Browse
Submit Data
Databases
API
Help

Dataset Information

530 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Comprehensive proteomic analysis of human erythropoiesis - experiment 2

ABSTRACT: We performed a proteomic analysis of human erythropoiesis using 4 umbilical cord's blood samples. This study revealed the absolute and quantitative expression of more than 6000 proteins throughout 7 stages of erythroid differentiation using a label-free technique. We found new informations on erythropoiesis such as unexpected protein expression depicted the article.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Umbilical Cord Blood Cell, Erythroblast

SUBMITTER: François GUILLONNEAU

LAB HEAD: Patrick Mayeux

PROVIDER: PXD004314 | Pride | 2016-08-08

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	MaxQuantOutputExperiment2.tar.gz	Other
	PaMA150423_J1-1_O4197.raw	Raw
	PaMA150423_J1-2_O4198.raw	Raw
	PaMA150423_J1-3_O4199.raw	Raw
	PaMA150423_J1-4_O4200.raw	Raw

Items per page:

1 - 5 of 51

Publications

Comprehensive Proteomic Analysis of Human Erythropoiesis.

Gautier Emilie-Fleur EF Ducamp Sarah S Leduc Marjorie M Salnot Virginie V Guillonneau François F Dussiot Michael M Hale John J Giarratana Marie-Catherine MC Raimbault Anna A Douay Luc L Lacombe Catherine C Mohandas Narla N Verdier Frédérique F Zermati Yael Y Mayeux Patrick P

Cell reports 20160721 5

Mass spectrometry-based proteomics now enables the absolute quantification of thousands of proteins in individual cell types. We used this technology to analyze the dynamic proteome changes occurring during human erythropoiesis. We quantified the absolute expression of 6,130 proteins during erythroid differentiation from late burst-forming units-erythroid (BFU-Es) to orthochromatic erythroblasts. A modest correlation between mRNA and protein expression was observed. We identified several protein ...[more]

PMID: 27452463

Similar Datasets

Comprehensive proteomic analysis of human erythropoiesis - experiment 4 over 4

Project description:We performed a proteomic analysis of human erythropoiesis using 4 umbilical cord's blood samples. This study revealed the absolute and quantitative expression of more than 6000 proteins throughout 7 stages of erythroid differentiation using a label-free technique. We found new informations on erythropoiesis such as unexpected protein expression depicted the article.

2016-08-08 | PXD004316 | Pride

Comprehensive proteomic analysis of human erythropoiesis - experiment 3 over 4

2016-08-08 | PXD004315 | Pride

Comprehensive proteomic analysis of human erythropoiesis - experiment1

2016-08-08 | PXD004313 | Pride

DNA Replication Stress Due to Loss of R-Loops in Myelodysplastic Syndromes with SF3B1 Mutation

Project description:Myelodysplastic syndromes (MDS) with mutated SF3B1 gene have many features including a favorable outcome that are distinct from MDS with mutations in other splicing factor genes SRSF2 or U2AF1. Molecular bases of these divergences are poorly understood. Here we show that SF3B1-mutated MDS are characterized by a dramatically reduced R-loop formation predominating in gene bodies, which tightly associates with reduced retention of introns specifically found in SF3B1-mutated, but not in U2AF1- or SRSF2-mutated MDS. Compared to erythroblasts from SRSF2- or U2AF1-mutated patients, SF3B1-mutated erythroblasts exhibited augmented DNA synthesis, accelerated replication forks, and single-stranded DNA exposure upon differentiation, which were recapitulated in murine Sf3b1K700E/+ proerythroblasts. Importantly, R-loop formation was restored by histone deacetylase inhibition using SAHA/vorinostat, which improved Sf3b1K700E/+ erythroblast differentiation. In conclusion, loss of R-loops with associated DNA replication stress is a hallmark of SF3B1- mutated MDS ineffective erythropoiesis, which could be used as a new therapeutic target.

2024-04-08 | PXD038700 | Pride

DNA Replication Stress Due to Loss of R-Loops in Myelodysplastic Syndromes with SF3B1 Mutation

2024-05-29 | PXD038656 | Pride

LKB1 is a suppressor of amino acid-driven gluconeogenesis in the liver

Project description:Excessive hepatic glucose production is a major contributor to the hyperglycemia observed in Type 2 diabetes mellitus. It is widely accepted that it is due to an increase in hepatic gluconeogenesis. While much attention has been devoted to the transcriptional regulation of key gluconeogenic enzymes, much less is known about the regulation of amino acid catabolism that provides gluconeogenic substrates. Here, we emphasize a novel role of LKB1 in this regulation. We show that mice with a hepatocyte-specific deletion of Lkb1 have increased hepatic amino acid catabolism for gluconeogenesis. This occurred during fasting, as well as during the postprandial period, identifying Lkb1 as a critical suppressor of hepatic postprandial gluconeogenesis. Hepatic Lkb1 deletion was also associated with severe alterations in whole body metabolism leading to decreased lean body mass deposition on MRI analysis and, at a longer term, cachexia and sarcopenia as a consequence of the diversion of amino acids for liver metabolism at the expense of muscle. Using genetic and pharmacological approaches, we identified the aminotransferases and Agxt and as critical effectors of the suppressor function of Lkb1 in amino acid-driven gluconeogenesis.

2020-12-01 | PXD013478 | Pride

Project description:Proteome of purified erythrocytes from blood samples from patients diagnosed with a PIEZO1-HX based on familial history, non-spherocytic chronic hemolysis, typical osmotic gradient ektacytometry and molecular testing and from healthy donors were analyzed by a label free quantification approach.

2023-03-11 | PXD031963 | Pride

Deep proteomic analysis of murine erythroid differentiation

Project description:Erythropoiesis is a tightly controlled process. Although human and murine erythropoiesis are grossly similar, several aspects of these processes present significant differences. We have performed a label free quantification of proteins expressed during murine erythroid differentiation of primary cells with the aim to compare human and murine differentiations. Furthermore, we also analyzed the proteome of three murine cell lines, MEDEP, G1ER and Friend cells, to determine their similarities with the proteome of primary cells.

2020-05-26 | PXD009384 | Pride

Proteomic analysis of reticulocytes treated with the PIEZO-1 activator YODA

Project description:We performed a label free proteomic analysis on reticulocytes produced in vitro from CD34+ of healthy donors cells either exposed to DMSO as a control or to the PIEZO1 activator YODA1 at 1µM.

2023-03-11 | PXD035122 | Pride

The proteome of neutrophils in sickle cell disease

Project description:Polymorphonuclear neutrophils are key actors in the pathophysiology of sickle cell disease, but specific factors underlying their activation and sustained inflammation are not well documented. In the present study, we investigated the proteome of neutrophils by a label-free global comparative approach between 4 non-treated sickle patients (SS genotype) at steady state and 4 healthy donors. We identified 101 proteins differentially expressed in SS and normal neutrophils. We found overexpression of CD64 and under-expression of CD62L suggestive of an activated and aged neutrophil profile in SS patients. Comparison of the two proteomes revealed a strong involvement of the type 1 interferon (IFN) response pathway with a 3- to 84-fold increase of type 1 IFN-induced proteins in SS neutrophils, and overexpression of STAT1 and STAT2. Thus, we next determined the plasmatic concentration of type 1 IFNs (IFNα and IFNβ) using the digital-ELISA technology and found a significant higher concentration of IFNα in the plasma from half of our SS patients compared to controls. Overall, a dramatic high-level expression of IFNα signaling proteins in neutrophils from SS patients suggests auto-inflammatory-like phenotype in sickle cell disease at steady state. This finding could open the way to new anti-inflammatory therapies.

2020-11-11 | PXD014457 | Pride