Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Polarized Endothelial Cell-Derived Extracellular Vesicles

ABSTRACT: Proteomics was performed on extracellular vesicles secreted bidirectionally (apical vs. basolateral surfaces) from in vitro cultures of activated and quiescent human endothelial cells.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human) Bos Taurus (bovine) Escherichia Coli Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Cell Culture, Endothelial Cell

SUBMITTER: Mark Blaser

LAB HEAD: Kathryn L Howe

PROVIDER: PXD038917 | Pride | 2024-01-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	26_MB_TranswellEC-EVs_3-CES-1_125ng.raw	Raw
	26_MB_TranswellEC-EVs_4-CES-2_125ng.raw	Raw
	26_MB_TranswellEC-EVs_5-CES-3_125ng.raw	Raw
	26_MB_TranswellEC-EVs_6-SES-1_125ng.raw	Raw
	26_MB_TranswellEC-EVs_7-SES-2_125ng.raw	Raw

Items per page:

1 - 5 of 53

Similar Datasets

Human Cardiovascular Tissue Extracellular Vesicles

Project description:Fewer than 50% of patients develop vascular and valvular calcification, implying differential pathogenesis. Tissue-entrapped extracellular vesicles (EVs) are found in mineralization but their contents and functions are unstudied. Tissue EVs were isolated from normal and diseased human carotid arteries and aortic valves by enzymatic digestion, serial (ultra)centrifugation and density-gradient separation.

2023-07-10 | PXD035529 | Pride

Human Cardiovascular Tissue Extracellular Vesicles – Density Gradient

Project description:Fewer than 50% of patients develop vascular and valvular calcification, implying differential pathogenesis. Tissue-entrapped extracellular vesicles (EVs) are found in mineralization but their contents and functions are unstudied. Tissue EVs were isolated from diseased human carotid arteries and aortic valves by enzymatic digestion, serial (ultra)centrifugation and density-gradient separation. Mass spectrometry characterized the density-gradient separation and quantified protein cargoes of tissue-derived cardiovascular EVs.

2023-07-10 | PXD035580 | Pride

Human Cardiovascular Tissue Extracellular Vesicles – Iodixanol Mass Exclusion

2023-07-10 | PXD035505 | Pride

Human Cardiovascular Tissue Extracellular Vesicles – Ultracentrifugation vs. Density Gradient

2023-07-10 | PXD035485 | Pride

Human Diseased Cardiovascular Tissue

Project description:Fewer than 50% of patients develop vascular and valvular calcification, implying differential pathogenesis. Disease stage-specific proteomics (non-diseased/fibrotic/calcified areas) was performed on human carotid endarterectomy specimens and stenotic aortic valves.

2023-07-10 | PXD035538 | Pride

Human Normal & Diseased Cardiovascular Tissue

Project description:Fewer than 50% of patients develop vascular and valvular calcification, implying differential pathogenesis. Disease stage-specific proteomics (normal/non-diseased/fibrotic/calcified areas) was performed on human carotid artery specimens from autopsy, carotid endarterectomy specimens, aortic valves from heart transplant recipients, and stenotic aortic valves.

2023-07-10 | PXD035555 | Pride

Human Diseased Cardiovascular Tissue – Fractionated

2023-07-10 | PXD035563 | Pride

Quiescent vs. Activated Endothelial Cell-Derived Extracellular Vesicles

Project description:Proteomics was performed on extracellular vesicles derived from in vitro cultures of activated and quiescent human endothelial cells.

2024-01-04 | PXD038914 | Pride

Valvular interstitial cells and mesenchymal stem cell proteomes

Project description:Proteome profiling of valvular disease driver cell populations and mesenchymal stem cells undergoing osteogenic differentiation.

2024-01-25 | PXD029949 | Pride

Simultaneous N-deglycosylation and digestion of human and chicken proteins on S-Traps

Project description:N-linked glycosylation is an important post-translational modification that is difficult to identify and quantify in traditional bottom-up proteomics experiments. Enzymatic deglycosylation of proteins by peptide:N-glycosidase F (PNGase F) prior to digestion and subsequent mass spectrometry analysis has been shown to improve coverage of various N-linked glycopeptides, but inclusion of this step may add up to a day to an already lengthy sample preparation process. An efficient way to integrate deglycosylation with bottom-up proteomics would be a valuable contribution to the glycoproteomics field. Here, we demonstrate a proteomics workflow in which deglycosylation and proteolytic digestion of samples occurs simultaneously using suspension trapping (S-Trap). This approach adds no additional time to standard digestion protocols. Applying this sample preparation strategy to a human serum sample, we demonstrate improved identification of potential N-glycosylated peptides in deglycosylated samples compared with non-deglycosylated samples, identifying 156 unique peptides that contain the N-glycosylation motif (Asparagine–X–Serine/Threonine), the deamidation modification characteristic of PNGase F, and an increase in peptide intensity over a control sample. We expect that this rapid sample preparation strategy will assist in the identification and quantification of both known and potential glycoproteins.

2023-02-09 | PXD037921 | 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