c-Abl Kinase Is Required for β2 Integrin-Mediated Neutrophil Adhesion

被引:22
作者
Cui, Lingling [1 ]
Chen, Cuixia [1 ,2 ]
Xu, Ting [1 ]
Zhang, Juechao [1 ]
Shang, Xin [1 ]
Luo, Jixian [1 ]
Chen, Liang [1 ]
Ba, Xueqing [1 ]
Zeng, Xianlu [1 ]
机构
[1] NE Normal Univ, Inst Cytol & Genet, Changchun 130024, Peoples R China
[2] China Univ Petr E China, Ctr Bioengn & Biotechnol, Qingdao, Peoples R China
基金
中国国家自然科学基金;
关键词
SRC FAMILY KINASES; TYROSINE KINASE; F-ACTIN; PHOSPHORYLATION; ACTIVATION; TALIN; SYK; MECHANISMS; ENGAGEMENT; GENERATION;
D O I
10.4049/jimmunol.0802621
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Integrin regulation in neutrophil adhesion is essential for innate immune response. c-Abl kinase is a nonreceptor tyrosine kinase and is critical for signaling transduction from various receptors in leukocytes. Using neutrophils find dHL-60 (neutrophil-like differentiation of HL-60) cells, we show that c-Abl kinase is activated by beta(2) integrin engagement and is required for beta(2) integrin-dependent neutrophil sustained adhesion and spreading. The expression of beta(2) integrin on neutrophils induced by TNF-alpha is not affected by c-Abl kinase inhibitor STI571, suggesting that c-Abl kinase is not involved in TNF-alpha-induced integrin activation. The recruitment of c-Abl kinase to beta(2) integrin is dependent on talin head domain, which constitutively interacts with beta(2) integrin cytoplasmic domain. After activated, c-Abl kinase increases the tyrosine phosphorylation of Vav. The SH3 domain of c-Ahl kinase is involved in its interaction with talin and Vav. Thus, c-Abl kinase plays an essential role in the activation of Vav induced by beta(2), integrin ligation and in regulating neutrophil-sustained adhesion and spreading. The Journal of Immunology, 2009, 182: 3233-3242.
引用
收藏
页码:3233 / 3242
页数:10
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