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- W2102149451 abstract "Leukocyte-specific protein 1 (LSP1) is an intracellular, F-actinand Ca-binding, phosphoprotein expressed in leukocytes and endothelial cells (ECs). It is important in leukocyte motility and recruitment during inflammation. The role of LSP1 and its signaling mechanisms in chemokine-induced neutrophil transendothelial recruitment are not well understood. In this study, the role of neutrophil LSP1 (N-LSP1) and endothelial LSP1 (E-LSP1) in neutrophil-endothelial cell interactions in the post-capillary venules was investigated by using intravital microscopy and time-lapse video photography. This was determined in response to two very similar CXC chemokines keratinocyte-derived chemokine (KC, CXCL1) and macrophage inflammatory protein-2 (MIP-2, CXCL2). To induce neutrophil recruitment, one mm piece of agarose gel containing MIP-2 or KC was carefully placed on 350 μm from the observed post-capillary venule of the mouse cremaster muscle. Neutrophil intraluminal crawling, transmigration, and chemotaxis in the muscle were analyzed by the use of LSP1-deficient (Lsp1) mice, wild-type (WT) 129/SvJ mice and their four types of chimeric mice (Lsp1→Lsp1, WT→Lsp1, Lsp1→WT and WT→WT)*. We observed that Lsp1 mice exhibited similar responses to MIP-2 or KC-induced neutrophil recruitment compared to the WT mice. Emigration in neutrophil recruitment was significantly inhibited in Lsp1 mice. Neutrophils in Lsp1 mice, compared to those in the WT mice, displayed longer crawling time, slower crawling velocities and had lower chemotaxis index during their intraluminal crawling in venules in response to MIP-2. The transmigration time of Lsp1 neutrophils was longer than that of WT neutrophils, although LSP1 did not appear to play" @default.
- W2102149451 created "2016-06-24" @default.
- W2102149451 creator A5034503988 @default.
- W2102149451 date "2011-08-01" @default.
- W2102149451 modified "2023-09-28" @default.
- W2102149451 title "The role of LSP1 in chemokine-induced neutrophil recruitment" @default.
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