@entity22879 , but not @entity6438 , induces the priming of the NADPH oxidase activation in XXXX neutrophils.

@entity1 @entity20995 @entity1113 @entity57276 @entity72135 @entity72134 @entity6438 @entity224 @entity41543 @entity1521 @entity1366 @entity22879
Neutrophils play a key role in host defense against invading pathogens by releasing toxic agents, such as ROS and antimicrobial peptides. @entity1 neutrophils express several TLRs that recognize a variety of microbial motifs. The interaction between TLR and their agonists is believed to help neutrophils to recognize and to kill pathogens efficiently by increasing their activation, a process called priming. However, excessive activation can induce tissue injury and thereby, contribute to inflammatory disorders. Agonists that activate @entity6438 and @entity22879 induce priming of neutrophil ROS production; however, which receptor is involved in this process has not been elucidated. In this study, we show that the selective @entity22879 agonist, @entity72134 (3M002), induced a dramatic increase of fMLF-stimulated @entity1113 activation, whereas the selective @entity6438 agonist, @entity72135 , failed to induce any priming effect. Interestingly, @entity72134 , but not @entity72135 , induced the phosphorylation of the @entity1113 cytosolic component @entity20995 on several serines and the phosphorylation of p38MAPK and @entity1366 . The inhibitor of p38MAPK completely blocked @entity72134 -induced phosphorylation of @entity20995 Ser345. Moreover, @entity72134 , but not @entity72135 , induced the activation of the @entity1521 isomerase @entity41543 , and @entity57276 , a @entity41543 inhibitor, prevented @entity72134 -mediated priming of fMLF-induced @entity224 production. These results indicate that @entity22879 , but not @entity6438 , is involved in priming of @entity1 neutrophil ROS production by inducing the phosphorylation of @entity20995 and p38MAPK and that @entity41543 is also involved in this process.
