Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Inhibition of adhesion molecule gene expression and cell adhesion by the metabolic regulator PGC-1alpha

ABSTRACT: Cell adhesion plays an important role in determining cell shape and function in a variety of physiological and pathophysiological conditions. While links between metabolism and cell adhesion were previously suggested, the exact context and molecular details of such a cross-talk remain incompletely understood. Our study shows that PGC-1alpha, a pivotal transcriptional co-activator of metabolic gene expression, acts to inhibit expression of cell adhesion genes. Using cell lines as well as primary cells, we show that both endogenous and exogenous PGC-1a down-regulate expression of a variety of cell adhesion molecules.

OTHER RELATED OMICS DATASETS IN: PRJNA320774

ORGANISM(S): Mus musculus Homo sapiens

PROVIDER: GSE81171 | GEO | 2017/01/17

SECONDARY ACCESSION(S): PRJNA320774

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Analysis of TLS activity in PGC-1alpha+/+ and PGC-1alpha-/- hepatocytes

Project description:We found that TLS can work as a PGC-1alpha cofactor and this assay was carried out to test the functional dependency of TLS on PGC-1alpha on a whole genome scale

2013-07-26 | GSE23242 | GEO

Inhibition of adhesion molecule gene expression and cell adhesion by the metabolic regulator PGC-1alpha

Project description:Inhibition of adhesion molecule gene expression and cell adhesion by the metabolic regulator PGC-1alpha

| PRJNA320774 | ENA

Regulation of HSF1-mediated transcriptional programs by PGC-1alpha

Project description:We examined global gene expression patterns in response to PGC-1 expression in cells derived from liver or muscle. As our study revealed regulation of HSF1 by PGC-1alpha, in some experiments we knocked-down HSF1 using siRNAs in addition to inducing PGC-1alpha expression. Cells were grown in 24-well plates and adenoviruses encoding either GFP ("Ad-GFP"), PGC-1alpha ("Ad-PGC-1alpha") or PGC-1beta ("Ad-PGC-1beta") were directly added to the culture medium. For experiments involving siRNA transfections, cells were transfected with the indicated siRNAs 48hr prior to infection with adenoviruses encoding either GFP ("Ad-GFP") or PGC-1alpha ("Ad-PGC-1alpha").

2015-09-19 | E-GEOD-51498 | biostudies-arrayexpress

Pyruvate induces mitochondrial biogenesis by a PGC-1alpha independent mechanism

Project description:The present study examines the impact of altering energy provision on mitochondrial biogenesis in muscle cells. C2C12 myoblasts were chronically treated with supraphysiological levels of sodium pyruvate for 72 hr. Treated cells exhibited increased mitochondrial protein expression, basal respiratory rate and maximal oxidative capacity. The increase in mitochondrial biogenesis was independent of increases in PGC-1alpha and PGC-1alpha mRNA expression. To further assess whether PGC-1alpha expression was necessary for pyruvate action, cells were infected with adenovirus containing shRNA for PGC-1alpha prior to treatment with pyruvate. Despite a 70% reduction in PGC-1alpha mRNA the effect of pyruvate was preserved. Furthermore, pyruvate induced mitochondrial biogenesis in primary myoblasts from PGC-1alpha null mice. These data suggest that regulation of mitochondrial biogenesis by pyruvate in myoblasts is independent of PGC-1alpha, suggesting the existence of a novel energy-sensing pathway regulating oxidative capacity. Keywords: basal state versus treatment at one time point

2006-08-12 | GSE5497 | GEO

Regulation of HSF1-mediated transcriptional programs by PGC-1alpha

2015-09-19 | GSE51498 | GEO

Regulation of PGC-1alpha function by its C-terminal domain [RNA-seq]

Project description:PGC-1alpha has been proposed to couple gene transcription and RNA processing via SR-rich domains and an RNA recognition motif located at the C-terminal domain (CTD). However, the full extent by which the CTD of PGC-1alpha regulates its function in gene expression and RNA processing remains largely unknown. Here, we used RNA-seq to evaluate the effects of CTD deletion (dCTD) on PGC-1alpha function. We found that deletion of the CTD of PGC-1alpha virtually abolished its effects on transcriptome remodeling and the resulting increase in oxidative capacity in skeletal muscle cells. Moreover, we implemented in vitro affinity purification followed by sequencing (in vitro AP-seq), which revealed more than 700 RNAs bound to the CTD of PGC-1alpha. The majority of these RNAs were transcribed at DNA regulatory elements such as promoters and distal intergenic regions. These results demonstrate that PGC-1alpha function is highly modulated at the CTD via multivalent protein-RNA interactions.

2021-09-04 | GSE156592 | GEO

Analysis of TLS activity in PGC-1alpha+/+ and PGC-1alpha-/- hepatocytes

Project description:We found that TLS can work as a PGC-1alpha cofactor and this assay was carried out to test the functional dependency of TLS on PGC-1alpha on a whole genome scale Three independently-isolated cultures of primary hepatocytes from PGC-1Î±+/+ and PGC-1Î±-/- mice were infected with shTLS or control adenovirus. RNA was extracted by Trizol extraction, re-purified with RNAeasy (Invitrogen), and checked for integrity and quantity with the Agilent Bio-Analyzer QC. RNA was amplified and labeled with the One-Color Microarray-Based Gene Expression Analysis Protocol (Agilent Technologies, Palo Alto, CA, USA). Samples were hybridized to a G4122F 4x44K whole mouse genome microarray (Agilent Technologies). Arrays were scanned at 5 mm resolution with a G2565BA DNA microarray scanner (Agilent Technologies) at the default settings for 4x44k format one-color arrays. Images were analyzed using Feature Extraction software v10.1.1.1 (Agilent Technologies). Raw signals were thresholded to 1 and normalized by quantile (Bolstad et al., 2003) was performed using GeneSpring software. Data were analyzed on the log2 scale. Default flags were considered as absent, except for saturated spots that were flagged as marginal.

2013-07-26 | E-GEOD-23242 | biostudies-arrayexpress

Mitochondrial biogenesis induced by PGC-1alpha

Project description:Microarray time-course of mouse myotubes transduced with the transcriptional co-activator PGC-1alpha, which is known to induce mitochondrial biogenesis in muscle cells. Keywords: time course

2006-04-03 | GSE4330 | GEO

PGC-1a isoform-specific nuclear interactome

Project description:PGC-1α (Peroxisome proliferator-activated receptor gamma coactivator-1alpha) coactivators regulate adaptive gene expression in response to challenges such as cold exposure, fasting, or physical exercise to balance energy supply and demand. Transcription of a single PGC-1α gene produces different isoforms (e.g. PGC-1α1 to α4) with different biological functions. We aimed to characterize the nuclear interactome for each PGC-1α variant, in particular the transcription factors they bind to regulate gene expression. This was done by generating GST-fusions of all PGC-1a variants, expressed in an insect cell system. These were used to capture associated protein complexes from HeLa nuclear extracts.

2022-03-01 | PXD009232 | Pride

Progressive loss of PGC-1alpha expression in aging muscle potentiates glucose intolerance and systemic inflammation

Project description:Decreased mitochondrial mass and function in muscle of diabetic patients is associated with low PGC-1alpha, a transcriptional coactivator of the mitochondrial gene program. To investigate whether reduced PGC-1alpha and oxidative capacity in muscle directly contributes to age-related glucose intolerance, we compared the genetic signatures and metabolic profiles of aging mice lacking muscle PGC-1alpha. Microarray analysis revealed that a significant proportion of PGC-1alpha-dependent changes in gene expression overlapped with age-associated effects, and aging muscle and muscle lacking PGC-1alpha shared gene signatures of impaired electron transport chain activity and TGFbeta signalling.

2013-12-05 | GSE52550 | 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