ABSTRACT
In this study, we have found a reduced binding of monoclonal antibodies (CD42b and CD41a) to glycoproteins Ib and IIb/IIIa of uremic platelets. Presumably, this was due to the altered structure of the sugary part of these glycoproteins. Change in the glycoprotein composition may have effected the disturbed adhesion and aggregation of uremic platelets.
Subject(s)
Antibodies, Monoclonal/metabolism , Platelet Glycoprotein GPIIb-IIIa Complex/chemistry , Platelet Glycoprotein GPIb-IX Complex/chemistry , Uremia/metabolism , Adult , Antibodies, Monoclonal/immunology , Blood Platelets/metabolism , Humans , Middle Aged , Oligosaccharides/chemistry , Platelet Glycoprotein GPIIb-IIIa Complex/immunology , Platelet Glycoprotein GPIIb-IIIa Complex/metabolism , Platelet Glycoprotein GPIb-IX Complex/immunology , Platelet Glycoprotein GPIb-IX Complex/metabolism , Protein Binding , Renal DialysisABSTRACT
In the study, platelet count and volume, granulocyte number, binding of monoclonal antibodies to platelet glycoproteins Ib and IIb/IIIa were evaluated in hemodialyzed patients. Exclusively, the granulocyte count dropped significantly at 15 minutes after the initiation of dialysis as compared to predialysis samples. It seems that contemporary used cuprophane dialyzer membrane is more biocompatibile and does not have major impact on platelets.
