Dataset Information

Quantitative analysis of the erythrocyte kinome

ABSTRACT: The erythrocytes, the most numerous cells of the human body (Sender 2016), have the fundamental function of providing oxygen to the other cells throughout the organism. Protein phosphorylations are involved in the regulation of several important mechanisms in erythrocytes, such as cytoskeleton remodeling and membrane deformability allowing them to transit into the smallest capillaries. We performed a label free quantitative analysis aimed at specifically identify the set of kinases expressed in erythrocytes (the erythrocyte kinome).

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Erythrocyte, Blood

SUBMITTER: Emilie-Fleur GAUTIER

LAB HEAD: Patrick MAYEUX

PROVIDER: PXD009396 | Pride | 2018-09-18

REPOSITORIES: Pride

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Publications

Absolute proteome quantification of highly purified populations of circulating reticulocytes and mature erythrocytes.

Gautier Emilie-Fleur EF Leduc Marjorie M Cochet Sylvie S Bailly Karine K Lacombe Catherine C Mohandas Narla N Guillonneau François F El Nemer Wassim W Mayeux Patrick P

Blood advances 20181001 20

Reticulocytes produced in the bone marrow undergo maturation in the bloodstream to give rise to erythrocytes. Although the proteome of circulating red cells has been the subject of several reports, the cellular populations used for these studies were never completely devoid of reticulocytes. In our current study, we used highly purified erythrocyte and reticulocyte populations to quantify the absolute expression levels of the proteins in each cell population. Erythrocytes and reticulocytes were ...[more]

PMID: 30327373

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Project description:Diamond Blackfan Anemia (DBA) is a rare, congenital erythrocyte aplasia that is usually caused by haploinsufficiency of ribosomal proteins due to diverse mutations in one of several ribosomal protein genes. A striking feature of this disease is that a range of different mutations in ribosomal proteins results in similar disease phenotypes primarily characterized by erythrocyte abnormalities and macrocytic anemia, while most other cell types are minimally affected. Previously, we analyzed the erythrocyte membrane proteomes of several DBA patients and identified several proteins that are not typically associated with this cell type that suggested inflammatory mechanisms contribute to the pathogenesis of DBA. In this study, we evaluated the erythrocyte cytosolic proteome of DBA patients through in-depth analysis of hemoglobin-depleted erythrocyte cytosol. The simple, reproducible, hemoglobin depletion using nickel columns enabled in-depth analysis of over 1000 cytosolic erythrocyte proteins with minimal subsequent fractionation of the proteome. Label-free quantitation and statistical analysis identified 29 proteins that were significantly changed in DBA patients compared to matched healthy control donors. Some of the proteins that were significantly increased in DBA erythrocyte cytoplasm included three proteasome subunit beta proteins that make up the immunoproteasome and proteins induced by interferon-γ such as n-myc interactor and interferon-induced 25 kDa protein [NMI and IFI35 respectively]. Pathway analysis confirmed the presence of an inflammatory signature with erythrocytes of DBA patients and predicted key upstream regulators including mitogen activated kinase 1, interferon-γ, tumor suppressor p53, and tumor necrosis factor. These results show that erythrocytes in DBA patients are intrinsically different from those in healthy controls which may be due to an inflammatory response resulting from the inherent molecular defect of ribosomal protein haploinsufficiency or changes in the bone marrow microenvironment that leads to red cell aplasia in DBA patients.

Dataset Information

Quantitative analysis of the erythrocyte kinome

Publications

Absolute proteome quantification of highly purified populations of circulating reticulocytes and mature erythrocytes.

Similar Datasets

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