Antithrombotics by L. Leblond, P. D. Winocour (auth.), Andrew C. G. Uprichard

By L. Leblond, P. D. Winocour (auth.), Andrew C. G. Uprichard M.D., Kim P. Gallagher Ph.D. (eds.)

An up to date review of blood coagulation, hemostatis, and thrombosis, this quantity additionally offers a cutting-edge record of present anti-thrombotic and anti-coagulant innovations in addition to a precis of present examine curiosity within the sector and power destiny objectives. It makes an attempt to stability conventional pharmacology with the more moderen sciences of molecular biology and in so doing, units a framework for destiny advances within the box. The e-book is a concise, present and invaluable reference for the fundamental researcher in addition to the working towards healthcare professional operating within the fields of cardiology, inner drugs or surgery.

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Hirudin complexes with thrombin by apolar interactions with regions adjacent to thrombin's catalytic site and by interactions with the anion-binding exosite (TULINSKY 1996). The bivalent nature of the hirudin-thrombin interaction has led to the design of hirulog and a hirulog-like class of thrombin inhibitors (FENTON 1992). These molecules literally form a bridge between the active site and the fibrinogen exosite and show effective inhibition in the nano- to picomolar range (MARAGANORE et al. 1990; TSUDA et al.

Nature 380:41-46 Bar-Shavit R, Eldor A, Vlodavsky I (1989) Binding of thrombin to subendothelial extracellular matrix. Protection and expression of functional properties. J Clin Invest 84: 1096-11 04 Beijering RJR, ten Cate H, ten Cate JW (1996) Clinical applications of new anti thrombotic agents. Ann Hematol 72:177-183 Berg DT, Wiley MR, Grinnell BW (1996) Enhanced protein C activation and inhibition of fibrinogen cleavage by a thrombin modulator. Science 273:1389-1391 Bernatowicz MS, Klimas CE, Hart KS, Peluso M, Allegretto NJ, Seiler SM (1996) Development of potent thrombin receptor antagonist peptides.

Platelets adhere to the altered vascular tissue at the site of injury, then aggregate and form a plug that stops blood loss. Platelet adhesion is mediated by the plasma protein, von Willebrand factor (vWf) , that forms a bridge between specific glycoprotein receptors (GpIb/GpIX) located on activated platelets and on the subendothelium (SAKARIASSEN et al. 1979). Conformational changes within the vWf molecule induced by shear stress forces in flowing blood appear to be responsible for regulating vWf affinity for GpIb (for review see KROLL et al.

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