Platelet membrane glycoprotein abnormalities in patients with myeloproliferative disorders and secondary thrombocytosis.
Carbohydrate-specific surface labelling and 125I-labelled lectin binding techniques, in combination with one- or two-dimensional (non-reduced/reduced) SDS-polyacrylamide gel electrophoresis have been used with platelets from patients with myeloproliferation disorders and secondary thrombocytosis and from healthy donors. In essential thrombocythaemia platelet membrane glycoproteins were significantly less sialylated than in normals (particularly GP Ib and IIIa). Increased binding of 125I-labelled Lens culinaris lectin to thrombospondin and GP IIIa indicated a defect in the glucose/mannose glycosylation of the platelet glycoproteins in essential thrombocythaemia. In polycythaemia vera and in chronic myeloid leukaemia the terminal sialic acid of glycoprotein IIIb was labelled slightly more than normal. In chronic myeloid leukaemia there was increased labelling of the penultimate galactose/N-acetylgalactosamine residues of GP Ib, IIb, IIIa and IIIb. In comparison to myeloproliferative disorders, platelets from patients with secondary thrombocytosis showed no significant changes, except for platelets from two patients with idiopathic thrombocytopenic purpura which showed an increased sialylation of all surface glycoproteins.
D001792:Blood Platelets / Q000378:metabolism*; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis*; D009196:Myeloproliferative Disorders / Q000378:metabolism*; D013922:Thrombocytosis / Q000378:metabolism
D006023:Glycoproteins; D008565:Membrane Proteins