to asses which genes are up- or downregulated by FOXO1 after AKT inhibition by MK2206.

2020-09-02 | GSE120940 | GEO

Expression data of the human multiple myeloma cell line MM1.S after AKT inhibition in a FOXO3 deficient background

Project description:Forkhead box O transcription factors are important downstream targets of AKT signalling. In the human Multiple Myeloma celline MM1.S, AKT inhibtion leads to cell death in a FOXO3 dependent fashion. We used microarrays to asses which genes are up- or downregulated by FOXO3 after AKT inhibition by MK2206.

2020-09-02 | GSE120939 | GEO

Expression data of the human multiple myeloma cell line XG-3 after AKT inhibition in a FOXO3 deficient background

Project description:Forkhead box O transcription factors are important downstream targets of AKT signalling. In the human Multiple Myeloma celline XG-3, AKT inhibtion leads to cell death in a FOXO3 dependent fashion. We used microarrays to asses which genes are up- or downregulated by FOXO3 after AKT inhibition by MK2206.

2020-09-02 | GSE120938 | GEO

Expression data of the human multiple myeloma cell line MM1.S after AKT inhibition in a FOXO3 deficient background

Project description:Expression data of the human multiple myeloma cell line MM1.S after AKT inhibition in a FOXO3 deficient background

| PRJNA495068 | ENA

Expression data of the human multiple myeloma cell line XG-3 after AKT inhibition in a FOXO3 deficient background

Project description:Expression data of the human multiple myeloma cell line XG-3 after AKT inhibition in a FOXO3 deficient background

| PRJNA495069 | ENA

Novel Foxo1-dependent Transcriptional Programs Control Treg Cell Function [ChIP-Seq]

Project description:Regulatory T (Treg) cells characterized by expression of the transcription factor forkhead box P3 (Foxp3) maintain immune homeostasis by suppressing self-destructive immune responses1-4. Foxp3 operates as a late acting differentiation factor controlling Treg cell homeostasis and function5, whereas the early Treg cell lineage commitment is regulated by the Akt kinase and the forkhead box O (Foxo) family of transcription factors6-10. However, whether Foxo proteins act beyond the Treg cell commitment stage to control Treg cell homeostasis and function remains largely unexplored. Here we show that Foxo1 is a pivotal regulator of Treg cell function. Treg cells express high amounts of Foxo1, and display reduced T-cell receptor-induced Akt activation, Foxo1 phosphorylation, and Foxo1 nuclear exclusion. Mice with Treg cell-specific deletion of Foxo1 develop a fatal inflammatory disorder similar in severity to Foxp3-deficient mice, but without the loss of Treg cells. Genome-wide analysis of Foxo1 binding sites reveals ~300 Foxo1-bound target genes, including the proinflammatory cytokine Ifng, that do not appear to be directly regulated by Foxp3. These findings demonstrate that the evolutionarily ancient Akt-Foxo1 signaling module controls a novel genetic program indispensable for Treg cell function. Treg cells were isolated from wild-type B6 mice or Foxo1tagBirA mice in which foxo1 is endogenously biotinylated. Foxo1 binding targets in Treg cells were identified by using Foxo1 antibody- and Streptavidin- ChIP-Seq approaches.

2012-09-07 | E-GEOD-40656 | biostudies-arrayexpress

Novel Foxo1-dependent Transcriptional Programs Control Treg Cell Function [Affymetrix gene expression data]

Project description:Regulatory T (Treg) cells characterized by expression of the transcription factor forkhead box P3 (Foxp3) maintain immune homeostasis by suppressing self-destructive immune responses1-4. Foxp3 operates as a late acting differentiation factor controlling Treg cell homeostasis and function5, whereas the early Treg cell lineage commitment is regulated by the Akt kinase and the forkhead box O (Foxo) family of transcription factors6-10. However, whether Foxo proteins act beyond the Treg cell commitment stage to control Treg cell homeostasis and function remains largely unexplored. Here we show that Foxo1 is a pivotal regulator of Treg cell function. Treg cells express high amounts of Foxo1, and display reduced T-cell receptor-induced Akt activation, Foxo1 phosphorylation, and Foxo1 nuclear exclusion. Mice with Treg cell-specific deletion of Foxo1 develop a fatal inflammatory disorder similar in severity to Foxp3-deficient mice, but without the loss of Treg cells. Genome-wide analysis of Foxo1 binding sites reveals ~300 Foxo1-bound target genes, including the proinflammatory cytokine Ifng, that do not appear to be directly regulated by Foxp3. These findings demonstrate that the evolutionarily ancient Akt-Foxo1 signaling module controls a novel genetic program indispensable for Treg cell function. Regulatory T cells were FACS sorted in WT mice (2 reps), Foxo1 KO mice (2 reps), mice expressing a constitutively active form of Foxo1 (1 rep), and Foxo1 KO mice expressing constitutively active Foxo1. We identified genes differentially expressed in WT vs. KO mice and assessed whether expression was recovered in the KO in presence of constitutively active Foxo1

2012-09-07 | E-GEOD-40655 | biostudies-arrayexpress

Multiple myeloma

Project description:Multiple myeloma

| PRJNA515992 | ENA

Trasncripional regulation by overexpression of constitutively active FOXO1 (CA-FOXO1) in human endothelial cells

Project description:To identify genes regulated by FOXO1, we performed RNA-seq analysis of human unbilical vein endothelial cells (HUVECs) overexpressing CA-FOXO1 by adenovirus. CA-FOXO1 is constructed by mutating three amino-acids phosphorylated by Akt, T24, S256, and S319, and is constitutively localized in the nucleus compared to wild-type FOXO1.

2024-03-01 | GSE220503 | GEO

Serum protein N-glycosylation changes in multiple myeloma

Project description:<h4><strong>BACKGROUND:</strong> Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies only detected limited serum N-glycan features.</h4><h4><strong>METHODS:</strong> Here, a more detailed study of the human serum N-glycome of 91 multiple myeloma patients and 51 controls was performed. We additionally analyzed sequential samples from patients (n = 7) which were obtained at different time points during disease development as well as 16 paired blood serum and bone marrow plasma samples. N-glycans were enzymatically released and measured by mass spectrometry after linkage specific derivatization of sialic acids.</h4><h4><strong>RESULTS:</strong> A decrease in both α2,3- and α2,6-sialylation, galactosylation and an increase in fucosylation within complex-type N-glycans were found in multiple myeloma patients compared to controls, as well as a decrease in difucosylation of diantennary glycans. The observed glycosylation changes were present in all ISS stages, including the 'low-risk' ISS I. In individual patients, difucosylation of diantennary glycans decreased with development of the disease. Protein N-glycosylation features from blood and bone marrow showed strong correlation. Moreover, associations of monoclonal immunoglobulin (M-protein) and albumin levels with glycan traits were discovered in multiple myeloma patients.</h4><h4><strong>CONCLUSIONS & GENERAL SIGNIFICANCE: </strong>In conclusion, serum protein N-glycosylation analysis could successfully distinguish multiple myeloma from healthy controls. Further studies are needed to assess the potential roles of glycan trait changes and the associations of glycans with clinical parameters in multiple myeloma early detection and prognosis.</h4>

2022-04-27 | MTBLS676 | MetaboLights

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