Browse
Submit Data
Databases
API
Help

Dataset Information

2 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mm_splenocyte_Alzheimer

ABSTRACT: Mouse splenocyte proteome

REANALYSIS of: PXD000203

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus

SUBMITTER:

PROVIDER: PAe005206 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

ACCESS DATA

Json Xml

Publications

Proteome characterization of splenocytes from an Aβpp/ps-1 Alzheimer's disease model.

Cao Zhiyun Z Robinson Renã A S RA

Proteomics 20140106 2-3

Alzheimer's disease (AD) is the sixth leading cause of US deaths. In addition to neurodegenerative deficits in AD, changes in the immune system have also been observed. Proteomic analysis of specific immune cell populations may help gain insights into mechanisms of peripheral immunity in AD. Herein, we report proteome characterization for two subsets of splenocytes (i.e. CD90+ cells and a heterogeneous pool of CD90- cells) from a double transgenic mutant amyloid precursor protein/presenilin-1 (A ...[more]

PMID: 24293237

Similar Datasets

Profiling proteome-scale antibody responses to M. tuberculosis

Project description:This SuperSeries is composed of the following subset Series: GSE30721: Profiling proteome-scale antibody responses to M. tuberculosis proteins in sera of macaques infected with M. tuberculosis GSE30722: Profiling proteome-scale antibody responses to M. tuberculosis proteins in TB suspect's sera Refer to individual Series

2012-07-05 | E-GEOD-31368 | biostudies-arrayexpress

Dynamic profiling of the protein life cycle in response to pathogens (protein)

2015-03-06 | GSE59792 | GEO

Dynamic profiling of the protein life cycle in response to pathogens (protein)

Project description:Protein expression is regulated by production and degradation of mRNAs and proteins, but their specific relationships remain unknown. We combine measurements of protein production and degradation and mRNA dynamics to build a quantitative genomic model of the differential regulation of gene expression in LPS stimulated mouse dendritic cells. Changes in mRNA abundance play a dominant role in determining most dynamic fold changes in protein levels. Conversely, the preexisting proteome of proteins performing basic cellular functions is remodeled primarily through changes in protein production or degradation, accounting for over half of the absolute change in protein molecules in the cell. Thus, the proteome is regulated by transcriptional induction of novel cellular functions and remodeling of preexisting functions through the protein life cycle. Mouse primary dendritic cells were treated with LPS or mock stimulus and profiled over a 12-hour time course. Cells were grown in M-labeled SILAC media, which was replaced with H-labeled SILAC media at time 0. Aliquots were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, 9, and 12 hours post-stimulation and added to equal volumes of a master mix of unlabeled (L) cells for the purpose of normalization. RNA-Seq was performed at 0, 1, 2, 4, 6, 9, and 12 hours post-stimulation.

2015-03-06 | E-GEOD-59792 | biostudies-arrayexpress

Profiling proteome-scale antibody responses to M. tuberculosis proteins in sera of macaques infected with M. tuberculosis

Project description:Human infection with Mycobacterium tuberculosis results in a continuum of ill-defined, clinical manifestations with stable latent M. tuberculosis infection (LTBI) and severe active disease at the ends. Identifying different states of infection is of importance to tuberculosis (TB) control since risk of developing active disease varies among different asymptomatic states while infectiousness varies among patients with different bacterial burden. We investigated changes in proteome-scale antibody responses during disease progression in a non-human primate model of tuberculosis. We probed M. tuberculosis proteome microarrays with serial sera collected from three infection-outcome groups (active, reactivation, and latent). We found that each infection outcome is associated with characteristic changes in the antibody levels and number of antigenic targets, which suggested an association between antibody responses and bacillary burden. Additional proteome-scale serological profiling of > 400 human TB suspects established that antibody responses are positively associated with bacterial load. Thus tuberculosis-specific antibody levels and number of antigenic targets increases with disease progression. To investigate antibody responses during the course of infection, we probed M. tuberculosis proteome microarrays with serial sera collected from experimentally infected cynomolgus macaques. Based on infection outcome, the macaques were grouped into three classes; A) active disease (n = 4), B) latent infection (n=5) and C) reactivation disease (n = 5). Note that the macaques in the reactivation class developed signs of disease spontaneously without any experimental intervention. For each animal, we tested one pre-infection time point and approximately ten post-infection time points at one-month intervals.

2012-07-05 | E-GEOD-30721 | biostudies-arrayexpress

Profiling antibody responses to M. tuberculosis proteins in TB suspects’ sera using full-proteome microarrays.

Project description:Understanding the immune response to tuberculosis requires greater knowledge of humoral responses. To characterize antibody targets and the effect of disease parameters on target recognition, we developed a systems immunology approach that integrated detection of antibodies against the entire Mycobacterium tuberculosis proteome, bacterial metabolic and regulatory pathway information, and patient data. Probing ~4,000 M. tuberculosis proteins with sera from >500 suspected tuberculosis patients worldwide revealed that antibody responses recognized ~10% of the bacterial proteome. This result defines the immunoproteome of M. tuberculosis, which is rich in membrane-associated and extracellular proteins. Most serum reactivity during active tuberculosis focused onto ~0.5% of the proteome. Within this pool, which is selectively enriched for extracellular proteins (but not for membrane-associated proteins), relative target preference varied among patients. The shift in relative M. tuberculosis protein reactivity observed with active tuberculosis defines the evolution of the humoral immune response during M. tuberculosis infection and disease.

2010-07-14 | GSE19433 | GEO

E-PROT-76

Project description:The Comprehensive Mouse Retina Proteome

2022-01-14 | E-PROT-76 | ExpressionAtlas

Characterization of rubella-specific humoral immunity following two doses of MMR vaccine using proteome microarray technology

Project description:This study uses proteome microarray technology/data to identify predictive biomarkers of neutralizing antibody response and potential new correlates of protective immunity in rubella virus serology.

2017-09-23 | GSE104148 | GEO

Profiling proteome-scale antibody responses to M. tuberculosis proteins in TB suspect's sera

2012-07-06 | GSE30722 | GEO

Profiling proteome-scale antibody responses to M. tuberculosis proteins in sera of macaques infected with M. tuberculosis

2012-07-06 | GSE30721 | GEO

Cytokine interactome alterations promote oropharyngeal Epstien-barr virus (EBV) replication and shedding during HIV infection

Project description:Proteomic analysis of cytokines in unstimulated oropharyngeal secretions. Epstein-barr virus (EBV) is a type 1 carcinogen which causes many cancers in humans. Here we explored the cytokine involvement of the EBV replication process in the oropharynx. Cytokine interactomic profiles were geneerated to understand the involved signalling pathways in HIV infected group and the healthy group. Proteome profilers were used to understand the major cytokine expression levels that are related to infection and immune regulation. We analyzed unstimulated oropharyngeal samples (UOPS) from 42 healthy subjects and 72 HIV positive subjects using the R & D Proteome Profiler array panels. No techinical replicates were performed. 14 samples in HIV group without therapy (NHAART group); 58 HIV patients with highly active antiretroviral therapy (HAART group); 42 samples in healthy group

2010-04-15 | E-GEOD-21339 | biostudies-arrayexpress

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