Abstract
Changes to the membrane proteins and rearrangement of the cytoskeleton must occur for a reticulocyte to mature into a red blood cell (RBC). Different mechanisms of reticulocyte maturation have been proposed to reduce the size and volume of the reticulocyte plasma membrane and to eliminate residual organelles. Lysosomal protein degradation, exosome release, autophagy and the extrusion of large autophagic–endocytic hybrid vesicles have been shown to contribute to reticulocyte maturation. These processes may occur simultaneously or perhaps sequentially. Reticulocyte maturation is incompletely understood and requires further investigation. RBCs with membrane defects or cation leak disorders caused by genetic variants offer an insight into reticulocyte maturation as they present characteristics of incomplete maturation. In this review, we compare the structure of the mature RBC membrane with that of the reticulocyte. We discuss the mechanisms of reticulocyte maturation with a focus on incomplete reticulocyte maturation in red cell variants.
Highlights
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In this review we have discussed the structure of the mature red blood cell (RBC) membrane and how it differs from the membrane of the reticulocyte
Lysosomal protein degradation is a standard process for the removal of unwanted or damaged proteins in nucleated cells and probably occurs even before enucleation of the erythroblast
Summary
The mature red blood cell (RBC) has a unique biconcave shape that provides flexibility and withstands shear stress during circulation through narrow blood capillaries. The gross structure of the red cell membrane is a lipid bilayer with attachments to the underlying cytoskeleton via tethering transmembrane protein complexes. This structure provides the membrane with a dynamic fluidity and elasticity to survive for 120 days during circulation [7]. The tail ends of the spectrin tetramers contain binding sites for actin, protein 4.1 and other associated cytoskeletal proteins of the junctional complex, the other main attachment site between the cytoskeleton and the membrane [32]. Aside from the junctional complex the ankyrin associations with band 3 and with spectrin are known to promote the self-association of spectrin tetramers, adding to the equilibrium between intact and dissociated tetramers in the resting membrane This association is strengthened by the presence of protein 4.2 [21]
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