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Published on: June 5, 2019
ABH antigens on human platelets: expression on the glycosyl phosphatidylinositol-anchored protein CD109
J G Kelton1, J W Smith, P Horsewood
1Department of Medicine, McMaster University, Hamilton, Ontario, Canada.
Platelets express alloantigens that are platelet specific (eg, the HPA antigens) and alloantigens that are shared with other blood cells (eg, the ABH antigens). The blood group A and B determinants are expressed on glycolipids and on some intrinsic platelet membrane glycoproteins. This report characterizes multiple platelet proteins reacting with blood group antibodies in serum samples from mothers of children born with neonatal alloimmune thrombocytopenia. ABH antigens on additional platelet proteins are identified, including the glycosyl phosphatidylinositol-anchored protein CD109. The proteins that carry ABH antigens were identified by using monoclonal antibodies to glycoproteins Ib, IIb/IIIa, Ia/IIa, CD31, and CD109 and immunoprecipitation/immunoblotting techniques with monoclonal antibodies to A and B antigens. The maternal serum samples and anti-A and anti-B monoclonal antibodies immunoprecipitated identical radiolabeled platelet proteins including proteins at 220 and 175 kd and proteins with mobilities corresponding to glycoproteins Ib, IIb/IIIa, IV, and V. Treatment of platelets with phosphatidylinositol-specific phospholipase C released into the supernatant a 175-kd protein that expressed the blood group determinants. This protein comigrated with the glycosyl phosphatidylinositol-anchored protein CD109. When platelet proteins were purified by immunoprecipitation with monoclonal antibodies and then tested by immunoblotting, anti-A reacted with the glycosyl phosphatidylinositol-anchored protein CD109 and to glycoproteins Ib, IIb, IIa, IIIa, and CD31 (PECAM). These results indicate that structures for modification by glycosyltransferases exist on platelet CD109, which also expresses the Gov alloantigen system. This study indicates that certain platelet proteins express both platelet-specific and blood group antigens that may contribute to platelet transfusion refractoriness and to neonatal alloimmune thrombocytopenia.
Platelets express alloantigens that are platelet specific (eg, the HPA antigens) and alloantigens that are shared with other blood cells (eg, the ABH antigens). The blood group A and B determinants are expressed on glycolipids and on some intrinsic platelet membrane glycoproteins. This report characterizes multiple platelet proteins reacting with blood group antibodies in serum samples from mothers of children born with neonatal alloimmune thrombocytopenia. ABH antigens on additional platelet proteins are identified, including the glycosyl phosphatidylinositol-anchored protein CD109. The proteins that carry ABH antigens were identified by using monoclonal antibodies to glycoproteins Ib, IIb/IIIa, Ia/IIa, CD31, and CD109 and immunoprecipitation/immunoblotting techniques with monoclonal antibodies to A and B antigens. The maternal serum samples and anti-A and anti-B monoclonal antibodies immunoprecipitated identical radiolabeled platelet proteins including proteins at 220 and 175 kd and proteins with mobilities corresponding to glycoproteins Ib, IIb/IIIa, IV, and V. Treatment of platelets with phosphatidylinositol-specific phospholipase C released into the supernatant a 175-kd protein that expressed the blood group determinants. This protein comigrated with the glycosyl phosphatidylinositol-anchored protein CD109. When platelet proteins were purified by immunoprecipitation with monoclonal antibodies and then tested by immunoblotting, anti-A reacted with the glycosyl phosphatidylinositol-anchored protein CD109 and to glycoproteins Ib, IIb, IIa, IIIa, and CD31 (PECAM). These results indicate that structures for modification by glycosyltransferases exist on platelet CD109, which also expresses the Gov alloantigen system. This study indicates that certain platelet proteins express both platelet-specific and blood group antigens that may contribute to platelet transfusion refractoriness and to neonatal alloimmune thrombocytopenia.
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