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Imaging of blood plasma coagulation and its propagation at surfaces.
J Biomed Mater Res A
June 2008
Department of Clinical Chemistry, Laboratory Medicine, University Hospital, SE-581 85 Linköping, Sweden.
A new method utilizing image capture and processing was developed for the analysis of blood plasma coagulation at surfaces. The coagulation was detected in a cuvette by time-lapse image capture of light scattering from the developing fibrin network. By image processing and computer analysis of the captured image data, both early detection of coagulation at the surface and the propagation phase of coagulation could be measured in the same experiment.
View Article and Find Full Text PDFPlatelet moesin interacts with PECAM-1 (CD31).
Platelets
June 2003
Department of Cardiology and Pneumology, Faculty of Medicine, University of Technology, Aachen, Germany.
Platelet activation results information of filopodia and cell spreading by extension of lamellae. Moesin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which localize in cell extensions like filopodia and function as cross-linkers between the actin cytoskeleton and the plasma membrane. Here we investigated whether the adhesion molecule PECAM-1 (CD31) is a membrane-binding partner for moesin in platelets.
View Article and Find Full Text PDFSpatiotemporal dynamics of contact activation factors of blood coagulation.
Biochim Biophys Acta
January 2002
Research Center for Hematology, Russian Academy of Medical Sciences, Novozykovskii proezd 4a, Moscow 125167, Russia.
A new in vitro model is proposed for studying the spatiotemporal distributions of activated clotting factors, in which clotting is activated in a thin layer of non-stirred plasma supplemented with a fluorogenic substrate and is monitored by fluorescence from its cleavage product. Analysis of the spatiotemporal dynamics of factor XIa and kallikrein in glass-activated human plasma provides evidence that both contact factors remain restricted to the glass surface and possibly a narrow boundary zone (<0.1 mm).
View Article and Find Full Text PDFAnnexin V binds to the actin-based cytoskeleton at the plasma membrane of activated platelets.
Exp Cell Res
August 1999
School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Immunocytochemical studies demonstrate that annexin V relocates to the plasma membranes of intact stimulated blood platelets. Anti-annexin V antibodies label the cytoplasmic side of the substrate-adherent plasma membrane of mechanically unroofed, glass-activated platelets and colocalize with actin. In addition, crosslinking experiments using detergent-solubilized membranes of activated platelets have identified an 85-kDa complex containing annexin V.
View Article and Find Full Text PDFA comparative study of recombinant hirudin and standard heparin in the Wessler model.
Thromb Res
October 1992
Laboratoire Thrombose Expérimentale, Faculté de Médecine, Paris, France.
The in vitro anticoagulant activity of recombinant desulphated hirudin (HBW 023) and its antithrombotic activity in a rabbit venous stasis model were assessed in comparison to unfractionated heparin (UH). The specific activity of r-hirudin in rabbit plasma is similar to that of unfractionated heparin on a weight basis when using the whole blood clotting time or APTT, while it was five times more potent according to the thrombin clotting time (TCT). Forty-eight (6x8) anaesthetized New Zealand male rabbits were randomized to receive HBW 023 (12.
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