Tyrosine phosphorylation of pp125FAK by the aggregation of high affinity immunoglobulin E receptors requires cell adherence.
作者： M.M. Hamawy , S.E. Mergenhagen , R.P. Siraganian
DOI: 10.1016/S0021-9258(18)53114-8
关键词:
摘要: The aggregation of the high affinity IgE receptor (Fc epsilon RI) in adherent rat basophilic leukemia (RBL-2H3) cells induces tyrosine phosphorylation several proteins. We examined whether focal adhesion-associated kinase, pp125FAK, is one these Anti-pp125FAK monoclonal antibody immunoblotted and precipitated a 115-kDa tyrosine-phosphorylated protein. In absence Fc RI aggregation, pp125FAK was only cells. Aggregating markedly enhanced pp125FAK. This increase detectable within 1 min maximal by 15 min. contrast, nonadherent did not induce influx calcium ionophore or activation protein kinase C phorbol myristate acetate induced Thus, RI-induced could be mediated and/or induction influx. data indicate that cell adherence essential for
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