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2 results on '"Emilie-fleur Gautier"'

1. Comprehensive Proteomic Analysis of Human Erythropoiesis

Author

Emilie-Fleur Gautier, Sarah Ducamp, Marjorie Leduc, Virginie Salnot, François Guillonneau, Michael Dussiot, John Hale, Marie-Catherine Giarratana, Anna Raimbault, Luc Douay, Catherine Lacombe, Narla Mohandas, Frédérique Verdier, Yael Zermati, and Patrick Mayeux

Subjects
Biology (General), QH301-705.5
Abstract

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 proteins with unexpected expression patterns in erythroid cells, highlighting a breakpoint in the erythroid differentiation process at the basophilic stage. We also quantified the distribution of proteins between reticulocytes and pyrenocytes after enucleation. These analyses identified proteins that are actively sorted either with the reticulocyte or the pyrenocyte. Our study provides the absolute quantification of protein expression during a complex cellular differentiation process in humans, and it establishes a framework for future studies of disordered erythropoiesis.

Published
2016
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2. Comprehensive Proteomic Analysis of Human Erythropoiesis

Author

Patrick Mayeux, Narla Mohandas, Anna Raimbault, Michael Dussiot, Virginie Salnot, John Hale, Yael Zermati, Sarah Ducamp, Marie-Catherine Giarratana, Luc Douay, François Guillonneau, Marjorie Leduc, Frédérique Verdier, Emilie-Fleur Gautier, Catherine Lacombe, Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme protéomique 3P5 [Institut Cochin] (3P5), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Red Cell Physiology Laboratory [New York, USA], New York Blood Center, Centre de Recherche Saint-Antoine (UMRS893), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Ligue Nationale Contre le Cancer - Paris, Ligue Nationnale Contre le Cancer, ANR-11-IDEX-0005,USPC,Université Sorbonne Paris Cité(2011), Institut Cochin ( UM3 (UMR 8104 / U1016) ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratory of Excellence GR-Ex, Sorbonne Paris Cité-Université Paris Descartes - Paris 5 ( UPD5 ) -Imagine Institute, Plateforme protéomique 3P5 [Institut Cochin] ( 3P5 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), New York Blood Center - NYBC, Centre de Recherche Saint-Antoine ( CR Saint-Antoine ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), ANR-11-IDEX-0005-02/11-LABX-0051,GR-Ex,Biogenèse et pathologies du globule rouge ( 2011 ), ANR-11-IDEX-0005-02/11-IDEX-0005,USPC,USPC ( 2011 ), Bos, Mireille, Université Sorbonne Paris Cité - - USPC2011 - ANR-11-IDEX-0005 - IDEX - VALID, and Ligue Nationale Contre le Cancer (LNCC)

Subjects
Proteomics, 0301 basic medicine, Cell type, Erythroblasts, Proteome, Cellular differentiation, Biology, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Reticulocyte, hemic and lymphatic diseases, medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, Erythropoiesis, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, lcsh:QH301-705.5, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Cells, Cultured, Erythroid Precursor Cells, Messenger RNA, RNA, Cell Differentiation, Molecular biology, Cell biology, 030104 developmental biology, medicine.anatomical_structure, lcsh:Biology (General)
Abstract

SUMMARY 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 proteins with unexpected expression patterns in erythroid cells, highlighting a breakpoint in the erythroid differentiation process at the basophilic stage. We also quantified the distribution of proteins between reticulocytes and pyrenocytes after enucleation. These analyses identified proteins that are actively sorted either with the reticulocyte or the pyrenocyte. Our study provides the absolute quantification of protein expression during a complex cellular differentiation process in humans, and it establishes a framework for future studies of disordered erythropoiesis., In Brief Gautier et al. use quantitative mass spectrometry to determine the absolute proteome composition of human erythroid progenitors throughout the differentiation process and the quantitative distribution of proteins between reticulocytes and pyrenocytes after enucleation.

Published
2016
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