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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/134517
Proteomics study of human cord blood reticulocyte-derived exosomes
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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.
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DÍAZ VARELA, Míriam, et al. Proteomics study of human cord blood reticulocyte-derived
exosomes. Scientific Reports. 2018. Vol. 8, num. 14046. ISSN 2045-2322. [consulted: 9 of June of 2026]. Available at: https://hdl.handle.net/2445/134517