Mutation in the @entity8236 Inhibitory Wedge Modulates Integrin Activation and Leukocyte Recruitment during XXXX .

@entity8236 @entity32 @entity19 @entity71721 @entity12213 @entity358 @entity1104 @entity3804 @entity669 @entity526
UNASSIGNED: Neutrophil recruitment to the site of @entity32 plays a pivotal role in host defense. Src family kinases (SFKs) activation is required for integrin and chemokine signaling as well as immune cell function. The receptor-like protein @entity669 phosphatase @entity8236 positively regulates chemoattractant signaling acting on SFK activity. To further investigate the role of @entity8236 in neutrophil recruitment and function, we analyzed @entity19 carrying a single point mutation (CD45 @entity71721 ), which constitutively activates @entity8236 . By using intravital microscopy experiments, we demonstrated that different steps of the leukocyte recruitment cascade were affected in CD45E613R mutant @entity19 . The rolling velocity of CD45 @entity71721 mutant neutrophils was decreased compared with wild-type neutrophils that subsequently resulted in an increased number of adherent cells. The analysis of b2 integrins @entity12213 and @entity3804 ( @entity3804 ) showed that in CD45 @entity71721 mutant neutrophils @entity12213 @entity1104 was impaired, and avidity was enhanced, whereas @entity3804 @entity1104 was increased. Because of the increased @entity3804 @entity1104 , neutrophil crawling was impaired in CD45E613R mutant compared with wild-type neutrophils. In an @entity526 @entity358 model, CD45E613R @entity19 displayed a decreased neutrophil recruitment into the alveolar compartment, which resulted in an increased number of CFUs in the lung. Our data demonstrate that the CD45 @entity71721 mutation modulates integrin activation and leukocyte recruitment during @entity32 .
