Is Willebrand Factor Indicative of Chronic Inflammation in Children with Asthma?

Objective: To improve our knowledge and to understand how the level of von Willebrand factor indicates the development of chronic inflammation in children with recurrent wheezing and asthma.

Material And Methods: It was a prospective cohort study. This study was conducted in children with recurrent wheezing and asthma who were referred to a children's hospital during 2017-2018.

Binding of Coagulation Factor XIII Zymogen to Activated Platelet Subpopulations: Roles of Integrin αIIbβ3 and Fibrinogen.

Factor XIIIa (fXIIIa) is a transglutaminase that plays a crucial role in fibrin clot stabilization and regulation of fibrinolysis. It is known to bind to procoagulant platelets. In contrast, the zymogen fXIII interaction with platelets is not well characterized.

Interrelationship of endothelial function parameters in children with bronchial asthma in exacerbation and remission.

Introduction: In children with asthma, endothelial dysfunction signs are observed, and their extent depends on the severity of the disease. These changes are also present in remission. High level of soluble Vascular Cell Adhesion Molecule-1 (sVCAM-1) expression causes active adhesion of inflammatory cells and can indicate direct endothelium participation in development and supporting of chronic inflammation.

[The effect of "aging" of fibrinogen molecule on the structure and properties of fibrin gel].

The effect of molecular "aging" of fibrinogen stimulated by preincubation in solution on the fibrin three-dimensional architecture, its ability to crosslink fibrin-stabilizing factor, and the sensitivity of fibrin gel to plasmin hydrolysis have been studied. The method of elastic light scattering was used to demonstrate that fibrin generated from "defective" fibrinogen had a coarser structure with a higher mean mass-length ratio of polymeric fibers compared to native fibrinogen (2.24 x 10(9) and 1.

[Influence of end products of plasmin-mediated hydrolysis of fibrinogen and fibrin (EF and Ef fragments) on fibrinogen cross-linking].

We studied the influence of the end products of plasmin-mediated hydrolysis of fibrinogen and nonstabilized fibrin (EF and Ef fragments) on covalent cross-linking of fibrinogen molecules catalyzed by a fibrin-stabilizing factor (factor XIIIa). The data on elastic and dynamic light scattering reveal no difference in the spatial structure of covalently linked fibrinogen molecules in the presence of the hydrolysis end products EF and Ef. In contrast to the inactive fragment EF, fragment Ef significantly accelerates the enzymatic reaction.