Protein‐tyrosine phosphorylations induced by concanavalin A and N‐formyl‐methionyl‐leucyl‐phenylalanine in human neutrophils

• DOI: 10.1111/j.1432-1033.1992.tb16998.x
• Publication Date: 2005-03-04T07:02:35Z
• Authors: Shinji OHTA; Tetsuya INAZU; Takanobu TANIGUCHI; Gizo NAKAGAWARA; Hirohei YAMAMURA
• Keywords: N-Formylmethionine leucyl-phenylalanine

The ability of the lectin concanavalin A (ConA) and N ‐formyl‐methionyl‐leucyl‐phenylalanine (fMLF) to induce protein‐tyrosine phosphorylation in human neutrophils was examined by immunoblot analysis. ConA caused an increase tyrosine protein bands with apparent molecular masses 120, 80, 76, 66 40 kDa; on other hand, fMLF those only 80‐kDa 40‐kDa proteins. These phosphorylations were time‐ dose‐dependent. induced suppressed but that not pertussis toxin pretreatment. At same time, pretreatment also inhibited lysozyme release aggregation did inhibit responses ConA. results suggest may be involved a part neutrophil activation regulated via pleiotropic signal transduction pathways. In addition, analysis employing antibodies against microtubule‐associated 2 (MAP2) kinase suggested this tyrosine‐phosphorylated might MAP2 kinase.