FEBS Letters | |
β2 integrin‐dependent phosphorylation of protein‐tyrosine kinase Pyk2 stimulated by tumor necrosis factor α and fMLP in human neutrophils adherent to fibrinogen | |
Yan, Sen Rong1  Novak, M.John1  | |
[1] Department of Periodontics, University of Pittsburgh School of Dental Medicine, Pittsburgh, PA 15206, USA | |
关键词: Neutrophil; Protein-tyrosine kinase; Integrin; Cytoskeleton; Signal transduction; Focal adhesion; | |
DOI : 10.1016/S0014-5793(99)00539-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Tumor necrosis factor α and fMLP can activate a broad range of cellular functions in neutrophils adherent to biological surfaces. These functions are mediated by integrins and involve the activation of tyrosine kinases. Here, we report that Pyk2, a member of the focal adhesion kinase family, was present in human neutrophils and was rapidly phosphorylated and activated following tumor necrosis factor α and fMLP stimulation in an adhesion-dependent manner. Tyrosine phosphorylation of Pyk2 was attenuated by β2 integrin blocking with specific antibodies. The tyrosine phosphorylation of Pyk2 was downstream of protein kinases Lyn, Syk and protein kinase C and cytoskeletal organization. The activation of Pyk2 may play a role in adhesion/cytoskeleton-associated neutrophils function.
【 授权许可】
Unknown
【 预 览 】
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RO201912020307688ZK.pdf | 255KB | download |