How sensitive may cytochemical methods detect alterations of the glycocalyx?
This review reports on the relationship of light and electron microscopic cytochemical staining and chemo-affinity labelling to the conformational state of the human erythrocyte glycocalyx glycophorin. According to a recent suggestion, primary glycophorin conformation is associated with binding to the lipid bilayer of this glycoprotein's N-terminal segment. Pretreatment of cells prior to fixation may cause this segment of detach from the lipid lamella and to acquire a less orientation. Alterations of the glycocalyx were sensitively demonstrated by topo-optical staining and by the labelling of unmasked binding sites.
D000954:Antigens, Surface / Q000032:analysis; D003102:Colloids; D004910:Erythrocyte Membrane / Q000032:analysis*; D004912:Erythrocytes / Q000032:analysis*; D006021:Glycophorins / Q000032:analysis; D006651:Histocytochemistry / Q000379:methods*; D006801:Humans; D007501:Iron; D037102:Lectins; D011487:Protein Conformation; D011955:Receptors, Drug / Q000032:analysis; D012430:Ruthenium Red; D012795:Sialoglycoproteins / Q000032:analysis; D014048:Tolonium Chloride
D000954:Antigens, Surface; D003102:Colloids; D006021:Glycophorins; D037102:Lectins; D011955:Receptors, Drug; D012795:Sialoglycoproteins; D012430:Ruthenium Red; D014048:Tolonium Chloride; D007501:Iron