@entity556 modulates synthesis of plasminogen activator inhibitor type 2 by XXXX peripheral blood monocytes.

@entity1 @entity32 @entity527 @entity556 @entity2289 @entity10933 @entity2290
Fibrin deposition is characteristic of inflammatory diseases. The monocytes is central to the inflammatory response and can affect fibrinolysis by expression of urokinase ( @entity2290 ) and plasminogen activator inhibitor types 1 and 2 ( @entity2289 and @entity10933 , respectively). This study examines whether @entity556 , which promotes @entity527 , can contribute to fibrin persistence by modulating expression of proteins of the fibrinolytic system. Monocytes were isolated from @entity1 peripheral blood and analyzed for @entity10933 , @entity2289 , and @entity2290 antigens by enzyme-linked immunosorbent assay (ELISA). Monocytes responded to @entity556 by increased expression of @entity10933 in a dose- and time-dependent manner, with maximal synthesis at a concentration of 1 U/mL to 10 U/mL. This trend was also evident for @entity2289 , which was present at much lower levels. @entity556 and lipopolysaccharide (LPS) stimulated comparable levels of @entity10933 , studied at the antigen and mRNA level. The dose effet of LPS on @entity10933 and @entity2289 was found to differ from that of @entity556 . The level of @entity2290 was undetectable by ELISA and zymography in all samples. @entity556 stimulates @entity10933 synthesis by @entity1 monocytes, therefore creating an imbalance in the fibrinolytic system. This may contribute to persistence of fibrin, deposited during @entity32 .
