期刊
JOURNAL OF IMMUNOLOGY
卷 182, 期 5, 页码 3233-3242出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.0802621
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资金
- National Natural Science Foundation of China [30570927, 30570929]
- National Basic Research Program of China [2005CB522404]
- Northeast Normal University's Scientific Innovation Project [NENU-STC 7011]
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.
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