Comprehensive Proteomic Analysis of Human Erythropoiesis

作者：Emilie‐Fleur Gautier, Sarah Ducamp, Marjorie Leduc, Virginie Salnot, François Guillonneau, Michaël Dussiot, John Hale, Marie‐Catherine Giarratana, Anna Raimbault, Luc Douay, Catherine Lacombe, Narla Mohandas, Frédèrique Verdier, Yaël Zermati, Patrick Mayeux · 发表于：Cell Reports · 年份：2016 · DOI：10.1016/j.celrep.2016.06.085 · 被引用次数：256 · 研究领域：Erythrocyte Function and Pathophysiology、Blood properties and coagulation、Advanced Proteomics Techniques and Applications

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.