[THE EFFECTS OF LYS-PLASMINOGEN ON HUMAN PLATELET SECRETION].

The effects of Lys-plasminoge on platelet α-granule secretion were studied. The level of P-selectin exposed on the surface of plasma membranes of washed human platelets was measured by flow cytometry as a market of α-granule secretion. It was shown that Lys-plasminogen facilitates partial release of α-granules, but impedes thrombin-induced platelet exocytosis. It is suggested that Lys-plasminogen may affect platelet secretion rather through interaction of its non-catalytic (kringle) domains with membrane receptors than due to contaminating plasmin activity. In contrast to Lys-form, native proenzyme (Glu-plasminogen) had no effects on α-granule releasing. Here, we provide the first experimental demonstration that Lys-form of plasminogen is able to modulate platelet α-granule secretion, and this effect can be considered as one of the plausible mechanisms of its anti-aggregating activity.

[Role of plasminogen/plasmin in functional activity of blood cells].

The article deals with the data concerning structural peculiarities of plasminogen/plasmin molecule, which define the specificity of intermolecular interactions and provide the variety of its biological functions. The main principles of the modern classification of plasminogen receptors and factors, which modulate their expression, have been presented. We have considered the mechanisms regulating both plasmin formation and activity on the surface of cells, fibrin and proteins of extracellular matrix. The data of previous investigators and our own results, concerning the influence of plasminogen/plasmin on platelet aggregation induced by different agonists, have been summarized. The participation of plasminogen/plasmin in atherogenesis and angiogenesis mediated by endotheliocyte receptors has been discussed. Special attention was given to plasminogen/plasmin proinflammatory function, which is realized by regulatory processes of activation, secretion, migration and apoptosis of monocytes and macrophages.

[Interaction of adhesion proteins with structural components of cytoskeleton in animal cells]. / Vzaiemodiia bilkiv adheziï zi strukturnymy skladovymy tsytoskeleta tvarynnykh klityn.

The short characteristic of cell adhesion molecules and the main components of cytoskeleton are submitted at the present review. Structural and functional peculiarities of these proteins are presented. On the basis of different sources an attempt to clarify the possible mechanism of the interaction of adhesion proteins cytoskeleton structure has been done. It is suggested that information about adhesion contacts is transmitted from the adhesion proteins to cytoskeleton structures that induces the transformation of the letter ones and promotes the cellular metabolic response.

[Characteristics of various nerve tissue proteins using group-specific sorbents]. / Kharakteristika nekotorykh belkov nervnoi tkani s primeneniem gruppospetsifichnykh sorbentov.

The use of micro-scale column chromatography and affinity immunoelectrophoresis with group-specific sorbents allows studying some physical and chemical properties of protein molecules. A comparison of properties of soluble and membrane brain amino-peptidases carried out by means of micro-scale phenyl-sepharose and ConA-sepharose column chromatography shows that the membrane-bound aminopeptidase is a glycoprotein which possesses a high capacity to hydrophobic interactions. Soluble forms of aminopeptidase do not interact with ConA or phenyl residues. The crossed affinity immunoelectrophoresis in the presence of phenyl-sepharose also shows the presence of hydrophobic domains on the surface of glial fibrillary acidic protein molecules. The both approaches may be useful to predict conditions for large-scale affinity chromatography methods of protein and enzyme purification.