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Journal of Biochemistry Advance Access originally published online on July 13, 2006
Journal of Biochemistry 2006 140(2):229-235; doi:10.1093/jb/mvj149
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© 2006 The Japanese Biochemical Society.

Regular Paper

c-Abl Is Involved in the F-Actin Assembly Triggered by L-Selectin Crosslinking

Cuixia Chen, Xueqing Ba, Ting Xu, Lingling Cui, Shui Hao and Xianlu Zeng*

Institute of Genetics and Cytology, Northeast Normal University, Changchun 130024, P.R. China

* To whom correspondence should be addressed. Phone: +86-431-5099317, Fax: +86-431-568751, E-mail: zengx779{at}nenu.edu.cn

L-selectin is a cell adhesion molecule mediating the initial capture and subsequent rolling of leukocytes along the endothelial cells expressing L-selectin ligands. In addition to its action in adhesion, an intracellular signaling role for L-selectin has been recognized. Its cytoplasmic domain is involved in signal transduction following antibody crosslinking and in the regulation of receptor binding activity in response to intracellular signals. In this work, we demonstrated that L-selectin crosslinking led to F-actin polymerization and redistribution in human neutrophils. Using immuno-fluorescence microscopy, we observed that F-actin redistribution spatiotemporally related to the polarization of L-selectin. STI571, a specific inhibitor for cytoplasmic tyrosine kinase c-Abl, can inhibit F-actin polymerization and c-Abl redistribution in the activated neutrophils. Furthermore, we determined that c-Abl redistributed to the region where L-selectin polarized and associated with L-selectin in the activated neutrophils. The association between L-selectin and c-Abl was reduced by cytochalasin B. These results suggested that c-Abl was involved in the F-actin alteration triggered by L-selectin crosslinking in human neutrophils.


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