Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Investigation of plasma-derived extracellular vesicles in hypertrophic cardiomyopathy patients: insights from an Italian cohort

ABSTRACT: We applied a label-free mass spectrometry-based proteomic approach to comprehensively characterize the protein cargo of plasma-derived extracellular vesicles (EVs) in individuals with a diagnosis of hypertrophic cardiomyopathy (HCM) compared with healthy volunteers to explore their potential as a diagnostic tool.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma, Extracellular Vesicle

DISEASE(S): Hypertrophic Cardiomyopathy

SUBMITTER: Erica Gianazza

LAB HEAD: Cristina Banfi

PROVIDER: PXD080896 | Pride | 2026-08-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	CTR16_150525_UDMSE_120min_01.mzML	Mzml
	CTR16_150525_UDMSE_120min_03.mzML	Mzml
	CTR17_150525_UDMSE_120min_01.mzML	Mzml
	CTR17_150525_UDMSE_120min_02.mzML	Mzml
	CTR1_120525_UDMSE_120min_01.mzML	Mzml

Items per page:

1 - 5 of 43

Similar Datasets

The effects of silencing PCYOX1 on the proteome of mitochondria isolated from murine cardiomyocites HL-1

Project description:In order to evaluate the impact of PCYOX1 deletion on cardiomyocytes, we applied a label-free mass spectrometry-based proteomic approach to compare the proteome of mitochondria from Hl-1 after PCYOX1 gene silencing. Pcyox1 was silenced using shRNA lentiviral particles. Control cells were treated with shRNA lentiviral particles containing a negative construct.

2026-04-27 | PXD040093 | Pride

The effects of silencing PCYOX1 on the proteome of murine cardiomyocites HL-1

Project description:In order to evaluate the impact of PCYOX1 deletion on cardiomyocytes, we applied a label-free mass spectrometry-based proteomic approach to compare the proteome of Hl-1 after PCYOX1 gene silencing, at basal conditions, after hypoxia and after hypoxia/reoxygenation. Pcyox1 was silenced using shRNA lentiviral particles. Control cells were treated with shRNA lentiviral particles containing a negative construct.

2026-04-27 | PXD040095 | Pride

The effects of silencing PCYOX1 on the proteome of murine fibroblast cells 3t3-L1 differentiated to adipocyte-like cells

Project description:In order to evaluate the impact of PCYOX1 deletion on adipogenesis, we applied a label-free mass spectrometry-based proteomic approach to compare the proteome of 3T3-L1 differentiated for 9 days to adipocytes after PCYOX1 gene silencing. Pcyox1 was silenced using shRNA lentiviral particles. Control cells were treated with shRNA lentiviral particles containing a negative construct.

2023-05-10 | PXD039943 | Pride

The effects of silencing PTX3 oin the proteome of human endothelial cells

Project description:The human long pentraxin PTX3 has complex regulatory roles at the crossroad of innate immunity, inflammation, and tissue repair. PTX3 can be produced by various cell types, including vascular endothelial cells (ECs), in response to pro-inflammatory cytokines or bacterial molecules. But PTX3 has also been involved in the regulation of cardiovascular biology, even if contrasting results have been so far provided in both preclinical and clinical research. Therefore, we compared the proteomic profiles of human ECs isolated from umbilical cords (Human Umbilical Vein ECs, HUVECs), and we identified 19 proteins more abundant in the proteome of control ECs and 23 proteins more expressed in PTX3 silenced cells.

2023-03-11 | PXD036691 | Pride

The SIRT1 activating compound SRT2104 exerts exercise mimetic effects and promotes Duchenne muscular dystrophy recovery

Project description:Duchenne muscular dystrophy (DMD) is a rare and devastating genetic disorder, whose management is still a major challenge, despite progress in genetic and pharmacological disease-modifying treatments have been made. Mitochondrial dysfunctions contribute to DMD, however, there are no effective mitochondrial therapies for DMD. SIRT1 is a NAD+-dependent class III histone deacetylase that controls several key processes and whose impairment is involved in determining mitochondrial dysfunction in DMD. In addition to well-known resveratrol, other potent selective activators of SIRT1 exist, with better pharmacokinetics properties. Among these, SRT2104 is the most promising and advanced in clinical studies. Here we unveil the beneficial effects of SRT2104 in flies, mice, and patient-derived myoblasts as different models of DMD, demonstrating an anti-inflammatory, anti-fibrotic, and pro-regenerative action of the drug. We also elucidate, by molecular dynamics simulations, that a conformational selection mechanism is responsible for the activation of SIRT1. Further, the impact of SRT2104 in reshaping muscle proteome and acetylome profiles has been investigated, highlighting the drug as an attractive exercise mimetic for the treatment of DMD. Overall, our data suggest SRT2104 as a possible therapeutic candidate to successfully counteract the progression of the dystrophic phenotype in DMD.

2025-05-07 | PXD055878 | Pride

Gender differences in human endothelial cell secretome

Project description:We performed proteomic and gene ontology (GO) analyses of secretome from human serum-deprived male and female endothelial cells (ECs).

2021-09-09 | PXD020375 | Pride

Effects of prenylcysteine oxidase 1 (PCYOX1) silencing on HepG2 cell secretome

Project description:We performed a label free mass spectrometry-based proteomic analysis to investigate the effects of PCYOX1 silencing on the secretome of human HepG2 cells

2021-10-12 | PXD022302 | Pride

Normal human mitral valve proteome: a preliminary investigation by gel-based and gel-free proteomic approaches

Project description:The mitral valve is a highly complex structure which regulates blood flow from the left atrium to the left ventricle (LV) avoiding a significant forward gradient during diastole or regurgitation during systole. The integrity of the mitral valve is also essential for the maintenance of normal LV size, geometry, and function. Significant advances in the comprehension of the biological, functional, and mechanical behavior of the mitral valve have recently been made. However, current knowledge of protein components in the normal human mitral valve is still limited and complicated by the low cellularity of this tissue and the presence of high abundant proteins from the extracellular matrix. We employed here an integrated proteomic approach to analyse the protein composition of the normal human mitral valve and reported confident identification of 422 proteins, some of which have not been previously described in this tissue. In particular, we described the ability of pre-MS separation technique based on liquid-phase IEF and SDS-PAGE to identify the largest number of proteins. These initial results provide a valuable basis for future studies aimed at analysing in depth the mitral valve protein composition and at investigating potential pathogenetic molecular mechanisms.

2016-08-18 | PXD004397 | Pride

Reanalysis of Pandey lab's draft of the human proteome

Project description:The availability of human genome sequence has transformed biomedical research over the past decade. However, an equivalent map for the human proteome with direct measurements of proteins and peptides was lacking. To this end, Akhilesh Pandey's lab reported a draft map of the human proteome based on high resolution Fourier transform mass spectrometry-based proteomics technology, which included an in-depth proteomic profiling of 30 histologically normal human samples including 17 adult tissues, 7 fetal tissues and 6 purified primary hematopoietic cells ( http://dx.doi.org/10.1038/nature13302 ). The profiling resulted in identification of proteins encoded by greater than 17,000 genes accounting for ~84% of the total annotated protein-coding genes in humans. This large human proteome catalog (available as an interactive web-based resource at http://www.humanproteomemap.org) complements available human genome and transcriptome data to accelerate biomedical research in health and disease. Pandey's lab and collaborators request that those considering use of this primary dataset for commercial purposes contact pandey@jhmi.edu. The full details of this study can be found in the PRIDE database: www.ebi.ac.uk/pride/archive/projects/PXD000561/. This ArrayExpress entry represents a top level summary of the metadata only which formed the basis of the reanalysis performed by Joyti Choudhary's team ( jc4@sanger.ac.uk ), results of which are presented in the Expression Atlas at EMBL-EBI : http://www.ebi.ac.uk/gxa/experiments/E-PROT-1.

2015-03-10 | E-PROT-1 | biostudies-arrayexpress

Neisseria meningitides small RNA's regulate Citric acid cycle activity under Feast and Famine conditions

Project description:We identified twin small non-coding RNAs regulating tricarboxylic acid (TCA) cycle activity in Neisseria meningitidis. Expression of TCA cycle enzymes was elevated in sRNA deletion mutants. Direct interaction between sRNAs and the ribosomal entry sites on target mRNAs was demonstrated. Expression of the sRNAs was down-regulated in cells grown in poor medium with glucose as the sole carbon source but not without lrp, indicating that sRNA expression is controlled by the stringent response. N. meningitidis, over-expressing the sRNAs replicated in blood, but not in human cerebrospinal fluid. In addition, Lrp synthesis was inhibited by direct interaction between the sRNA and the 5’ UTR of lrp. sRNAs control adaptation of N. meningitidis to variation in nutrient supply in different niches of its host.

2017-03-22 | PXD000891 | 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