Conformational alterations within the glycocalyx of erythrocyte membranes studied by spin labelling.
The structure of the glycocalyx of the membrane of human erythrocytes and spectrin-depleted vesicles was studied under various conditions by two spin-labelling approaches: covalently labelling sialic acid residues of the glycocalyx and incorporation of a charged hydrophobic spin probe, CAT 16, being sensitive to alterations on the membrane surface into the lipid phase. Although cell electrophoretic measurements which were performed, additionally, indicated an erection of the glycocalyx upon decreasing the ionic strength of the suspension medium a more restricted mobility of spin-labelled sialic acid residues was found, in this case probably due to electrostatic interactions. The enhanced mobility of the spin probe CAT 16 at low ionic strength as well as in the case of neuraminidase-treated cells could be caused by reduced steric and electrostatic interaction with glycoproteins and glycolipids. La3+ adsorption and virus attachment on the human erythrocyte membrane were accompanied with a reduced mobility of sugar headgroups of the surface coat. No indication of cluster formation or lateral segregation of glycophorin molecules was found upon virus binding. After denaturation of the spectrin cytoskeleton of intact erythrocytes, increased mobility of spin-labelled sialic acid residues was observed.
D004578:Electron Spin Resonance Spectroscopy; D004903:Erythrocyte Aggregation; D004910:Erythrocyte Membrane / Q000032:analysis*; D006023:Glycoproteins; D006801:Humans; D007811:Lanthanum / Q000378:metabolism; D008433:Mathematics; D009994:Osmolar Concentration; D011134:Polysaccharides; D012794:Sialic Acids / Q000097:blood
D006023:Glycoproteins; D011134:Polysaccharides; D012794:Sialic Acids; D007811:Lanthanum