Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteome analysis of pig heart tissue to study the molecular consequences of hyperbaric oxygen treatment

ABSTRACT: The overall goal of the project was to confirm the presence of different energetic states of mitochondrial subpopulations depending on their subcellular localization within cardiomyocytes, i.e., subsarcolemmal (SSM) and interfibrillar mitochondria (IFM). Here we analysed proteomic changes upon treatment of pigs with hyperbaric oxygen.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Sus Scrofa Domesticus (domestic Pig)

TISSUE(S): Heart

SUBMITTER: Ilka Wittig

LAB HEAD: Marten Szibor

PROVIDER: PXD047678 | Pride | 2024-06-22

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	160427_Z01_HBO_fullProteome_Ctr_1110_pellet_B.raw	Raw
	160427_Z01_HBO_fullProteome_Ctr_1110_pellet_C.raw	Raw
	160427_Z01_HBO_fullProteome_Ctr_1110_pellet_DE.raw	Raw
	160427_Z01_HBO_fullProteome_Ctr_1110_supernatant_B.raw	Raw
	160427_Z01_HBO_fullProteome_Ctr_1110_supernatant_SCX126.raw	Raw

Items per page:

1 - 5 of 99

Publications

Hyperbaric oxygen treatment reveals spatiotemporal OXPHOS plasticity in the porcine heart.

Heidler Juliana J Cabrera-Orefice Alfredo A Wittig Ilka I Heyne Estelle E Tomczak Jan-Niklas JN Petersen Bjoern B Henze Dirk D Pohjoismäki Jaakko L O JLO Szibor Marten M

PNAS nexus 20240530 6

Cardiomyocytes meet their high ATP demand almost exclusively by oxidative phosphorylation (OXPHOS). Adequate oxygen supply is an essential prerequisite to keep OXPHOS operational. At least two spatially distinct mitochondrial subpopulations facilitate OXPHOS in cardiomyocytes, i.e. subsarcolemmal (SSM) and interfibrillar mitochondria (IFM). Their intracellular localization below the sarcolemma or buried deep between the sarcomeres suggests different oxygen availability. Here, we studied SSM and ...[more]

PMID: 38881840

Similar Datasets

Complexome profiling of mitochondrial protein complexes from pig heart to study the molecular consequences of hyperbaric oxygen treatment

Project description:The overall goal of the project was to confirm the presence of different energetic states of mitochondrial subpopulations depending on their subcellular localization within cardiomyocytes, i.e., subsarcolemmal (SSM) and interfibrillar mitochondria (IFM). At the same time, we aimed to elucidate possible respiratory plasticity of mitochondrial states in response to oxygen availability because of treatment with hyperbaric oxygen. The results could form the basis for a more efficient therapy of contractile dysfunction of the heart but also of other diseases if they are due to mitochondrial respiratory dysfunction caused by a lack of tissue oxygenation.

2024-06-22 | PXD035554 | Pride

Identification of lncRNA CALA-dependent protein interaction partners of G3BP1 in the cytoplasm

Project description:We previously identified the stimuli-responsive lncRNA CALA to impact endothelial cell function and identified G3BP1 as a main interaction partner of CALA in the cytoplasm of human umblical vein endothelial cells (HUVECs). To uncover the role of the lncRNA CALA in G3BP1-RNPs in the cytoplasm, we purified the G3BP1 interactome in control and CALA-silenced HUVECs via anti-G3BP1 immunoprecipitation followed by mass spectrometry. We thereby uncover the basal G3BP1 protein interactome in HUVECs and additionally identify lncRNA-dependent protein interactions of G3BP1 in the cytoplasm of HUVEC.

2022-07-04 | PXD033517 | Pride

Identification of protein interaction partners of the lncRNA ADPGK-AS1

Project description:M2-like macrophage upregulated lncRNA ADPGK-AS1 regulates macrophage phenotype and modulates the influence of macrophages on lung tumor apoptosis and migration. Here we identified proteins that interact with ADPGK-AS1 that might give insight into how this regulation this is regulated on molecular level. We were able to identify interaction with mitochondrial ribosomal proteins, leading to regulation of mitochondrial oxidative phosphorylation.

2023-08-13 | PXD030605 | Pride

Identification of proteins that interact with the lncRNA Sarrah

Project description:Long non-coding RNAs (lncRNAs) contribute to (patho)physiological processes in the heart. Aging is the major risk factor for cardiovascular disease. Apoptosis of individual cardiomyocytes is one of the underlying causes for age-related cardiac dysfunction. Here, we identified the lncRNA Sarrah that is regulated during aging in cardiomyocytes and show that it has a protective effect on the myocardium. We used an RNA pulldown approach to identify proteins interacting with endogenous Sarrah to determine the mechanism by which Sarrah induces a cardioprotective gene expression pattern.

2020-04-01 | PXD018315 | Pride

Identification of protein interaction partners of the lncRNA Lassie

Project description:The shear stress-regulated lncRNA LASSIE interferes with endothelial cell function as knockdown of Lassie affects apoptosis, proliferation and angiogenic sprouting in vitro. RNA-antisense purification and subsequent mass spectrometry analysis identifed junctional proteins (such as PECAM-1) as interactors of LASSIE . Additional functional analyses demonstrate a role of LASSIE in shear stress sensing and barrier function in endothelial cells, by stabilizing endothelial cell junctions through connection to the cytoskeleton.

2021-07-22 | PXD018724 | Pride

Label-free quantification of proteins in wild type and CLPP-null mouse embryonic fibroblasts

Project description:We studied consequences of genetic deletion of mitochondrial peptidase CLPP for global proteome profile in unstressed cells.

2022-02-16 | PXD023677 | Pride

Identification of NOS3 interacting proteins

Project description:The endothelial nitric oxide (NO) synthase (eNOS, or NOS3) can be activated in response to fluid shear stress and numerous agonists via cellular events such as increased intracellular Ca2+, interaction with substrate, co-factors as well as adaptor and regulatory proteins, protein phosphorylation and S-glutathionylation in addition to shuttling between distinct sub-cellular domains. While some protein interactors modulate enzymatic activity, others can be S-nitrosation targets, which are brought in close proximity to the NO source under specific conditions. The identification of proteins interacting with eNOS in human endothelial cells stimulated with serum and growth factors may provide new insight into the regulation of eNOS activity as well as NO signaling via S-nitrosation.

2021-09-08 | PXD013755 | Pride

Identification of interacting proteins with U4 snRNA with and without USP39

Project description:RNA splicing and protein degradation systems allow the functional adaptation of the proteome in response to changing cellular contexts. However, the regulatory mechanisms connecting these processes remain poorly understood. Here, we show that impaired spliceosome assembly caused by USP39 deficiency leads to a pathogenic splicing profile characterized by the use of cryptic 5′ splice sites. We performed MS analysis to identify the main interactors of U4 snRNA with and without USP39

2024-09-25 | PXD050688 | Pride

VE-cadherin associated proteins in the absence of lncRNA LASSIE

Project description:The shear stress-regulated lncRNA LASSIE interacts with junctional proteins (e.g. PECAM-1, which interacts with VE-cadherin) and influences endothelial barrier function. Here we characterize the remodeling of the VE-Cadherin complex by the lncRNA LASSIE. LASSIE silenced HUVECs were subjected to co-immunoprecipitation using an anti-VE-cadherin antibody. Differentially associated proteins were identified by Mass spectrometry. This analysis revealed a significantly decreased association of cytoskeleton-linked proteins with VE-cadherin after silencing of LASSIE. Functional assays confirmed this result and characterized LASSIE as a stabilizer of junctional complexes in endothelial cells, important for normal shear stress sensing and barrier function.

2021-09-09 | PXD018725 | Pride

Protein interaction partners of long non-coding RNA NUDT6 in human aortic smooth muscle cells

Project description:The long non-coding RNA NUDT6 was found to be deregulated in abdominal aortic aneurysm (AAA) with higher expression in diseased human tissue specimens versus control aortic tissue. Apart from the already well-studied DNA: RNA interaction as a natural antisense transcript to Fibroblast Growth Factor 2 (FGF2), we were interested in identifying protein interaction partners to unravel further involvement in the pathogenesis and progression of abdominal aortic aneurysm. Therefore, we performed a RNA pulldown experiment using biotinylated NUDT6 and control RNA in human aortic smooth muscle cell lysate to identify further interaction partners.

2024-01-26 | PXD033922 | Pride

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