The Contribution of Sialic Acid to the Surface Charge of the Erythrocyte

Eylar, E.H.; Madoff, Morton A.; Brody, O.V.; Oncley, J. L.

doi:10.1016/s0021-9258(19)73972-6

Cited by 641 publications

(62 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This can be attributed to a larger contact area since Ea decreased in parallel [43]. Concerning hydrophilicity as another cause for speciesspecificity, we found congruence between the measured detachment work at RT and the reported sialic acid concentration of the tested species [24,25,28,29,32]. Both parameters show the same ranking: horse/human fetus/camel > human adult > chicken (due to the different methods used in the reports, the sialic acid concentration from horse, human fetus, and camel RBC cannot be further discriminated).…”

Section: Discussionsupporting

confidence: 66%

“…Moreover, we attempted to assess the feasibility of SCFS under largely physiological conditions by suspending RBCs in autologous plasma. 28.5 ± 6.6 [19] 0.618 (0.612/0.623) [19] --none Human fetus 11% wider diameter than adult [20] 4.84 ± 0.89 [21] higher rigidity index [21], lower shear elastic modulus [22] comparable [23] increased [24,25] none, 21% bigger cell volume [20] Horse biconcave diameter 5.7 µm 55.9 ± 13.4 [19] 0.679 (0.590/0.878) [19] deficient in band 4.2 and band 6 [26,27] increased [28,29] none Camel elliptic dimension 7 × 4 µm [30] none [31] n.a.…”

Section: Introductionmentioning

confidence: 99%

“…higher amount of band 3, less mobile [32,33] increased [32] none Chicken elliptic dimension 12.1 × 7.3 µm nucleus: 4.2 × 2.8 µm [30] none n.a. less band 3 copies, no adherence to GAPDH [34][35][36] lower [29] nucleus, mitochondria, marginal band, filaments [37,38] In this study, several knowledge gaps are being addressed. Firstly, one aim was to investigate the biomechanical characteristics of certain animal RBCs used as representative models for distinct phenotypical features within one comparative approach.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Red Blood Cell Stiffness and Adhesion Are Species-Specific Properties Strongly Affected by Temperature and Medium Changes in Single Cell Force Spectroscopy

et al. 2021

View full text Add to dashboard Cite

Besides human red blood cells (RBC), a standard model used in AFM-single cell force spectroscopy (SCFS), little is known about apparent Young’s modulus (Ea) or adhesion of animal RBCs displaying distinct cellular features. To close this knowledge gap, we probed chicken, horse, camel, and human fetal RBCs and compared data with human adults serving as a repository for future studies. Additionally, we assessed how measurements are affected under physiological conditions (species-specific temperature in autologous plasma vs. 25 °C in aqueous NaCl solution). In all RBC types, Ea decreased with increasing temperature irrespective of the suspension medium. In mammalian RBCs, adhesion increased with elevated temperatures and scaled with reported membrane sialic acid concentrations. In chicken only adhesion decreased with higher temperature, which we attribute to the lower AE-1 concentration allowing more membrane undulations. Ea decreased further in plasma at every test temperature, and adhesion was completely abolished, pointing to functional cell enlargement by adsorption of plasma components. This halo elevated RBC size by several hundreds of nanometers, blunted the thermal input, and will affect the coupling of RBCs with the flowing plasma. The study evidences the presence of a RBC surface layer and discusses the tremendous effects when RBCs are probed at physiological conditions.

show abstract

Section: Discussionsupporting

confidence: 66%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Red Blood Cell Stiffness and Adhesion Are Species-Specific Properties Strongly Affected by Temperature and Medium Changes in Single Cell Force Spectroscopy

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Sialic acid residues are responsible for the negative charge at the cell surface in human erythrocytes (Eylar et al, 1962), and are involved in Mand N-group specificity (Ebert & Jurgen, 1972). The sialic acid content decreases as erythrocytes age (Balduini et al, 1974;Baxter & Beeley, 1975), and its role as a determinant of the erythrocyte lifespan is described in several reports (Jancik & Schauer, 1974;Durocher et al, 1975;Gattegno et al, 1975).…”

mentioning

confidence: 99%

Self-digestion of human erythrocyte membranes. Role of adenosine triphosphate and glutathione

Brovelli¹,

Suhail²,

Pallavicini³

et al. 1977

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Carboxyl groups of sialic acid determine the negative charge of human red blood cells by more than 80% [24]. The integral protein glycophorin A represents 75% of all sialoglycoproteins in the membrane of RBCs [25].…”

Section: Discussionmentioning

confidence: 99%

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

2021

Preprint

View full text Add to dashboard Cite

We study the influence of trypsin on aggregation, disaggregation, and aggregate morphology of RBCs in autologous plasma and serum. The effect of trypsin on the surface charge of red blood cells and the aggregation of glutaraldehyde fixed cells after treatment with the enzyme was also studied. RBC aggregation was studied by means of an aggregometer and microscopic observations. The results obtained in this study indicate that trypsin treatment increases RBCs aggregation in autologous plasma and serum. The disaggregation of erythrocytes after trypsin treatment considerably decreased in autologous plasma and serum. Increase in the strength of red blood cell aggregates was observed in autologous plasma and serum. The microscopic images of RBCs aggregates indicate the formation of globular (pathologic) structures of aggregates in autologous plasma and serum. Trypsin decrease the surface charge of RBCs. In autologous plasma and serum, the cup shapes of RBCs appear. The control RBCs fixed with glutaraldehyde were not aggregated after their placement in autologous plasma. At the same time, red blood cells pretreated with trypsin and fixed with glutaraldehyde interact with each other in autologous plasma. The physiological significance of glycoproteins of erythrocyte surface for RBCs aggregation was discussed.

show abstract

The Contribution of Sialic Acid to the Surface Charge of the Erythrocyte

Cited by 641 publications

References 32 publications

Red Blood Cell Stiffness and Adhesion Are Species-Specific Properties Strongly Affected by Temperature and Medium Changes in Single Cell Force Spectroscopy

Red Blood Cell Stiffness and Adhesion Are Species-Specific Properties Strongly Affected by Temperature and Medium Changes in Single Cell Force Spectroscopy

Self-digestion of human erythrocyte membranes. Role of adenosine triphosphate and glutathione

Effects of trypsin on aggregation, disaggregation and aggregate morphology of red blood cells in autologous plasma and serum

Contact Info

Product

Resources

About