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Human MNC proteome - Proteome profiling of peripheral mononuclear cells from human blood

ABSTRACT: Proteome characterization of mononuclear cells extracted from human blood - Dataset 3

INSTRUMENT(S): LTQ-Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Mononuclear Cell, Blood

SUBMITTER: Daniel Martins-de-Souza

LAB HEAD: Daniel Martins-de-Souza

PROVIDER: PRD000732 | Pride | 2013-01-03

REPOSITORIES: Pride

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			Action	DRS
	PRIDE_Exp_Complete_Ac_26905.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_26905.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_26905.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_26906.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_26906.pride.mztab.gz	Mztab

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Publications

Proteome profiling of peripheral mononuclear cells from human blood.

Maccarrone Giuseppina G Rewerts Christiane C Lebar Maria M Turck Christoph W CW Martins-de-Souza Daniel D

Proteomics 20130124 5

Peripheral blood mononuclear cells (MNCs) are accessible through blood collection and represent a useful source for investigations on disease mechanisms and treatment response. Aiming to build a reference proteome database, we generated three proteome data sets from MNCs using a combination of SDS-PAGE and nanoflow LC-MS. Experiments were performed in triplicates and 514 unique proteins were identified by at least two non-redundant peptides with 95% confidence for all replicates. Identified prot ...[more]

PMID: 23281267

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Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells

Project description:Primary human peripheral blood mononuclear cells were isolated from full blood by standard ficoll centrifugation. Cells were washed and processed immediately.

2012-07-16 | PRD000731 | Pride

Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells.

Project description:Proteome profiling is the method of choice to identify marker proteins whose expression may be characteristic for certain diseases. The formation of such marker proteins results from disease-related pathophysiologic processes. In healthy individuals, peripheral blood mononuclear cells (PBMCs) circulate in a quiescent cell state monitoring potential immune-relevant events, but have the competence to respond quickly and efficiently in an inflammatory manner to any invasion of potential pathogens. Activation of these cells is most plausibly accompanied by characteristic proteome alterations. Therefore we investigated untreated and inflammatory activated primary human PBMCs by proteome profiling using a 'top down' 2D-PAGE approach in addition to a 'bottom up' LC-MS/MS-based shotgun approach. Furthermore, we purified primary human T-cells and monocytes and activated them separately. Comparative analysis allowed us to characterize a robust proteome signature including NAMPT and PAI2 which indicates the activation of PBMCs. The T-cell specific inflammation signature included IRF-4, GBP1 and the previously uncharacterized translation product of GBP5; the corresponding monocyte signature included PDCD5, IL1RN and IL1B. The involvement of inflammatory activated PBMCs in certain diseases as well as the responsiveness of these cells to anti-inflammatory drugs may be evaluated by quantification of these marker proteins. This article is part of a Special Issue entitled: Integrated omics.

| S-EPMC3509337 | biostudies-literature

Protocol for cell surface biotinylation of magnetic labeled and captured human peripheral blood mononuclear cells

Project description:Analysis of the surfaceome of a blood cell subset requires cell sorting, followed by surface protein enrichment. Here, we present a protocol combining magnetically activated cell sorting (MACS) and surface biotinylation of the target cell subset from human peripheral blood mononuclear cells (PBMCs). We describe the steps for isolating target cells and their in-column surface biotinylation, followed by isolation and mass spectrometry analysis of biotinylated proteins. The protocol enables in-column surface biotinylation of specific cell subsets with minimal membrane disruption.

2022-11-08 | PXD038027 | Pride

S-Nitrosylation Proteome Profile of Peripheral Blood Mononuclear Cells in Human Heart Failure.

Project description:Nitric oxide (NO) protects the heart against ischemic injury; however, NO- and superoxide-dependent S-nitrosylation (S-NO) of cysteines can affect function of target proteins and play a role in disease outcome. We employed 2D-GE with thiol-labeling FL-maleimide dye and MALDI-TOF MS/MS to capture the quantitative changes in abundance and S-NO proteome of HF patients (versus healthy controls, n = 30/group). We identified 93 differentially abundant (59-increased/34-decreased) and 111 S-NO-modified (63-increased/48-decreased) protein spots, respectively, in HF subjects (versus controls, fold-change | ≥1.5|, p ≤ 0.05). Ingenuity pathway analysis of proteome datasets suggested that the pathways involved in phagocytes' migration, free radical production, and cell death were activated and fatty acid metabolism was decreased in HF subjects. Multivariate adaptive regression splines modeling of datasets identified a panel of proteins that will provide >90% prediction success in classifying HF subjects. Proteomic profiling identified ATP-synthase, thrombospondin-1 (THBS1), and vinculin (VCL) as top differentially abundant and S-NO-modified proteins, and these proteins were verified by Western blotting and ELISA in different set of HF subjects. We conclude that differential abundance and S-NO modification of proteins serve as a mechanism in regulating cell viability and free radical production, and THBS1 and VCL evaluation will potentially be useful in the prediction of heart failure.

| S-EPMC5007369 | biostudies-literature

Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells

Project description:Human T-cells were isolated from full blood by ficoll centrifugation and subsequent negative depletion with magnetic beads of monocytes and B-cells and treated with 5ug/ml PHA for 24 hours.

2012-07-16 | PRD000668 | Pride

Profiling of the proteome of peripheral blood mononuclear cells of subjects diagnosed with primary open angle glaucoma

Project description:This study reports the first characterization of the intracellular proteome of peripheral blood mononuclear cells (PBMC) isolated from subjects diagnosed with primary open angle glaucoma (POAG)by shot-gun proteomics. Glaucoma is a chronic optic neuropathy and among the first causes of irreversible blindness on a global scale. Several recent data have pointed out alterations of immune system processes in glaucoma subjects. Very recently, oxygen consumption rate (OCR) and NAD levels have been proposed as biomarkers of disease severity.

2025-09-22 | PXD059976 | Pride

Microarray profiling peripheral blood mononuclear cells

Project description:Microarray profiling peripheral blood mononuclear cells

| PRJNA418401 | ENA

Immunophenotyping peripheral blood mononuclear cells in human HFpEF

Project description:Immunophenotyping peripheral blood mononuclear cells in human HFpEF

| PRJNA926645 | ENA

The Impact of Blood-Processing Time on the Proteome of Human Peripheral Blood Mononuclear Cells

Project description:Human peripheral blood mononuclear cells (PBMC) are key to several diagnostics assays and basic science research. Blood pre-analytical variations that occur before obtaining the PBMC fraction can have a significant impact on the results of the assays, including viability, composition, integrity, and gene expression changes of immune cells. With this as motivation, we performed a quantitative shotgun proteomics analysis using Isobaric Tag for Relative and Absolute Quantitation (iTRAQ 8plex) labeling to compare PBMC obtained from fresh versus 24h-stored blood at room temperature. We identified 3,195 proteins, of which 245 were differentially abundant. Our results revealed enriched pathways in the fresh-PBMC samples related to exocytosis, localization, vesicle-mediated transport, cell activation, and secretion. In contrast, pathways related to exocytosis, neutrophil degranulation and activation, granulocyte activation, leukocyte degranulation, and myeloid leukocyte activation involved in immune response were enriched in the 24h-PBMC samples, which may indicate probable granulocyte contamination and activation due to blood storage time and temperature. Examples of upregulated proteins in the 24h-PBMC sample are: CAMP, S100A8, LTA4H, RASAL3, and S100A6, which are involved in an adaptive immune system and antimicrobial activity, proinflammatory mediation, aminopeptidase activities, and naïve T cells survival. Moreover, examples of downregulated proteins are: NDUFA5, TAGLN2, H3C1, TUBA8, and CCT2 that are related to the cytoskeleton, cell junction, mitochondrial respiratory chain. In conclusion, blood-processing time directly impacts the proteomic profile of human PBMC.

2020-12-14 | PXD021367 | Pride

Peripheral blood mononuclear cell proteome changes in patients with myelodysplastic syndrome.

Project description:Our aim was to search for proteome changes in peripheral blood mononuclear cells (PBMCs) of MDS patients with refractory cytopenia with multilineage dysplasia. PBMCs were isolated from a total of 12 blood samples using a Histopaque-1077 solution. The proteins were fractioned, separated by 2D SDS-PAGE (pI 4-7), and double-stained. The proteomes were compared and statistically processed with Progenesis SameSpots; then proteins were identified by nano-LC-MS/MS. Protein functional association and expression profiles were analyzed using the EnrichNet application and Progenesis SameSpots hierarchical clustering software, respectively. By comparing the cytosolic, membrane, and nuclear fractions of the two groups, 178 significantly (P < 0.05, ANOVA) differing spots were found, corresponding to 139 unique proteins. Data mining of the Reactome and KEGG databases using EnrichNet highlighted the possible involvement of the identified protein alterations in apoptosis, proteasome protein degradation, heat shock protein action, and signal transduction. Western blot analysis revealed underexpression of vinculin and advanced fragmentation of fermitin-3 in MDS patients. To the best of our knowledge, this is the first time that proteome changes have been identified in the mononuclear cells of MDS patients. Vinculin and fermitin-3, the proteins involved in cell adhesion and integrin signaling, have been shown to be dysregulated in MDS.

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