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RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in PyMT-BO1 breast cancer cells

ABSTRACT: We sought to transcriptomically characterize the effect of integrin β3 expression on breast cancer cell responses to the microtubule-inhibiting chemotherapeutic agent docetaxel. Experiments were performed in PyMT-BO1 murine breast cancer cells with CRISPR mediated deletion of the Itgb3 gene. Cells were subsequently retrovirally rescued using either an empty vector construct (pMx), a functional human integrin β3 construct (hβ3), or a signaling-deficient integrin β3 mutant.

ORGANISM(S): Mus musculus

PROVIDER: GSE166315 | GEO | 2021/02/08

REPOSITORIES: GEO

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RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in 4T1 breast cancer cells

Project description:We sought to transcriptomically characterize the effect of integrin β3 expression on breast cancer cell responses to the microtubule-inhibiting chemotherapeutic agent docetaxel. Experiments were performed in 4T1 murine breast cancer cells with or without CRISPR mediated deletion of the Itgb3 gene.

2021-02-11 | GSE166536 | GEO

IGDQ motogenic peptide gradient induces directional cell migration through integrin (αv)β3 activation in metastatic breast cancer

Project description:In the context of breast cancer metastasis study, we have shown in an in vitro model of cell migration that IGDQ-exposing (IsoLeu-Gly-Asp-Glutamine type I Fibronectin motif) monolayers (SAMs) on gold sustain the adhesion of MDA-MB-231 cells by triggering Focal Adhesion Kinase by activating integrins. Such tunable scaffolds are used to mimic the extracellular environment, inducing and controlling cell migration towards an anisotropic surface. The observed migratory behavior induced by the IGDQ-bearing peptide gradient along the surface suggests the presence of cell subpopulations: “stationary” or a “migratory” phenotype. We focused on the integrins α5(β1) and (αv)β3, already known to be implicated in cell migration. To this aim, a whole proteomic analysis was performed in beta 3 integrin (ITGB3) or alpha 5 integrin (ITGA5) knock-down MDA-MB-231, in order to highlight the pathways implied into the integrin-dependent cell migration. Our results showed that i) ITGB3 depletion influenced ITGA5 mRNA expression, ii) ITGB3 and ITGA5 were both necessary for IGDQ-mediated directional single cell migration, iii) integrin (αv)β3 was activated by IGDQ fibronectin type I motif and iv) co-regulation of retrograde transport of ITGB3 by ITGA5 is potentially necessary for directional IGDQ-mediated cell migration.

2022-11-08 | PXD024540 | Pride

RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in PyMT-BO1 breast cancer cells

Project description:RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in PyMT-BO1 breast cancer cells

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RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in 4T1 breast cancer cells

Project description:RNAseq analysis of integrin β3-mediated responses to in vitro docetaxel in 4T1 breast cancer cells

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Cancer burden is controlled by mural cell- β3-integrin regulated crosstalk with tumor cells

Project description:Phosphoproteomics analysis were performed in WT and β3-integrin-null pericytes. On the other hand, phosphoproteomics experiments were done in B16F0 melanoma cells treated for 24 hours with conditioned medium from WT and β3-integrin-null pericytes.

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The Itgb3 Adhesome - Integrin β3 is seen as a key anti-angiogenic target for cancer treatment due to its expression on neovasculature

Project description:Integrin β3 is seen as a key anti-angiogenic target for cancer treatment due to its expression on neovasculature, but the role it plays in the process is complex; whether it is pro- or anti-angiogenic depends on the context in which it is expressed. To understand precisely β3’s role in regulating integrin adhesion complexes in endothelial cells, we characterised, by mass spectrometry, the β3-dependent adhesome. We show that depletion of β3-integrin in this cell type leads to changes in microtubule behaviour that control their migration. β3-integrin regulates microtubule stability in endothelial cells through Rcc2/Anxa2 driven control of active Rac1 localisation. Our findings reveal that angiogenic processes, both in vitro and in vivo, are more sensitive to microtubule targeting agents when β3-integrin levels are reduced.

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Integrin beta 3 regulates cellular senescence by activating the TGFβ pathway

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Ileal Crohn’s disease exhibits reduced activity of phospholipase C-β3 (PLC-β3)-dependent Wnt/b-catenin signaling pathway [microarray]

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2024-10-06 | GSE244937 | GEO

Ileal Crohn’s disease exhibits reduced activity of phospholipase C-β3 (PLC-β3)-dependent Wnt/b-catenin signaling pathway [16S rRNA]

Project description:Crohn’s disease is a chronic, debilitating inflammatory bowel disease. Here we report a critical role for phospholipase C-β3 (PLC-β3) in intestinal homeostasis. In PLC-β3- deficient mice, exposure to oral dextran sodium sulfate induced lethality and severe inflammation in the small intestine. The lethality was due to PLC-3 deficiency in multiple non-hematopoietic cell types. PLC-β3 deficiency resulted in reduced Wnt/-catenin signaling, which is essential for homeostasis and regeneration of the intestinal epithelium. PLC-β3 regulated the Wnt/β-catenin pathway in small intestinal epithelial cells (IECs) at transcriptional, epigenetic, and potentially protein-protein interaction levels. PLC-β3- deficient IECs were unable to respond to stimulation by R-spondin 1, an enhancer of Wnt/β-catenin signaling. Reduced expression of PLC-β3 and its signature genes was found in biopsies of ileal Crohn’s disease patients. PLC-β regulation of Wnt signaling was evolutionally conserved in Drosophila. Our data indicate that reduction of PLC-β3- mediated Wnt/β-catenin signaling contributes to the pathogenesis of ileal Crohn’s disease.

2024-10-06 | GSE244936 | GEO

Ileal Crohn’s disease exhibits reduced activity of phospholipase C-β3 (PLC-β3)-dependent Wnt/b-catenin signaling pathway [ATAC-Seq]

Project description:Crohn’s disease is a chronic, debilitating inflammatory bowel disease. Here we report a critical role for phospholipase C-β3 (PLC-β3) in intestinal homeostasis. In PLC-β3- deficient mice, exposure to oral dextran sodium sulfate induced lethality and severe inflammation in the small intestine. The lethality was due to PLC-3 deficiency in multiple non-hematopoietic cell types. PLC-β3 deficiency resulted in reduced Wnt/-catenin signaling, which is essential for homeostasis and regeneration of the intestinal epithelium. PLC-β3 regulated the Wnt/β-catenin pathway in small intestinal epithelial cells (IECs) at transcriptional, epigenetic, and potentially protein-protein interaction levels. PLC-β3- deficient IECs were unable to respond to stimulation by R-spondin 1, an enhancer of Wnt/β-catenin signaling. Reduced expression of PLC-β3 and its signature genes was found in biopsies of ileal Crohn’s disease patients. PLC-β regulation of Wnt signaling was evolutionally conserved in Drosophila. Our data indicate that reduction of PLC-β3- mediated Wnt/β-catenin signaling contributes to the pathogenesis of ileal Crohn’s disease.

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