Extrusion of Na,K-ATPase and transferrin receptor with lipid raft-associated proteins in different populations of exosomes during reticulocyte maturation in dogs
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The present study characterizes canine reticulocyte exosomes. Exosomes are smallmembrane vesicles involved in membrane remodeling that are released from reticulocytesduring the final maturation step of red blood cells. The vesicles collected from reticulocyteculture supernatants by differential centrifugation contained major exosomal proteinsincluding heat shock protein cognate 70 (Hsc70) and transferrin receptors (TfR), consistentwith the definition of the exosome. In addition, the Na,K-ATPase α-subunit and stomatin, alipid raft-associated protein, were extruded by the exosome pathway, possibly leading tothe absence of these proteins in erythrocytes, while the major protein constituents oferythrocyte membranes, spectrin and band 3 were retained in reticulocytes and notexpelled into exosomes. The Na,K-ATPase α-subunit, as well as TfR and about half of thestomatin contained in exosomes, was obtained in a detergent-soluble fraction that wasdistinct from the lipid raft microdomain. Moreover, Na,K-ATPase and a portion of stomatinwere distributed differently to Hsc70, TfR, stomatin, and ganglioside Gm1 in vesiclesseparated with sucrose density gradient centrifugation. These results demonstrate that aheterogeneous group of exosomes participates in the loss of Na,K-ATPase and membraneremodeling during reticulocyte maturation in dogs.
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