A sensitive and specific test was used to identify a platelet-agglutinating factor in sera from patients with thrombotic thrombocytopenic purpura. Serum from patients plus a preparation rich in large multimers of factor VIII: von Willebrand factor were added to target platelets, and agglutination occurred in 41 of 48 samples. Edetic acid, heparin, or heating, but not aspirin, monomeric IgG, or dansylarginine N-(3-ethyl-1,5-pentanediyl)amide inhibited the platelet-agglutinating factor. In-vitro agglutination requires the presence of a platelet-agglutinating factor and large multimers of von Willebrand factor. High concentrations of either component lowers the amount of the other required for platelet agglutination. Some patients may be more susceptible to the agglutinating factor because of a congenital or acquired abnormality in processing unusually large multimers of von Willebrand factor or because of infections or inflammatory disorders that lead to increased synthesis of large multimers of von Willebrand factor.
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http://dx.doi.org/10.7326/0003-4819-101-5-589 | DOI Listing |
J Thromb Haemost
March 2017
Department of Blood Transfusion Medicine, Nara Medical University, Kashihara, Japan.
Unlabelled: Essentials Botrocetin-2 (Bot2) binds to von Willebrand factor (VWF) and induces platelet agglutination. We identified Bot2 residues that are required for binding to VWF and glycoprotein (GP) Ib. We produced a mutant Bot2 that binds to VWF but inhibits platelet agglutination.
View Article and Find Full Text PDFToxicon
June 2005
Department of Biology, Fujita Health University School of Health Sciences, Toyoake, Aichi 470-1192, Japan.
Hemostatic plug formation is a complex event mediated by platelets, subendothelial matrices and von Willebrand factor (VWF) at the vascular injury. Snake venom proteins have an excellent potency to regulate the interaction between VWF and platelet membrane receptors in vitro. Two protein families, C-type lectin-like proteins and Zn(2+)-metalloproteinases, have been found to affect platelet-VWF interaction.
View Article and Find Full Text PDFBiochem J
March 2004
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei 11529, Taiwan.
Platelet glycoprotein Ib (GPIb)-binding proteins (GPIb-BPs) from snake venoms are usually C-type lectins, which target specific sites of GPIbalpha and elicit distinct effects on platelets. In the present paper, we report a tetrameric platelet-agglutinating factor (molecular mass 121.1 kDa), termed mucrocetin, purified from the venom of Taiwan habu (Trimeresurus mucrosquamatus ).
View Article and Find Full Text PDFJ Biochem Mol Biol
September 2002
Life Science Division, Lab of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology, Taejon, Korea.
Thrombotic thrombocytopenic purpura (TTP) is characterized by widespread platelet thrombi in arterioles and capillaries. Unusually large or multimeric von Willebrand factor, as well as one or more platelet-agglutinating factors, have been implicated in the pathogenesis of TTP. But, the actual mechanisms of platelet agglutination have not been satisfactorily explained.
View Article and Find Full Text PDFBiochem Mol Biol Int
June 1993
Division of Hematology/Oncology, Sylvester Cancer Center, University of Miami School of Medicine, Florida.
We have previously reported the purification of a 37 KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura and have shown that it is present in a subset of TTP patients, but absent in normal subjects. In this study, we would like to report some of the physico-chemical and immunological properties of this protein. The native molecular weight of PAP p37 from gel filtration was found to be 36,000, which is in agreement with denatured molecular weight (37,000), determined by SDS--polyacrylamide gel electrophoresis under both reducing and non-reducing conditions.
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