[Morphologic and molecular aspects of the interaction of platelets with elements of the vascular wall].

The review presents and analyzes the data available on the structure and functions of adhesive proteins, Willebrand's factor, fibrinogen, thrombospondin, and fibronectin, their secretion and interaction with blood cells and subendothelial matrix in the focus of endothelial desquamation. A structural similarity of these modular glycoproteins, their domain structure-related functions, distinctive features of cellular reception are shown. The authors also consider structural changes in platelets in their activation, rearrangement of glycoprotein complexes IIb/IIIa on the membrane for binding adhesive proteins, role of these proteins in the organization of reversible and stabilized cellular aggregates and their location in the area of the damaged endothelium. The evidence is given for one of the most important mechanisms of limiting the platelet formation-activation system of C protein, which is mediated through thrombin binding to endothelial thrombomodulin. Hemostatic abnormalities occur with congenital defects in the structure of adhesive factors or their receptors while protein deficiency in the C protein system results in formation of thromboses.