The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein

Tanner, Michael; Anstee, David J.

doi:10.1042/bj1530271

Cited by 129 publications

(34 citation statements)

References 22 publications

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“…and IIIb may possibly be due to a cellular compensatory mechanism resulting from the absence or severe reduction in IIbAl and IIIaA1. A similar compensatory mechanism has been observed in En(a-) patients where glycophorin is absent from the erythrocyte membrane [21]. In addition lower molecular weight IVa, IVb and VII may not be detected in Glanzmann's thrombasthenia platelets due to their non-availability on the platelet surface as a result of changes in the position of other glycoproteins or may be due to an alteration in their sugar sequence.…”

Section: Discussionmentioning

confidence: 73%

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Glycoproteins of Platelet Membranes from Glanzmann's Thrombasthenia. A Comparison with Normal Using Carbohydrate-Specific or Protein-Specific Labelling Techniques and High-Resolution Two-Dimensional Gel Electrophoresis

McGregor

Clemetson

James³

et al. 1981

Eur J Biochem

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Platelets from Glanzmann's thrombasthenia patients and from normal donors were surface labelled by techniques specific for sugars (terminal sialic acid, penultimate galactose/N-acetylgalactosamine) and proteins (tyrosine-histidine residues). These labelled platelets were solubilized in sodium dodecyl sulphate and separated on a two-dimensional electrophoretic system [O'Farrell, P. H. (1975) J . Biol. Chem. 250,4007 -4021 ] first according to their isoelectric point (PI) and then according to their molecular weight. In addition, unlabelled sodiumdodecyl-sulphate-solubilized platelets were separated on a two-dimensional polyacrylamide gel and the glycoproteins were identified by binding of 12sI-labelled Lens culinaris lectin (specific for mannose and glucose). In one Glanzmann's thrombasthenia patient glycoproteins IIbAl and IIIaAl were absent and in two others lower amounts of two glycoproteins were found in positions similar or close to these two membrane glycoproteins. The terminal sialic acid moieties of major glycoproteins (IbAl, IbBl and IIIbAI) were more intensely labelled in Glanzmann's thrombasthenia than in normals and these glycoproteins had an altered PI. A glycoprotein tentatively designated as Ic/IIa(?) had an altered PI and was labelled more intensely in Glanzmann's thrombasthenia platelets than in normals. A number of low-molecular-weight glycoproteins (IVa, IVb, VII) and one highmolecular weight glycoprotein normally found in platelets of healthy donors were reproducibly not detected in Glanzmann's thrombasthenia platelets. These results obtained by a combination of highly sensitive techniques strongly indicate that in Glanzmann's throinbasthenia the absence or reduction of two major membrane glycoproteins (IIbA1, IIIaA1) is not the only defect but that there appears to be a profound perturbation of the platelet membrane surface.

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Section: Discussionmentioning

confidence: 73%

“…Increasing evidence shows that normal platelet survival time in circulation and haemostatic functions are closely dependent on thc presence of intact membrane proteins and glycoproteins [I, 21. An important contribution to the above findings has been the study of congenital platelet membrane abnormalities.…”

mentioning

confidence: 99%

Glycoproteins of Platelet Membranes from Glanzmann's Thrombasthenia. A Comparison with Normal Using Carbohydrate-Specific or Protein-Specific Labelling Techniques and High-Resolution Two-Dimensional Gel Electrophoresis

McGregor

Clemetson

James³

et al. 1981

Eur J Biochem

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“…2, ektacytometry of erythrocytes incubated with Fab (13-59 ,g/ml) revealed a dose-dependent decrease in deformability. To determine whether the monoclonal antibody was exerting its effect on deformability only through glycophorin A, we treated En(a-) erythrocytes, which lack glycophorin A (29)(30)(31)(32), with the antibody (30 ,ug/ml) and measured deformability. When the DI of these En(a-) cells was plotted as a function of shear stress, there was no increase in cell rigidity and the DI curve was not significantly different from that of normal cells (Fig.…”

Section: Resultsmentioning

confidence: 99%

Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins.

Chasis¹,

Mohandas²,

Shohet³

1985

J. Clin. Invest.

112

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Erythrocyte skeletal proteins are known to play an important role in determining membrane deformability. In order to see whether transmembrane proteins also influence deformability and, if so, whether this influence is mediated by an interaction with the membrane skeleton, we examined the effect on deformability of ligands specific for transmembrane proteins. We found membrane deformability markedly reduced in erythrocytes that were pretreated with glycophorin A-specific ligands. In contrast, ligands specific for band 3 and A and B blood group antigens had no effect. The increase in membrane rigidity appeared to depend upon a transmembrane event and not upon a rigidity-inducing lattice on the outside surface of the cell in that a monovalent Fab of antiglycophorin IgG caused decreased deformability. We therefore looked for a ligand-induced association of glycophorin and the skeletal proteins and found, in Triton X-100-insoluble residues, a partitioning of glycophorin with the skeletal proteins only after preincubation with a ligand specific for glycophorin. We then studied cells and resealed membranes with skeletal protein abnormalities. In spectrin-deficient and protein 4.1-deficient erythrocytes and in 2,3-diphosphoglycerate-treated resealed membranes, the antiglycophorin IgG was only one-third as effective in decreasing deformability as it was in normal cells. Thus, normal skeletal proteins appear to be essential for liganded glycophorin to affect membrane deformability maximally. Taken together, these observations indicate that there is a ligand-induced interaction between glycophorin A and skeletal proteins and that this interaction can directly influence membrane deformability.

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“…Of interest in this regard are the erythrocytes from En(a-) individuals. These erythrocytes have a total deficiency of glycophorin-a, yet there are no apparent clinical sequelae (27,60). The lack ofassociated symptomatology may be accounted for by a compensatory increase in glycosylation of other membrane glycoproteins (in particular band 3) (29).…”

Section: Discussionmentioning

confidence: 99%

Abnormality of glycophorin-alpha on paroxysmal nocturnal hemoglobinuria erythrocytes.

Parker¹,

Soldato²,

Rosse³

1984

J. Clin. Invest.

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Abstract. To investigate the greater enzymatic activity of the alternative pathway convertase (and the subsequent greater fixation of C3b) on paroxysmal nocturnal hemoglobinuria (PNH) erythrocytes, we have examined the topography of binding of C3b to PNH and normal erythrocytes. Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography, the a-chain of C3b was found to bind via predominantly ester bonds to free hydroxyl groups on glycophorin-a, the major erythrocyte sialoglycoprotein. The pattern of binding of nascent C3b was the same for normal and PNH erythrocytes. Thus, although C3b binding to a different membrane constituent did not appear to account for the greater enzymatic activity of the alternative pathway convertase when affixed to PNH erythrocytes, it seemed possible that the glycoproteins to which C3b bound might be qualitatively abnormal on the PNH cells, and that structural differences in these molecules might impose modifications in the enzyme-substrate interactions of the alternative pathway convertase. Using methods for radiolabeling both protein and carbohydrate residues, we therefore compared the electrophoretic pattern of the cellsurface glycoproteins on PNH and normal erythrocytes. The glycophorin-a dimer was found to be qualitatively abnormal on the PNH cells as evidenced by its greater susceptibility to trypsin-mediated proteolysis. In addition, the abnormal erythrocytes from patients with PNH had Parts of this work were presented to the

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The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein

Cited by 129 publications

References 22 publications

Glycoproteins of Platelet Membranes from Glanzmann's Thrombasthenia. A Comparison with Normal Using Carbohydrate-Specific or Protein-Specific Labelling Techniques and High-Resolution Two-Dimensional Gel Electrophoresis

Glycoproteins of Platelet Membranes from Glanzmann's Thrombasthenia. A Comparison with Normal Using Carbohydrate-Specific or Protein-Specific Labelling Techniques and High-Resolution Two-Dimensional Gel Electrophoresis

Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins.

Abnormality of glycophorin-alpha on paroxysmal nocturnal hemoglobinuria erythrocytes.

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