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Development, migration, and survival of mast cells
The factors that regulate mast cell development, migration, and survival are discussed including cytokines that are secreted from activated T cells and other immune cells including mast cells themselves.
Regulation of mast-cell and basophil function and survival by IgE
The binding of IgE to FcɛRI might influence mast-cell and basophil survival directly or indirectly, and can also regulate cellular function.
Evidence that IgE molecules mediate a spectrum of effects on mast cell survival and activation via aggregation of the FcεRI
We demonstrate that binding of different IgE molecules (IgEs) to their receptor, FcεRI, induces a spectrum of activation events in the absence of a specific antigen and provide evidence that such
The Src family kinase Hck regulates mast cell activation by suppressing an inhibitory Src family kinase Lyn.
A hierarchical regulation among SFK members to fine-tune mast cell activation is revealed and is revealed via both Lyn-dependent and Lyn-independent mechanisms.
Protein Kinase C βII Regulates Akt Phosphorylation on Ser-473 in a Cell Type- and Stimulus-specific Fashion*♦
Evidence is presented that conventional isoforms of protein kinase C (PKC), particularly PKCβII, can regulate Akt activity by directly phosphorylating Ser-473 in vitro and in IgE/antigen-stimulated mast cells.
The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C.
Evidence was obtained that Btk is physically associated with protein kinase C in intact murine mast cells as well, and depletion or inhibition of protein Kinase C with pharmacological agents resulted in an enhancement of the tyrosine phosphorylation of Btk induced by mast cell activation.
Mast Cell Survival and Activation by IgE in the Absence of Antigen: A Consideration of the Biologic Mechanisms and Relevance1
Recent findings of the heterogeneity of IgEs in their ability to induce survival and activation events, their mechanisms, the potential in vivo significance of IgE-FcεRI interactions, and the implications of the mouse studies to human diseases are synthesized.
Redundant and Opposing Functions of Two Tyrosine Kinases, Btk and Lyn, in Mast Cell Activation1
The data together demonstrate that Btk and Lyn are involved in mast cell signaling pathways in distinctly different ways, emphasizing that multiple signal outcomes must be evaluated to fully understand the functional interactions of individual signaling components.
PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling.
Inhibition of PKC-beta promoted cell death in B lymphomas characterized by exaggerated NF-kappa B activity, which is defined as an essential role for PKc-beta in BCR survival signaling and highlighted as a key therapeutic target for B-lineage malignancies.