Browse
Submit Data
Databases
API
Help

Unknown,Transcriptomics,Genomics,Proteomics

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The effect of aneuploidy on gene expression

ABSTRACT: Analysis of the gene expression changes observed in aneuploid b1 integrin YYFF MEFs generated as a result of repeated cytokinesis failure compared to tetraploid wild-type MEFs or tetraploid b1YYFF integrin MEFs. The results reveal aneuploidy-specific gene expression changes, both up-and downregulated genes uniquely detected in the aneuploid MEFs. Total RNA isolated from b1 integrin YYFF and B1 wildtype mouse embryonic fibroblasts that had been passaged on laminin 0, 4 or 8 times (L0, L4 or L8)

ORGANISM(S): Mus musculus

SUBMITTER: Gunilla Högnäs

PROVIDER: E-GEOD-23729 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

ACCESS DATA

Json Xml

Publications

Aneuploidy facilitates oncogenic transformation via specific genetic alterations, including Twist2 upregulation.

Högnäs Gunilla G Hämälistö Saara S Rilla Kirsi K Laine Jukka O JO Vilkki Vesa V Murumägi Astrid A Edgren Henrik H Kallioniemi Olli O Ivaska Johanna J

Carcinogenesis 20130520 9

Aneuploidy, deviation from the normal chromosome number, and other chromosomal aberrations are commonly observed in cancer. Integrin-mediated adhesion and dynamic turnover of adhesion sites are required for successful cytokinesis of normal adherent cells and impaired cell division can lead to the generation of cells with abnormal chromosome contents. We find that repeated cytokinesis failure, due to impaired integrin traffic alone, is sufficient to induce chromosome aberrations resulting in the ...[more]

PMID: 23689353

Similar Datasets

The effect of aneuploidy on gene expression

Project description:Analysis of the gene expression changes observed in aneuploid b1 integrin YYFF MEFs generated as a result of repeated cytokinesis failure compared to tetraploid wild-type MEFs or tetraploid b1YYFF integrin MEFs. The results reveal aneuploidy-specific gene expression changes, both up-and downregulated genes uniquely detected in the aneuploid MEFs.

2013-07-02 | GSE23729 | GEO

Cre-mediated deletion of b1 integrin in pancreatic b-cells

Project description:In this study, we investigated the function of beta integrins in developing islet beta-cells by targeting the deletion of exon 3 of the B1 integrin gene using a Cre-lox approach. Our results demonstrate that this class of integrin receptors is critically important for proper beta cell expansion during development

2013-07-31 | E-MEXP-3736 | biostudies-arrayexpress

Alternate covalent form of platelet αIIbβ3

Project description:The αIIbβ3 integrin receptor coordinates platelet adhesion, activation and mechanosensing in thrombosis and haemostasis. Using differential cysteine alkylation and mass spectrometry, we have identified a disulfide bond in the αIIb subunit linking cysteines 490 and 545 that is missing in about one in three integrin molecules on the resting and activated human platelet surface. This alternate covalent form of αIIbβ3 is pre-determined as it is also produced by human megakaryoblasts and bovine hamster kidney cells transfected with recombinant human integrin. From co-immunoprecipitation experiments, the alternate form selectively partitions into focal adhesions on the activated platelet surface. Its function was evaluated in bovine hamster kidney cells expressing a mutant integrin with an ablated C490-C545 disulfide bond. The disulfide mutant integrin has extended residency time in focal adhesions due to reduced rate of clathrin-mediated integrin internalisation and recycling that is associated with enhanced affinity of the αIIb subunit for clathrin adaptor protein-2. The alternate covalent form also has different conformational dynamics measured by monoclonal antibody binding and molecular dynamic simulations, which is reflected in reduced fibrinogen binding and outside-in signalling. These findings indicate that the αIIbβ3 integrin receptor is produced in different covalent forms that have different functions. The C490, C545 cysteine pair is conserved across all 18 integrin α subunits and the disulfide bond in αV in a cancer cell line is similarly missing, suggesting that this alternate integrin form and function is also conserved.

2022-02-17 | PXD025907 | Pride

Transcription profiling of mouse C2C12 myoblast induced with tetracycline to enhance integrin alpha7 expression

Project description:Analysis of C2C12 myoblast induced with tetracycline to enhance integrin alpha7 expression. Integrin alpha7 is the major laminin binding integrin in muscle cells. Enhancing its expression has been demonstrated to alleviate pathology in a murine model of Duchenne muscular dystrophy. Results of this study provide insights into the effects of increasing integirn alpha7 expression on muscle cells and possible side effects associate with enhancing integrin alpha7 in muscle cells. Experiment Overall Design: Triplicate biological smaples for each condition(induced and non-induced) C2C12 myoblast were used.

2008-06-16 | E-GEOD-8312 | biostudies-arrayexpress

Transcription profiling of mouse hair follicle stem cell

Project description:Mouse keratinocytes were isolated from K15-EGFP transgenic mice for FACS sorting. RNA samples from EGFP-high and alpha-6 integrin positive cells (hair follicle stem cells) and from EGFP negative and alpha-6 integrin positive cells were used for Microarray analysis.

2007-10-06 | E-GEOD-1096 | biostudies-arrayexpress

Expression data from MEFs wt cells starved as compared to MEFs wt cells grown in Normal Medium

Project description:In order to identify the effects of starvation on the MEFs wt trascriptome, we performed Affymetrix Gene-Chip hybridization experiments for the starved cells Transcriptome analysis of the starved MEFs wt cells For the analysis on the starved MEFs wt cells, total RNA was extracted; RNA extracted from MEFs wt cells grown in Normal Medium was used as control

2015-02-24 | E-GEOD-56671 | biostudies-arrayexpress

Extensive protein group SUMO modification of repressive chromatin factors distinguishes pluripotent from somatic cells

Project description:Post-translational modification by SUMO is a key regulator of cell identity. In mouse embryonic fibroblasts (MEFs), SUMO impedes reprogramming to pluripotency, while in embryonic stem cells (ESCs), it represses the emergence of totipotent-like cells, suggesting that SUMO targets distinct substrates to preserve somatic and pluripotent states. Using MS-based proteomics, we show that the composition of endogenous SUMOylomes differs dramatically between MEFs and ESCs. In MEFs, SUMO2/3 targets proteins associated with canonical SUMO functions, such as splicing, and transcriptional regulators driving somatic enhancer selection. In contrast, in ESCs, SUMO2/3 primarily modifies highly interconnected repressive chromatin complexes, thereby preventing chromatin opening and transitioning to totipotent-like states. We also characterize several SUMO-modified pluripotency factors and show that SUMOylation of Dppa2 and Dppa4 impedes the conversion to 2-cell-embryo-like states. Altogether, we propose that rewiring the repertoire of SUMO target networks is a major driver of cell fate decision during embryonic development.

2020-09-16 | PXD017697 | Pride

Integrin adhesion complex (IAC) analysis from human pancreatic ductal cells (HPDE)

Project description:Pancreatic ductal adenocarcinoma (PDAC) is characterised by an abundant desmoplastic reaction which includes an excess production of extracellular matrix and interacts with integrin adhesion receptors. Integrin adhesion complexes formed by HPDE cells (H6c7), with and without expression of mutant KRas G12V, were isolated and analysed by LC-MSMS

2022-05-20 | PXD027827 | Pride

General structural features that regulate integrin affinity revealed by atypical αVβ8

Project description:Integrins αVβ8 and αVβ6 are master activators of proTGF-βs. Whereas most integrins including αVβ6 are activated by tensile force applied by the cytoskeleton, αVβ8 links differently to the cytoskeleton and lacks the open headpiece conformation that represents the high affinity state of other integrins. Here, we shed light on the atypical activation mechanism of integrin αVβ8 using crystal structures in the absence and presence of proTGF-β1 peptide, comparisons of the hydrogen deuterium exchange dynamics of αVβ8 and αVβ6, and affinity measurements on mutants in which structurally atypical residues of αVβ8 and typical residues of αVβ6 were reciprocally exchanged.

2019-12-03 | PXD014348 | Pride

b1 integrin regulates epithelial proliferation and cell shape during alveolar repair

Project description:Integrins are extracellular matrix receptors comprised of an a and b subunit that connect and mediate signaling between cells and the surrounding matrix. In organogenesis of epithelial tissues, the b1 integrin subunit regulates essential epithelial cell functions, but the role of b1 integrin in epithelial repair is poorly understood. To define the role of b1 integrin during alveolar repair, we challenged b1 integrin deficient mice with intratracheal lipopolysaccharide, resulting in increased mortality with emphysematous lungs 21 days following injury. The alveolar barrier was repopulated with an overabundance of type 2 alveolar epithelial cells, with reduced numbers of elongated alveolar type 1 cells, suggesting b1 integrin is required for type 2 to type 1 epithelial transition. Consistent with this finding, b1 deficient type 2 epithelial cells proliferated at increased rates throughout repair, lacked actin-rich cellular protrusions necessary for lateral cellular extension, and exhibited transcriptomic dysregulation of adherens junction and actin polymerization pathways. Finally, we show that b1 integrin balances actin polymerization versus stabilization through GTPase activation. Taken together, these data support a novel role for b1 integrin in re-establishing the alveolar niche after injury through modulation of type 2 epithelial cell proliferation and cytoskeletal-dependent cell shape change.

2023-06-10 | GSE205882 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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