Proteomics study of human cord blood reticulocyte-derived exosomes

Abstract Reticulocyte-derived exosomes (Rex), extracellular vesicles of endocytic origin, were initially discovered as a cargo-disposal mechanism of obsolete proteins in the maturation of reticulocytes into erythrocytes. In this work, we present the first mass spectrometry-based proteomics of human...

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Autores principales:	Míriam Díaz-Varela, Armando de Menezes-Neto, Daniel Perez-Zsolt, Ana Gámez-Valero, Joan Seguí-Barber, Nuria Izquierdo-Useros, Javier Martinez-Picado, Carmen Fernández-Becerra, Hernando A. del Portillo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Human Reticulocyte-derived Extracellular Vesicles Over-represention GO Analysis Transferrin Receptor Exosome Biogenesis Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6e212bd6253c48669cdaf24f5c9de782
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spelling	oai:doaj.org-article:6e212bd6253c48669cdaf24f5c9de7822021-12-02T15:08:38ZProteomics study of human cord blood reticulocyte-derived exosomes10.1038/s41598-018-32386-22045-2322https://doaj.org/article/6e212bd6253c48669cdaf24f5c9de7822018-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-32386-2https://doaj.org/toc/2045-2322Abstract Reticulocyte-derived exosomes (Rex), extracellular vesicles of endocytic origin, were initially discovered as a cargo-disposal mechanism of obsolete proteins in the maturation of reticulocytes into erythrocytes. In this work, we present the first mass spectrometry-based proteomics of human Rex (HuRex). HuRex were isolated from cultures of human reticulocyte-enriched cord blood using different culture conditions and exosome isolation methods. The newly described proteome consists of 367 proteins, most of them related to exosomes as revealed by gene ontology over-representation analysis and include multiple transporters as well as proteins involved in exosome biogenesis and erythrocytic disorders. Immunoelectron microscopy validated the presence of the transferrin receptor. Moreover, functional assays demonstrated active capture of HuRex by mature dendritic cells. As only seven proteins have been previously associated with HuRex, this resource will facilitate studies on the role of human reticulocyte-derived exosomes in normal and pathological conditions affecting erythropoiesis.Míriam Díaz-VarelaArmando de Menezes-NetoDaniel Perez-ZsoltAna Gámez-ValeroJoan Seguí-BarberNuria Izquierdo-UserosJavier Martinez-PicadoCarmen Fernández-BecerraHernando A. del PortilloNature PortfolioarticleHuman Reticulocyte-derivedExtracellular VesiclesOver-represention GO AnalysisTransferrin ReceptorExosome BiogenesisMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Human Reticulocyte-derived Extracellular Vesicles Over-represention GO Analysis Transferrin Receptor Exosome Biogenesis Medicine R Science Q
spellingShingle	Human Reticulocyte-derived Extracellular Vesicles Over-represention GO Analysis Transferrin Receptor Exosome Biogenesis Medicine R Science Q Míriam Díaz-Varela Armando de Menezes-Neto Daniel Perez-Zsolt Ana Gámez-Valero Joan Seguí-Barber Nuria Izquierdo-Useros Javier Martinez-Picado Carmen Fernández-Becerra Hernando A. del Portillo Proteomics study of human cord blood reticulocyte-derived exosomes
description	Abstract Reticulocyte-derived exosomes (Rex), extracellular vesicles of endocytic origin, were initially discovered as a cargo-disposal mechanism of obsolete proteins in the maturation of reticulocytes into erythrocytes. In this work, we present the first mass spectrometry-based proteomics of human Rex (HuRex). HuRex were isolated from cultures of human reticulocyte-enriched cord blood using different culture conditions and exosome isolation methods. The newly described proteome consists of 367 proteins, most of them related to exosomes as revealed by gene ontology over-representation analysis and include multiple transporters as well as proteins involved in exosome biogenesis and erythrocytic disorders. Immunoelectron microscopy validated the presence of the transferrin receptor. Moreover, functional assays demonstrated active capture of HuRex by mature dendritic cells. As only seven proteins have been previously associated with HuRex, this resource will facilitate studies on the role of human reticulocyte-derived exosomes in normal and pathological conditions affecting erythropoiesis.
format	article
author	Míriam Díaz-Varela Armando de Menezes-Neto Daniel Perez-Zsolt Ana Gámez-Valero Joan Seguí-Barber Nuria Izquierdo-Useros Javier Martinez-Picado Carmen Fernández-Becerra Hernando A. del Portillo
author_facet	Míriam Díaz-Varela Armando de Menezes-Neto Daniel Perez-Zsolt Ana Gámez-Valero Joan Seguí-Barber Nuria Izquierdo-Useros Javier Martinez-Picado Carmen Fernández-Becerra Hernando A. del Portillo
author_sort	Míriam Díaz-Varela
title	Proteomics study of human cord blood reticulocyte-derived exosomes
title_short	Proteomics study of human cord blood reticulocyte-derived exosomes
title_full	Proteomics study of human cord blood reticulocyte-derived exosomes
title_fullStr	Proteomics study of human cord blood reticulocyte-derived exosomes
title_full_unstemmed	Proteomics study of human cord blood reticulocyte-derived exosomes
title_sort	proteomics study of human cord blood reticulocyte-derived exosomes
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/6e212bd6253c48669cdaf24f5c9de782
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Proteomics study of human cord blood reticulocyte-derived exosomes

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