XXXX : a novel protein that induced platelets active and aggregation via @entity2939 , NF-kB and @entity6708 dependent mechanisms.

@entity6708 @entity32 @entity518 @entity556 @entity1423 @entity39 @entity2939 @entity1427 @entity715
BACKGROUND: @entity715 are a group of prevalent and life-threatening diseases. Selective inhibition of pathological @entity715 holds the key to treat variety of @entity715 . The pathological @entity715 can be induced by either tissue @entity39 and deregulated @entity32 . @entity518 , as an important proinflammatory cytokine and a late mediator, also involves on @entity715 disease. However, the underlying mechanisms are not fully understood. METHODS: Immunofluorescence, ELISA assay, Platelet Aggregation, Thromboelastogram (TEG) analyzes. Flow cytometric analysis and Western blot analysis were used to investigated the role of @entity518 in @entity1423 and obtained following observations. RESULTS: By doing so, we obtained the following observations: i) Highly purified @entity518 recombinant protein induces @entity1423 and secretion in a dose-dependent manner in the presence of serum. ii) Low concentration of extracellular @entity518 could synergistically promote subthreshold concentration of collagen or @entity556 induced @entity1423 . iii) Extracellular @entity518 promoted @entity1423 in a platelet-expressed @entity1427 /IIIa-dependent manner. iv) We proposed that extracellular @entity518 seems to promote the phosphorylation of @entity1427 /IIIa and subsequent @entity1423 via @entity2939 /NF-kB and @entity6708 pathway. CONCLUSIONS: In this study, we provide evidence for the hypothesis that @entity518 interact with platelet might play an important role in the haemostasis and @entity715 . Our research might be provide an interesting avenue for the treatment of @entity715 in the future.
