Factor VIII coagulant moiety binds to platelets by binding to phospholipids of the platelet membrane.

Abstract:

:Washed human platelets were incubated with commercial factor VIII concentrate, or with purified factor VIII coagulant moiety. Platelets were then washed again and lysed by sonication. VIII:Ag and vWf:Ag were measured in the platelet lysate prior to and after incubation of the lysate with phospholipase C (PL-C). Platelet bound VIII:Ag was significantly higher after incubation of washed platelets with factor VIII concentrate than after incubation with buffer. Platelet bound VIII:Ag was further increased when platelets had been incubated with concentrate in the presence of thrombin and collagen. In contrast, only a slight increase in platelet bound vWf:Ag was observed after incubation of platelets with concentrate. When washed platelets had been incubated with factor VIII coagulant moiety, also significantly more platelet bound VIII:Ag was observed than after incubation with buffer. Measurable VIII:Ag, but not vWf:Ag, increased significantly after incubation of the platelet lysate with PL-C. When intact washed platelets had been treated with PL-C prior to the incubation with concentrate, binding of VIII:Ag to platelets was nearly completely abolished. Our data suggest that the factor VIII coagulant moiety binds to phospholipids of the platelet membrane and thereby contributes to the assembly of the factor X activating complex on the platelet surface.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Muntean W,Leschnik B,Haas J

doi

10.1016/0049-3848(87)90223-4

subject

Has Abstract

pub_date

1987-02-15 00:00:00

pages

345-54

issue

4

eissn

0049-3848

issn

1879-2472

journal_volume

45

pub_type

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