Uptake of sialic acid by human erythrocyte. Characterization of a transport system

Bulai, Tatiana; Bratosin, Daniela; Artenie, Vlad; Montreuil, Jean

doi:10.1016/s0300-9084(03)00059-2

Cited by 13 publications

(7 citation statements)

References 19 publications

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“…Oetke et al [81], using human hematopoietic cell lines which are hyposialylated due to a deficiency in de novo sialic acid biosynthesis, demonstrated efficient uptake and incorporation of free sialic acid. Other studies reported that human thalassemic RBC have a lower content of sialic acid than normal RBC [82, 83], and that sialic acid can be taken up by human RBC [84, 85]. In our experiments, using several methodologies, Epo, at the concentrations tested in this study, did not demonstrate any ROS scavenging activity in a cell-free system (data not shown).…”

Section: Discussionsupporting

confidence: 42%

The Antioxidant Effect of Erythropoietin on Thalassemic Blood Cells

Amer

Dana

Fibach

2010

Anemia

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Because of its stimulating effect on RBC production, erythropoietin (Epo) is used to treat anemia, for example, in patients on dialysis or on chemotherapy. In β-thalassemia, where Epo levels are low relative to the degree of anemia, Epo treatment improves the anemia state. Since RBC and platelets of these patients are under oxidative stress, which may be involved in anemia and thromboembolic complications, we investigated Epo as an antioxidant. Using flow-cytometry technology, we found that in vitro treatment with Epo of blood cells from these patients increased their glutathione content and reduced their reactive oxygen species, membrane lipid peroxides, and external phosphatidylserine. This resulted in reduced susceptibility of RBC to undergo hemolysis and phagocytosis. Injection of Epo into heterozygous (Hbbth3/+) β-thalassemic mice reduced the oxidative markers within 3 hours. Our results suggest that, in addition to stimulating RBC and fetal hemoglobin production, Epo might alleviate symptoms of hemolytic anemias as an antioxidant.

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Section: Discussionsupporting

confidence: 42%

The Antioxidant Effect of Erythropoietin on Thalassemic Blood Cells

Amer

Dana

Fibach

2010

Anemia

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“…The presence of sialyltransferases in human serum may provide a possible way of changes in serum proteins with terminal α2-6 sialic acid [40]. Bulai et al have characterized a transport system and demonstrated the uptake of free sialic acids into human erythrocytes [41]. Therefore, free sialic acids could be transported across the membrane into RBC through a sialic acids transport system.…”

Section: Discussionmentioning

confidence: 99%

Glycosylation of Erythrocyte Spectrin and Its Modification in Visceral Leishmaniasis

et al. 2011

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Using a lectin, Achatinin-H, having preferential specificity for glycoproteins with terminal 9-O-acetyl sialic acid derivatives linked in α2-6 linkages to subterminal N-acetylgalactosamine, eight distinct disease-associated 9-O-acetylated sialoglycoproteins was purified from erythrocytes of visceral leishmaniaisis (VL) patients (RBCVL). Analyses of tryptic fragments by mass spectrometry led to the identification of two high-molecular weight 9-O-acetylated sialoglycoproteins as human erythrocytic α- and β-spectrin. Total spectrin purified from erythrocytes of VL patients (spectrinVL) was reactive with Achatinin-H. Interestingly, along with two high molecular weight bands corresponding to α- and β-spectrin another low molecular weight 60 kDa band was observed. Total spectrin was also purified from normal human erythrocytes (spectrinN) and insignificant binding with Achatinin-H was demonstrated. Additionally, this 60 kDa fragment was totally absent in spectrinN. Although the presence of both N- and O-glycosylations was found both in spectrinN and spectrinVL, enhanced sialylation was predominantly induced in spectrinVL. Sialic acids accounted for approximately 1.25 kDa mass of the 60 kDa polypeptide. The demonstration of a few identified sialylated tryptic fragments of α- and β-spectrinVL confirmed the presence of terminal sialic acids. Molecular modelling studies of spectrin suggest that a sugar moiety can fit into the potential glycosylation sites. Interestingly, highly sialylated spectrinVL showed decreased binding with spectrin-depleted inside-out membrane vesicles of normal erythrocytes compared to spectrinN suggesting functional abnormality. Taken together this is the first report of glycosylated eythrocytic spectrin in normal erythrocytes and its enhanced sialylation in RBCVL. The enhanced sialylation of this cytoskeleton protein is possibly related to the fragmentation of spectrinVL as evidenced by the presence of an additional 60 kDa fragment, absent in spectrinN which possibly affects the biology of RBCVL linked to both severe distortion of erythrocyte development and impairment of erythrocyte membrane integrity and may provide an explanation for their sensitivity to hemolysis and anemia in VL patients.

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“…One possibility is that lactate production increases substantially. Some studies have shown that RBCs can recycle the free SA cleaved by neuraminidase (12,13) through a cytosolic sialate pyruvate-lyase that specifically and reversibly catalyzes the cleavage of SA to form N-acetylmannosamine and pyruvate, and finally pyruvate can be transformed into lactate (29). In our study, incubation with high concentrations of SA (1 mg/mL) to stimulate the intracytoplasmic sialate pyruvate-lyase failed to increase RBC lactate concentrations, suggesting that this enzyme does not contribute directly to the increased RBC lactate concentrations.…”

Section: Discussionmentioning

confidence: 99%

“…SA may also participate in RBC metabolism. Indeed, some studies have shown that RBCs are able to recycle the free SA cleaved by neuraminidase (12,13). RBC SA content is decreased in senescent RBCs (14 -16) and even in nonsenescent RBCs in patients with diabetes mellitus (17,18).…”

mentioning

confidence: 99%