| First Author | Nishizumi H | Year | 1997 |
| Journal | J Immunol | Volume | 158 |
| Issue | 5 | Pages | 2350-5 |
| PubMed ID | 9036984 | Mgi Jnum | J:110687 |
| Mgi Id | MGI:3640883 | Doi | 10.4049/jimmunol.158.5.2350 |
| Citation | Nishizumi H, et al. (1997) Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells. J Immunol 158(5):2350-5 |
| abstractText | Signaling through the high affinity IgE receptor (Fc epsilon RI) on mast cells and basophils results in rapid increases in tyrosine phosphorylation on a number of proteins. Fc epsilon RI associates with two classes of the tyrosine kinases, the Src family kinases, such as Lyn, c-Yes, and c-Src, and the Syk kinase. In this work, using primary mast cells derived from wild-type (lyn +/+) and lyn-deficient (lyn -/-) mice, we report that Lyn plays a part in signaling via Fc epsilon RI. Unlike lyn +/+ mast cells, cross-linking of Fc epsilon RI in lyn -/- mast cells failed to induce protein-tyrosine phosphorylation of various substrates, and evoked a delayed and slow Ca2+ mobilization. However, degranulation, adhesion, and production of cytokines occurred normally in lyn -/- mast cells. Our data suggest that the activity of the other Src family kinases, such as c-Src, can complement the role of Lyn in inducing most, but not all, biologic and biochemical responses to Fc epsilon RI cross-linking. |
