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(Journal of Leukocyte Biology. 2001;69:497-504.)
© 2001 by Society for Leukocyte Biology

Leukocyte-specific gene 1 protein (LSP1) is involved in chemokine KC-activated cytoskeletal reorganization in murine neutrophils in vitro

Michael Hannigan, Lijun Zhan, Youxi Ai and Chi-Kuang Huang

Department of Pathology, University of Connecticut Health Center, Farmington

Correspondence: Michael Hannigan, Department of Pathology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030-3105. E-mail: michaelhanniga{at}snet.net

Leukocyte-specific gene 1 protein (LSP1) is a cytoskeletal-associated protein of leukocytes that in vitro cross-links F-actin into extensively branched bundles of mixed polarity. In this study, we examined chemotaxis and superoxide production in neutrophils prepared from wild-type (WT) and Lsp1 knockout mice. Compared to WT neutrophils, Lsp1-/- neutrophils showed impairment in both migration speed and chemotaxis direction during chemokine KC-directed chemotaxis. When examined by confocal microscopy, chemotaxing Lsp1-/- neutrophils showed abnormal morphologies. They had discontinuous primary actin-rich cortexes and large membrane protrusions. When stimulated by phorbol 12-myristate 13-acetate (PMA), Lsp1-/- peritoneal neutrophils produce more superoxide than WT. The data presented suggest that LSP1 plays important roles in the regulation of neutrophil morphology, motility, and superoxide production.

Key Words: neutrophil • activation • knockout mice




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