World Congress on Medical Physics and Biomedical Engineering
会议日期
MAY 26-31, 2012
会议地点
Beijing, China
摘要
LFA-1 and Mac-1, two β2 integrin members constitutively expressed on neutrophils, mediate leukocyte recruitment cascade by binding to the same ligand of ICAM-1. The slow rolling and firm adhesion of leukocytes rely on LFA-1 while the cell crawling is dependent on Mac-1. We hypothesized that their distinct roles are likely attributed to the differences in the binding kinetics or in the diverse responses of outside-in and inside-out signaling. In this study, we compared the ICAM-1 binding features between soluble or membrane-expressed LFA-1 and Mac-1 with different affinity conformation using optical trap technique. Our data indicated that the affinity up-regulation from wide type (WT) to high affinity (HA) is off-rate dependent for LFA-1 but on-rate dependent for Mac-1. The structural bases of this new finding were found to be consistent with our previous simulations. These results furthered our understanding in their function differences under shear flow.
Li N,Mao DB,Gong YX,et al. Distinct kinetics features of LFA-1 and Mac-1 in neutrophil activation[C]World Congress on Medical Physics and Biomedical Engineering,2013:139-142.
; Mao DB(毛德斌)
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