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β2 integrin‐dependent phosphorylation of protein‐tyrosine kinase Pyk2 stimulated by tumor necrosis factor α and fMLP in human neutrophils adherent to fibrinogen
Author(s) -
Yan Sen Rong,
Novak M.John
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00539-6
Subject(s) - tyrosine phosphorylation , microbiology and biotechnology , lyn , syk , ptk2 , phosphorylation , integrin , tyrosine kinase , chemistry , receptor tyrosine kinase , focal adhesion , cancer research , proto oncogene tyrosine protein kinase src , biology , signal transduction , protein kinase a , biochemistry , mitogen activated protein kinase kinase , receptor
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 β 2 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.