Disulfide bond requirements for assembly of the platelet glycoprotein Ib-binding domain of von Willebrand factor.
نویسندگان
چکیده
منابع مشابه
Thrombin decreases von Willebrand factor binding to platelet glycoprotein Ib.
Thrombin is a physiological agonist that promotes platelet aggregation and secretion. In this study we observed that thrombin can also inhibit a function of platelets related to primary hemostasis. Platelet stimulation by thrombin decreased the binding of von Willebrand factor (vWF) to glycoprotein (GP) Ib and decreased ristocetin-induced agglutination, in vitro reactions that correlate with in...
متن کاملPlasmin effect on platelet glycoprotein Ib-von Willebrand factor interactions.
We have studied the effect of streptokinase on platelets in platelet-rich plasma (PRP) and of plasmin on washed platelets. By three and one-half minutes after the addition of 50,000 IU/mL streptokinase to PRP, the maximum rate of ristocetin-induced platelet agglutination declined 40%, and by 60 minutes, it declined 70%. During the same time interval, the thrombin time increased from 20 seconds ...
متن کاملFibrin monomer induces binding of endogenous platelet von Willebrand factor to the glycocalicin portion of platelet glycoprotein IB.
This study demonstrates that when platelets are stimulated by thrombin in the presence of low concentrations of purified human fibrinogen (10 to 20 micrograms/mL, final concentration) binding of released platelet von Willebrand factor (plt-vWF) to the platelet membrane is enhanced. This effect appears to be mediated by fibrin monomer produced by the action of thrombin on the fibrinogen in the i...
متن کاملIdentification of discontinuous von Willebrand factor sequences involved in complex formation with botrocetin. A model for the regulation of von Willebrand factor binding to platelet glycoprotein Ib.
We have used proteolytic fragments and overlapping synthetic peptides to define the domain of von Willebrand factor (vWF) that forms a complex with botrocetin and modulates binding to platelet glycoprotein (GP) Ib. Both functions were inhibited by the dimeric 116-kDa tryptic fragment and by its constituent 52/48-kDa subunit, comprising residues 449-728 of mature vWF, but not by the dimeric frag...
متن کاملPlatelet adhesion to fibronectin in flow: the importance of von Willebrand factor and glycoprotein Ib.
We describe glycoprotein (GP) Ib as a mediator of adhesion to fibronectin, specifically in flow. A monoclonal antibody (MoAb) directed to the von Willebrand factor (vWF)-binding site on this receptor or the absence of this receptor on the platelet membrane, in the case of a patient with the Bernard-Soulier syndrome, reduced platelet coverage to fibronectin to approximately 30% of the control va...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)53847-3