Decay-accelerating factor (CD55) and membrane inhibitor of reactive lysis (CD59) are released within exosomes during In vitro maturation of reticulocytes

H Rabesandratana, JP Toutant… - Blood, The Journal of …, 1998 - ashpublications.org
H Rabesandratana, JP Toutant, H Reggio, M Vidal
Blood, The Journal of the American Society of Hematology, 1998ashpublications.org
Exosomes are membrane vesicles released by reticulocytes during their maturation into
erythrocytes. They have a clearing function because of their enrichment with some proteins
known to decrease or disappear from the cell surface during maturation, eg,
acetylcholinesterase (AChE) and transferrin receptor (TfR), respectively. To better
understand the molecular events leading to protein sorting in exosomes, we analyzed the
expression of glycosylphosphatidylinositol (GPI)-anchored proteins on the exosome surface …
Abstract
Exosomes are membrane vesicles released by reticulocytes during their maturation into erythrocytes. They have a clearing function because of their enrichment with some proteins known to decrease or disappear from the cell surface during maturation, eg, acetylcholinesterase (AChE) and transferrin receptor (TfR), respectively. To better understand the molecular events leading to protein sorting in exosomes, we analyzed the expression of glycosylphosphatidylinositol (GPI)-anchored proteins on the exosome surface through a technique involving bead coupling and flow cytometry immunodetection. The presence of AChE, decay-accelerating factor (DAF), membrane inhibitor of reactive lysis (MIRL), and lymphocyte function-associated antigen 3 (LFA-3) on the surface of exosomes obtained from normal and paroxysmal nocturnal hemoglobinuria (PNH) reticulocytes, suggests that (1) the GPI anchor is efficiently sorted during exosome formation, (2) exosome release could account for the observed discrepancy in GPI-protein expression between reticulocytes and erythrocytes from PNH patients, and (3) exosomes could have another physiologic function related to controlling membrane attack complex formation.
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