1995 Fiscal Year Final Research Report Summary
Structure and function of ABO blood group antigens fond in human von Willebrand factor
| Project/Area Number |
06671118
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Hematology
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| Research Institution | Institute for Comprehensive Medical Science, Fujita Health University |
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Principal Investigator |
MATSUI Taei Inst.Comprehens.Med.Sci., Fujita Health University Research associate, 総合医科学研究所, 助手 (90183946)
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| Co-Investigator(Kenkyū-buntansha) |
TITANI Koiti Inst.Comprehens.Med.Sci., Fujita Health Unviersity Professor, 総合医科学研究所, 教授 (60179942)
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| Project Period (FY) |
1994 – 1995
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| Keywords | ABO Blood group / von Willebrand factor / FVIII Concentrate / Lectin / Protease / Bone marrow transplantation / PCR / Plasma glycoprotein |
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| Research Abstract |
We have found that human von Willebrand factor (vWF) has a unique characteristic of possessing covalently-linked ABO blood group antigens. We are interested in the physiological significance of these antigens in vWF.ABO blood group genotype in Japanese was determined by PCR and the relationship among the blood group genotype, plasma concentration and the ristocetin- and/or botrocetin-induced platelet agglutinating activity of vWF was surveyed. vWF concentration in plasma was only significantly lower in hetero (AO,BO) than homo (AA,BB), suggesting the presence of some correlation between the turnover ratio of vWF and the expression of H (O) substance on vWF.We surveyed blood group antigens in commercially available FVIII concentrates and found that only vWF and factor VIII shows antigenicity. We also found that IgM and IgG are associated with vWF,suggesting that naturally occurring antibodies against blood group antigen might be bound to vWF since these concentrates were prepared from pooled plasma. Plasma with each blood group may provide more efficient recovery of uniform vWF and FVIII.To isolate vWF of certain blood group from the concentrates, we examined several blood group specific lectins. HPA from Helix pomatia and UEA from Ulex europaeus recognized blood group A and H (O) substances in vWF,respectively. Other lectins were not sufficiently specific, though they show blood group specific hemagglutination. vWF rich in blood group A substance was separated from the FVIII concentrates by a HPA-agarose column. Using blood group specific vWF obtained by this lectin column, protease susceptibility of vWF is now being studied to elucidate the physiological funciton of blood group substances in vWF.Further, we are collecting data on the blood group expression of vWF in individuals with several blood group subtypes and with bone marrow transplantation between different blood groups.
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