β2 integrin‐dependent phosphorylation of protein‐tyrosine kinase Pyk2 stimulated by tumor necrosis factor α and fMLP in human neutrophils adherent to fibrinogen

FEBS Letters

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