# name
Proteomics study of human cord blood reticulocyte-derived
                exosomes

# metadata.dc.description.abstract[].value
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.

# metadata.dc.source[].value
Articles publicats en revistes (ISGlobal)

# metadata.dc.title[].value
Proteomics study of human cord blood reticulocyte-derived
                exosomes