Abstract
Human red blood cells (RBC), which are the cells most commonly used in the study of biological membranes, have some glycoproteins in their cell membrane. These membrane proteins are band 3 and glycophorins A–D, and some substoichiometric glycoproteins (e.g., CD44, CD47, Lu, Kell, Duffy). The oligosaccharide that band 3 contains has one N-linked oligosaccharide, and glycophorins possess mostly O-linked oligosaccharides. The end of the O-linked oligosaccharide is linked to sialic acid. In humans, this sialic acid is N-acetylneuraminic acid (NeuAc). Another sialic acid, N-glycolylneuraminic acid (NeuGc) is present in red blood cells of non-human origin. While the biological function of band 3 is well known as an anion exchanger, it has been suggested that the oligosaccharide of band 3 does not affect the anion transport function. Although band 3 has been studied in detail, the physiological functions of glycophorins remain unclear. This review mainly describes the sialo-oligosaccharide structures of band 3 and glycophorins, followed by a discussion of the physiological functions that have been reported in the literature to date. Moreover, other glycoproteins in red blood cell membranes of non-human origin are described, and the physiological function of glycophorin in carp red blood cell membranes is discussed with respect to its bacteriostatic activity.
Highlights
The blood of mammals, such as humans, as well as of birds, reptiles, and teleosts, contains red blood cells
Fairbanks et al [1] developed a method in which red blood cell membranes were solubilized by sodium dodecyl sulfate (SDS), and the extracted membrane proteins were separated by acrylamide gel electrophoresis (SDS-PAGE)
The research on glycosylation of red blood cells (RBC) membrane proteins has not been fully investigated when compared to the research on the protein moiety of RBC glycoproteins
Summary
The blood of mammals, such as humans, as well as of birds, reptiles, and teleosts, contains red blood cells (erythrocytes). Studies on biological membranes normally use human red blood cells (RBC) because these erythrocytes have no nuclei and are easy to obtain for cell membrane preparation. Fairbanks et al [1] developed a method in which red blood cell membranes were solubilized by sodium dodecyl sulfate (SDS), and the extracted membrane proteins were separated by acrylamide gel electrophoresis (SDS-PAGE). Figure sulfate (SDS)-polyacrylamide gelgel electrophoresis of human red blood cell
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